CatLogenzyme kinetics catalog

EC 3.5.2.6: beta-lactamase

HydrolasesOpen in Browse

CatLog read 2,683 records for EC 3.5.2.6 from 131 papers, for 47 organisms. Names in these papers: metallo-β-lactamase L1, class C beta-lactamase (cephalosporinase), CphA metallo-beta-lactamase, BcII metallo-beta-lactamase (Zn2+-beta-lactamase II) and 146 more.

Read from the paper by an AI model and checked against the paper by a second, separate AI run; code converted the units.

CatLog also holds 716 records for EC 3.5.2.6 that are not yet re-read: from its earlier version, built from the enzyme databases and partly checked against the papers. All records for EC 3.5.2.6 in Browse.

Papers

PaperOrganismsRecords
Catalytic mechanism of active-site serine beta-lactamases: role of the conserved hydroxy group of the Lys-Thr(Ser)-Gly triadEscherichia coli93
Biochemical and structural analyses of metallo-β-lactamase VIM-28: impact of substitutions at residues 224 and 228 on substrate profile, stability, and zinc affinityPseudomonas aeruginosa90
Probing substrate binding to metallo-beta-lactamase L1 from Stenotrophomonas maltophilia by using site-directed mutagenesisStenotrophomonas maltophilia89
Mutational analysis of the two zinc-binding sites of the Bacillus cereus 569/H/9 metallo-beta-lactamaseBacillus cereus86
A survey of the kinetic parameters of class C beta-lactamases. Cephalosporins and other beta-lactam compoundsCitrobacter freundii, Enterobacter cloacae and 3 more84
Probing the specificity of the subclass B3 FEZ-1 metallo-beta-lactamase by site-directed mutagenesisFluoribacter gormanii70
Characterization of four beta-lactamases produced by Staphylococcus aureusStaphylococcus aureus67
Critical role of tryptophan 154 for the activity and stability of class D beta-lactamasesPseudomonas aeruginosa59
Biochemical characterization of New Delhi metallo-β-lactamase variants reveals differences in protein stability—56
Mutational analysis of the zinc- and substrate-binding sites in the CphA metallo-beta-lactamase from Aeromonas hydrophilaAeromonas hydrophila55
Kinetic properties of four plasmid-mediated AmpC beta-lactamases—53
The role of lysine-234 in beta-lactamase catalysis probed by site-directed mutagenesisBacillus licheniformis48
Effects on substrate profile by mutational substitutions at positions 164 and 179 of the class A TEM(pUC19) beta-lactamase from Escherichia coliEscherichia coli45
Role of residues 104, 164, 166, 238 and 240 in the substrate profile of PER-1 beta-lactamase hydrolysing third-generation cephalosporinsPseudomonas aeruginosa44
An overview of the kinetic parameters of class B beta-lactamasesAeromonas hydrophila, Bacillus cereus and 1 more43
Dramatic broadening of the substrate profile of the Aeromonas hydrophila CphA metallo-beta-lactamase by site-directed mutagenesisAeromonas hydrophila42
Analysis of the importance of the metallo-beta-lactamase active site loop in substrate binding and catalysisBacillus cereus, Pseudomonas aeruginosa36
Effect of an amino acid insertion into the omega loop region of a class C beta-lactamase on its substrate specificityEnterobacter cloacae35
The role of OXA-1 beta-lactamase Asp(66) in the stabilization of the active-site carbamate group and in substrate turnover—31
Characterization of the active-site residues asparagine 167 and lysine 161 of the IMP-1 metallo beta-lactamaseKlebsiella pneumoniae30
Cephalosporin substrate specificity determinants of TEM-1 beta-lactamaseEscherichia coli30
Overexpression, purification, and characterization of the cloned metallo-beta-lactamase L1 from Stenotrophomonas maltophiliaStenotrophomonas maltophilia29
TEM-89 beta-lactamase produced by a Proteus mirabilis clinical isolate: new complex mutant (CMT 3) with mutations in both TEM-59 (IRT-17) and TEM-3Proteus mirabilis28
Characterization of cell-bound papain-soluble beta-lactamases in BRO-1 and BRO-2 producing strains of Moraxella (Branhamella) catarrhalis and Moraxella nonliquefaciensMoraxella catarrhalis28
TEM-109 (CMT-5), a natural complex mutant of TEM-1 beta-lactamase combining the amino acid substitutions of TEM-6 and TEM-33 (IRT-5)Escherichia coli28
Site-directed mutagenesis of beta-lactamase I. Single and double mutants of Glu-166 and Lys-73Bacillus cereus28
Role of Ser-238 and Lys-240 in the hydrolysis of third-generation cephalosporins by SHV-type beta-lactamases probed by site-directed mutagenesis and three-dimensional modeling—28
High tolerance to simultaneous active-site mutations in TEM-1 beta-lactamase: Distinct mutational paths provide more generalized beta-lactam recognitionEscherichia coli27
Diverse evolutionary trajectories of Klebsiella pneumoniae carbapenemase: unraveling the impact of amino acid substitutions on β-lactam susceptibility and the role of avibactam in…Klebsiella pneumoniae27
Role of the Ser-287-Asn replacement in the hydrolysis spectrum extension of AmpC beta-lactamases in Escherichia coliEscherichia coli26
Kinetic properties and metal content of the metallo-beta-lactamase CcrA harboring selective amino acid substitutionsBacteroides fragilis24
Probing the dynamics of a mobile loop above the active site of L1, a metallo-beta-lactamase from Stenotrophomonas maltophilia, via site-directed mutagenesis and stopped-flow fluorescence…Stenotrophomonas maltophilia24
Biochemical characterization of metallo-beta-lactamase VIM-11 from a Pseudomonas aeruginosa clinical strainPseudomonas aeruginosa24
Citrobacter diversus ULA-27 beta-lactamases. Improved purification and general propertiesCitrobacter diversus24
Recombinant expression and characterization of the major beta-lactamase of Mycobacterium tuberculosisMycobacterium tuberculosis24
Metal binding Asp-120 in metallo-beta-lactamase L1 from Stenotrophomonas maltophilia plays a crucial role in catalysisStenotrophomonas maltophilia23
CMT-type beta-lactamase TEM-125, an emerging problem for extended-spectrum beta-lactamase detectionEscherichia coli23
Functional characterization of OXA-57, a class D beta-lactamase from Burkholderia pseudomalleiBurkholderia pseudomallei22
Role of Asp104 in the SHV beta-lactamaseKlebsiella pneumoniae21
Kinetic characterization of VIM-7, a divergent member of the VIM metallo-beta-lactamase familyPseudomonas aeruginosa21
Crystal structure of extended-spectrum beta-lactamase Toho-1: insights into the molecular mechanism for catalytic reaction and substrate specificity expansionEscherichia coli20
Asp-120 locates Zn2 for optimal metallo-beta-lactamase activityBacillus cereus20
Characterization of the new metallo-beta-lactamase VIM-13 and its integron-borne gene from a Pseudomonas aeruginosa clinical isolate in SpainPseudomonas aeruginosa20
Reduced catalytic activity of KPC β-lactamase can increase ceftazidime resistanceKlebsiella pneumoniae20
Site-directed mutagenesis of beta-lactamase I: role of Glu-166Bacillus cereus20
Characterization and amino acid sequence analysis of a new oxyimino cephalosporin-hydrolyzing class A beta-lactamase from Serratia fonticola CUVSerratia fonticola20
Class C beta-lactamases operate at the diffusion limit for turnover of their preferred cephalosporin substratesEnterobacter cloacae19
Biochemical and molecular characterization of three new variants of AmpC beta-lactamases from Morganella morganiiMorganella morganii19
E240V substitution increases catalytic efficiency toward ceftazidime in a new natural TEM-type extended-spectrum beta-lactamase, TEM-149, from Enterobacter aerogenes and Serratia marcescens clinical…—18
Structure and mechanism of copper- and nickel-substituted analogues of metallo-beta-lactamase L1Stenotrophomonas maltophilia18
Glutamate residues at positions 162 and 164 influence the beta-lactamase activity of SHV-14 obtained from Klebsiella pneumoniaeKlebsiella pneumoniae18
Properties of a class C beta-lactamase from Serratia marcescensSerratia marcescens18
Probing the role of Asp-120(81) of metallo-beta-lactamase (IMP-1) by site-directed mutagenesis, kinetic studies, and X-ray crystallographySerratia marcescens17
Irreversible inhibition of the Mycobacterium tuberculosis beta-lactamase by clavulanateMycobacterium tuberculosis17
Purification and properties of thiol beta-lactamase. A mutant of pBR322 beta-lactamase in which the active site serine has been replaced with cysteineEscherichia coli17
Biochemical characterization of laboratory mutants of extended-spectrum beta-lactamase TEM-60Providencia stuartii16
Molecular and kinetic comparison of the novel extended-spectrum beta-lactamases CTX-M-25 and CTX-M-26Escherichia coli, Klebsiella pneumoniae16
Biochemical characterisation of the CTX-M-14 beta-lactamaseEscherichia coli16
Resistance development in KPC-producing Klebsiella pneumoniae under ceftazidime/avibactam-meropenem pressure: KPC-2 Ω-loop mutations attenuate avibactam efficacyKlebsiella pneumoniae16
A kinetic study of NMC-A beta-lactamase, an Ambler class A carbapenemase also hydrolyzing cephamycinsEnterobacter cloacae16
Molecular characterization of a beta-lactamase gene, blaGIM-1, encoding a new subclass of metallo-beta-lactamasePseudomonas aeruginosa15
Probing active site chemistry in SHV beta-lactamase variants at Ambler position 244. Understanding unique properties of inhibitor resistanceKlebsiella pneumoniae15
Approaches to the simultaneous inactivation of metallo- and serine-beta-lactamasesEnterobacter cloacae15
Genetic and biochemical characterization of TRU-1, the endogenous class C beta-lactamase from Aeromonas enteropelogenesAeromonas enteropelogenes15
Substrate selectivity and a novel role in inhibitor discrimination by residue 237 in the KPC-2 beta-lactamaseKlebsiella pneumoniae15
Genetic context and biochemical characterization of the IMP-18 metallo-beta-lactamase identified in a Pseudomonas aeruginosa isolate from the United StatesPseudomonas aeruginosa15
Inhibitor-sensitive AmpC beta-lactamase variant produced by an Escherichia coli clinical isolate resistant to oxyiminocephalosporins and cephamycinsEscherichia coli14
Structure-function studies of arginine at position 276 in CTX-M beta-lactamases—14
Structural and biochemical evidence that a TEM-1 beta-lactamase N170G active site mutant acts via substrate-assisted catalysis—14
A Tyrosine Residue Along with a Glutamic Acid of the Omega-Like Loop Governs the Beta-Lactamase Activity of MSMEG_4455 in Mycobacterium smegmatisMycobacterium smegmatis14
Non-active site mutation (Q123A) in New Delhi metallo-β-lactamase (NDM-1) enhanced its enzyme activityKlebsiella pneumoniae14
Cefepime-taniborbactam and ceftibuten-ledaborbactam maintain activity against KPC variants that lead to ceftazidime-avibactam resistanceKlebsiella pneumoniae14
Ceftazidime and aztreonam resistance in Providencia stuartii: characterization of a natural TEM-derived extended-spectrum beta-lactamase, TEM-60Providencia stuartii14
Crystal structure of the OXA-48 beta-lactamase reveals mechanistic diversity among class D carbapenemasesKlebsiella pneumoniae13
Properties and distribution of a metallo-β-lactamase (ALI-1) from the fish pathogen Aliivibrio salmonicida LFI1238Aliivibrio salmonicida13
IMP-12, a new plasmid-encoded metallo-beta-lactamase from a Pseudomonas putida clinical isolatePseudomonas putida12
Genetic and biochemical characterization of a chromosome-encoded carbapenem-hydrolyzing ambler class D beta-lactamase from Shewanella algaeShewanella algae12
Site-saturation mutagenesis of Tyr-105 reveals its importance in substrate stabilization and discrimination in TEM-1 beta-lactamaseEscherichia coli12
BEL-1, a novel clavulanic acid-inhibited extended-spectrum beta-lactamase, and the class 1 integron In120 in Pseudomonas aeruginosaPseudomonas aeruginosa12
Characterisation of KLUA-9, a beta-lactamase from extended-spectrum cephalosporin-susceptible Kluyvera ascorbata, and genetic organisation of bla(KLUA-9)Kluyvera ascorbata12
Functional diversity among metallo-beta-lactamases: characterization of the CAR-1 enzyme of Erwinia carotovoraErwinia carotovora subsp. atroseptica12
Naturally occurring Class A ss-lactamases from the Burkholderia cepacia complexBurkholderia cenocepacia12
The role of a second-shell residue in modifying substrate and inhibitor interactions in the SHV beta-lactamase: a study of ambler position Asn276—12
Purification and biochemical characterization of IMP-13 metallo-beta-lactamasePseudomonas aeruginosa12
Biochemical characterization of the POM-1 metallo-β-lactamase from Pseudomonas otitidisPseudomonas otitidis12
High-yield expression, purification, and characterization of active, soluble Bacteroides fragilis metallo-beta-lactamase, CcrABacteroides fragilis12
Kinetic analysis of an inhibitor-resistant variant of the OHIO-1 beta-lactamase, an SHV-family class A enzyme—12
Kinetics study of KPC-3, a plasmid-encoded class A carbapenem-hydrolyzing beta-lactamaseEscherichia coli11
Molecular and biochemical characterization of the chromosome-encoded class A beta-lactamase BCL-1 from Bacillus clausiiBacillus clausii11
Serendipitous discovery of α-hydroxyalkyl esters as β-lactamase substratesEnterobacter cloacae11
Amino acid sequence determinants of extended spectrum cephalosporin hydrolysis by the class C P99 beta-lactamaseEnterobacter cloacae10
Characterization of a new extended-spectrum beta-lactamase (TEM-87) isolated in Proteus mirabilis during an Italian surveyProteus mirabilis10
Characterization of the naturally occurring oxacillinase of Acinetobacter baumanniiAcinetobacter baumannii10
Close amino acid sequence relationship between the new plasmid-mediated extended-spectrum beta-lactamase MEN-1 and chromosomally encoded enzymes of Klebsiella oxytocaEscherichia coli10
Biochemical characterization of SHV-55, an extended-spectrum class A beta-lactamase from Klebsiella pneumoniaeKlebsiella pneumoniae10
Characterization of RASA-1, a novel class A extended-spectrum beta-lactamase from Riemerella anatipestiferRiemerella anatipestifer10
Contrasting pH optima of β-lactamases CTX-M and CMY influence Escherichia coli fitness and resistance ecologyEscherichia coli10
KHM-1, a novel plasmid-mediated metallo-beta-lactamase from a Citrobacter freundii clinical isolateCitrobacter freundii9
Molecular and biochemical characterization of the natural chromosome-encoded class A beta-lactamase from Pseudomonas luteolaPseudomonas luteola9
Substituted aryl malonamates as new serine beta-lactamase substrates: structure-activity studiesEnterobacter cloacae9
Biochemical and structural characterization of the subclass B1 metallo-β-lactamase VIM-4Pseudomonas aeruginosa9
Biochemical characterization of the TEM-107 extended-spectrum β-lactamase in a Klebsiella pneumoniae isolate from South KoreaKlebsiella pneumoniae9
Genetic and biochemical characterization of GES-5, an extended-spectrum class A beta-lactamase from Klebsiella pneumoniaeKlebsiella pneumoniae8
Crystal structure of a cold-adapted class C beta-lactamasePseudomonas fluorescens8
Biochemical and genetic characterization of carbapenem-hydrolyzing β-lactamase OXA-229 from Acinetobacter bereziniaeAcinetobacter bereziniae8
Comparative insight into the roles of the non active-site residues E169 and N173 in imparting the beta-lactamase activity of CTX-M-15Escherichia coli8
Structural and Kinetic Basis for the Rational Design of Next-Generation β-Lactamase InhibitorsPseudomonas aeruginosa8
A Val292 substitution combined with an alanine duplication (ADUP) in the Ω loop of ADC β-lactamase confers reduced susceptibility to advanced β-lactam agents, including cefiderocolAcinetobacter baumannii8
Purification and characterization of a beta-lactamase from Haemophilus ducreyi in Escherichia coliHaemophilus ducreyi7
Kinetics of turnover of cefotaxime by the Enterobacter cloacae P99 and GCl beta-lactamases: two free enzyme forms of the P99 beta-lactamase detected by a combination of pre- and post-steady state…Enterobacter cloacae7
Cloning and functional characterization of the ambler class C beta-lactamase of Yersinia ruckeriYersinia ruckeri7
Genetic and biochemical characterization of FUS-1 (OXA-85), a narrow-spectrum class D beta-lactamase from Fusobacterium nucleatum subsp. polymorphumFusobacterium nucleatum subsp. polymorphum7
Exploring the role of L209 residue in the active site of NDM-1 a metallo-β-lactamase—7
Biochemical characterization of the carbapenem-hydrolyzing beta-lactamase AsbM1 from Aeromonas sobria AER 14M: a member of a novel subgroup of metallo-beta-lactamasesAeromonas sobria7
Characterization and sequence of the Chryseobacterium (Flavobacterium) meningosepticum carbapenemase: a new molecular class B beta-lactamase showing a broad substrate profileChryseobacterium meningosepticum7
Beta-lactamases (Actinomycetes species)Streptomyces albus6
Genetic and biochemical characterization of OXA-63, a new class D beta-lactamase from Brachyspira pilosicoli BM4442Brachyspira pilosicoli5
Novel chimeric beta-lactamase CTX-M-64, a hybrid of CTX-M-15-like and CTX-M-14 beta-lactamases, found in a Shigella sonnei strain resistant to various oxyimino-cephalosporins, including ceftazidimeShigella sonnei5
NCY-1 β-Lactamase Activity Correlates With Antimicrobial Susceptibility of a Clinical Strain of Nocardia cyriacigeorgicaNocardia cyriacigeorgica5
Role of Ambler Position 104 in Defining Substrate Specificity in the KPC Family of β-LactamasesKlebsiella pneumoniae5
Insights into the molecular basis for the carbenicillinase activity of PSE-4 beta-lactamase from crystallographic and kinetic studiesPseudomonas aeruginosa4
Penicillin sulfone inhibitors of class D beta-lactamases—4
A metallo-beta-lactamase enzyme in action: crystal structures of the monozinc carbapenemase CphA and its complex with biapenemAeromonas hydrophila3
Increased structural flexibility at the active site of a fluorophore-conjugated beta-lactamase distinctively impacts its binding toward diverse cephalosporin antibioticsBacillus cereus3
Emergence of Ceftazidime-Avibactam-Induced KPC Variants (KPC-25/127) in Intracranial Infection and Implications for Clinical ManagementKlebsiella pneumoniae3
Repeated insertions at positions 261-280 in KPC-2 highlight a ceftazidime-avibactam resistance hotspotKlebsiella pneumoniae3
Specificity inversion of Ochrobactrum anthropi D-aminopeptidase to a D,D-carboxypeptidase with new penicillin binding activity by directed mutagenesisOchrobactrum anthropi2
Tebipenem, a new carbapenem antibiotic, is a slow substrate that inhibits the β-lactamase from Mycobacterium tuberculosisMycobacterium tuberculosis2
Antibacterial activity of enmetazobactam against Acinetobacter spp.: a molecular dissection of mechanism of action and resistance determinantsAcinetobacter baumannii2
Beta-ketophosphonates as beta-lactamase inhibitors: Intramolecular cooperativity between the hydrophobic subsites of a class D beta-lactamaseEscherichia coli1
The continued evolution of the L2 cephalosporinase in Stenotrophomonas maltophilia: a key driver of beta-lactam resistanceStenotrophomonas maltophilia1

Records

The first 500 of 2,683 records, by enzyme, organism and substrate; all of them in Browse.

EnzymeOrganismSubstratekcat (s⁻¹)Km (mM)kcat/Km (mM⁻¹ s⁻¹)ConditionsPaper
ACT-1 beta-lactamase (plasmid-encoded class C AmpC)—Ampicillin10.0017600pH 7, 30 °CPMID 16189104Open
ACT-1 beta-lactamase (plasmid-encoded class C AmpC)—Aztreonam—1.2 × 10⁻⁵—pH 7, 30 °CPMID 16189104Open
ACT-1 beta-lactamase (plasmid-encoded class C AmpC)—Benzylpenicillin550.00212.6 × 10⁴pH 7, 30 °CPMID 16189104Open
ACT-1 beta-lactamase (plasmid-encoded class C AmpC)—Cefazolin5600.431.3 × 10³pH 7, 30 °CPMID 16189104Open
ACT-1 beta-lactamase (plasmid-encoded class C AmpC)—Cefotaxime0.057 × 10⁻⁵700pH 7, 30 °CPMID 16189104Open
ACT-1 beta-lactamase (plasmid-encoded class C AmpC)—Cefoxitin0.375 × 10⁻⁴740pH 7, 30 °CPMID 16189104Open
ACT-1 beta-lactamase (plasmid-encoded class C AmpC)—Cefuroxime0.121.9 × 10⁻⁵6.3 × 10³pH 7, 30 °CPMID 16189104Open
ACT-1 beta-lactamase (plasmid-encoded class C AmpC)—Cephalexin850.0422 × 10³pH 7, 30 °CPMID 16189104Open
ACT-1 beta-lactamase (plasmid-encoded class C AmpC)—Cephaloridine——1.3 × 10³pH 7, 30 °CPMID 16189104Open
ACT-1 beta-lactamase (plasmid-encoded class C AmpC)—Cephalothin4600.0381.2 × 10⁴pH 7, 30 °CPMID 16189104Open
ACT-1 beta-lactamase (plasmid-encoded class C AmpC)—Imipenem0.0113.7 × 10⁻⁴30pH 7, 30 °CPMID 16189104Open
ACT-1 beta-lactamase (plasmid-encoded class C AmpC)—Imipenem—3.8 × 10⁻⁴—pH 7, 30 °CPMID 16189104Open
ACT-1 beta-lactamase (plasmid-encoded class C AmpC)—Nitrocefin4000.0221.8 × 10⁴pH 7, 30 °CPMID 16189104Open
ACT-1 beta-lactamase (plasmid-encoded class C AmpC)—Oxacillin0.0449 × 10⁻⁵500pH 7, 30 °CPMID 16189104Open
ADC-30Acinetobacter baumanniicefiderocol0.0030.01360.2pH 7.2, 25 °CPMID 41949313Open
ADC-30Acinetobacter baumanniiceftazidime0.280.031810pH 7.2, 25 °CPMID 41949313Open
ADC-30Acinetobacter baumanniicephalothin2.26 × 10⁴0.69113.27 × 10⁴pH 7.2, 25 °CPMID 41949313Open
ADC-30Acinetobacter baumanniinitrocefin5.5 × 10³0.19422.82 × 10⁴pH 7.2, 25 °CPMID 41949313Open
ADC-33Acinetobacter baumanniicefiderocol0.350.12362.8pH 7.2, 25 °CPMID 41949313Open
ADC-33Acinetobacter baumanniiceftazidime2.20.023990pH 7.2, 25 °CPMID 41949313Open
ADC-33Acinetobacter baumanniicephalothin3100.04097.6 × 10³pH 7.2, 25 °CPMID 41949313Open
ADC-33Acinetobacter baumanniinitrocefin2.4 × 10³0.14511.69 × 10⁴pH 7.2, 25 °CPMID 41949313Open
ALI-1 metallo-β-lactamaseAliivibrio salmonicidaCefepime0.5810.1773.3pH 7.2PMID 25362569Open
ALI-1 metallo-β-lactamaseAliivibrio salmonicidaCefoxitin0.270.0793.4pH 7.2PMID 25362569Open
ALI-1 metallo-β-lactamaseAliivibrio salmonicidaCeftazidime0.090.0372.4pH 7.2PMID 25362569Open
ALI-1 metallo-β-lactamaseAliivibrio salmonicidaCefuroxime110.068160pH 7.2PMID 25362569Open
ALI-1 metallo-β-lactamaseAliivibrio salmonicidaErtapenem4——pH 7.2PMID 25362569Open
ALI-1 metallo-β-lactamaseAliivibrio salmonicidaErtapenem—0.073—pH 7.2PMID 25362569Open
ALI-1 metallo-β-lactamaseAliivibrio salmonicidaErtapenem——54pH 7.2PMID 25362569Open
ALI-1 metallo-β-lactamaseAliivibrio salmonicidaErtapenemwith 0.5 M NaCl4.3——pH 7.2PMID 25362569Open
ALI-1 metallo-β-lactamaseAliivibrio salmonicidaErtapenemwith 0.5 M NaCl—0.017—pH 7.2PMID 25362569Open
ALI-1 metallo-β-lactamaseAliivibrio salmonicidaErtapenemwith 0.5 M NaCl——250pH 7.2PMID 25362569Open
ALI-1 metallo-β-lactamaseAliivibrio salmonicidaImipenem80.9338.5pH 7.2PMID 25362569Open
ALI-1 metallo-β-lactamaseAliivibrio salmonicidaMeropenem130.14294pH 7.2PMID 25362569Open
ALI-1 metallo-β-lactamaseAliivibrio salmonicidaNitrocefin6.30.0061 × 10³pH 7.2PMID 25362569Open
AmpC beta-lactamaseEscherichia coli(3-Hydroxymethyl)phenoxymethylpenicillin110.002254.9 × 10³pH 8, 30 °CPMID 8042993Open
AmpC beta-lactamaseEscherichia coliAmpicillin30.00307980pH 8, 30 °CPMID 8042993Open
AmpC beta-lactamaseEscherichia coliAztreonam0.0024—410pH 8, 30 °CPMID 8042993Open
AmpC beta-lactamaseEscherichia coliBenzylpenicillin860.00451.95 × 10⁴pH 8, 30 °CPMID 8042993Open
AmpC beta-lactamaseEscherichia coliBenzylpenicillin methyl ester430.001752.4 × 10⁴pH 8, 30 °CPMID 8042993Open
AmpC beta-lactamaseEscherichia coliCarbenicillin0.00443 × 10⁻⁵135pH 8, 30 °CPMID 8042993Open
AmpC beta-lactamaseEscherichia coliCarbenicillin methyl ester0.0063 × 10⁻⁴23pH 8, 30 °CPMID 8042993Open
AmpC beta-lactamaseEscherichia colicarboxymethyl benzoylaminothioacetate——2.9pH 8, 30 °CPMID 8042993Open
AmpC beta-lactamaseEscherichia coliCefazolin4771.51320pH 8, 30 °CPMID 8042993Open
AmpC beta-lactamaseEscherichia coliCefotaxime0.158.7 × 10⁻⁴170pH 8, 30 °CPMID 8042993Open
AmpC beta-lactamaseEscherichia coliCefuroxime0.058.7 × 10⁻⁵575pH 8, 30 °CPMID 8042993Open
AmpC beta-lactamaseEscherichia coliCephaloridine1880.19990pH 8, 30 °CPMID 8042993Open
AmpC beta-lactamaseEscherichia coliCephalosporin C5400.0747.3 × 10³pH 8, 30 °CPMID 8042993Open
AmpC beta-lactamaseEscherichia colideacetylcephalosporin C3640.057.2 × 10³pH 8, 30 °CPMID 8042993Open
AmpC beta-lactamaseEscherichia coliDeacetylcephalosporin C lactone1130.01866.1 × 10³pH 8, 30 °CPMID 8042993Open
AmpC beta-lactamaseEscherichia coliDL-phenyl-lactyl benzoylaminoacetate301.3222.7pH 8, 30 °CPMID 8042993Open
AmpC beta-lactamaseEscherichia coliImipenem0.005—9.3pH 8, 30 °CPMID 8042993Open
AmpC beta-lactamaseEscherichia coliNitrocefin6700.521.29 × 10³pH 8, 30 °CPMID 8042993Open
AmpC beta-lactamaseEscherichia coliPhenoxymethylpenicillin430.00696.3 × 10³pH 8, 30 °CPMID 8042993Open
AmpC beta-lactamasevariant T316AEscherichia coli(3-Hydroxymethyl)phenoxymethylpenicillin4.80.00292.3 × 10³pH 8, 30 °CPMID 8042993Open
AmpC beta-lactamasevariant T316AEscherichia coliAmpicillin2.50.00373670pH 8, 30 °CPMID 8042993Open
AmpC beta-lactamasevariant T316AEscherichia coliAztreonam0.0014—77pH 8, 30 °CPMID 8042993Open
AmpC beta-lactamasevariant T316AEscherichia coliBenzylpenicillin830.01226.8 × 10³pH 8, 30 °CPMID 8042993Open
AmpC beta-lactamasevariant T316AEscherichia coliBenzylpenicillin methyl ester8.43 × 10⁻⁴2.8 × 10⁴pH 8, 30 °CPMID 8042993Open
AmpC beta-lactamasevariant T316AEscherichia coliCarbenicillin0.00314 × 10⁻⁴7.4pH 8, 30 °CPMID 8042993Open
AmpC beta-lactamasevariant T316AEscherichia coliCarbenicillin methyl ester0.0063 × 10⁻⁵176pH 8, 30 °CPMID 8042993Open
AmpC beta-lactamasevariant T316AEscherichia colicarboxymethyl benzoylaminothioacetate——0.7pH 8, 30 °CPMID 8042993Open
AmpC beta-lactamasevariant T316AEscherichia coliCefazolin907.512pH 8, 30 °CPMID 8042993Open
AmpC beta-lactamasevariant T316AEscherichia coliCefotaxime0.0770.0064112pH 8, 30 °CPMID 8042993Open
AmpC beta-lactamasevariant T316AEscherichia coliCefuroxime0.0325.2 × 10⁻⁴61pH 8, 30 °CPMID 8042993Open
AmpC beta-lactamasevariant T316AEscherichia coliCephalexin15.60.105150pH 8, 30 °CPMID 8042993Open
AmpC beta-lactamasevariant T316AEscherichia coliCephaloridine1001.8753pH 8, 30 °CPMID 8042993Open
AmpC beta-lactamasevariant T316AEscherichia coliCephalosporin C2160.36600pH 8, 30 °CPMID 8042993Open
AmpC beta-lactamasevariant T316AEscherichia coliCephalothin1750.93188pH 8, 30 °CPMID 8042993Open
AmpC beta-lactamasevariant T316AEscherichia colideacetylcephalosporin C5120.2232.3 × 10³pH 8, 30 °CPMID 8042993Open
AmpC beta-lactamasevariant T316AEscherichia coliDeacetylcephalosporin C lactone1390.02435.7 × 10³pH 8, 30 °CPMID 8042993Open
AmpC beta-lactamasevariant T316AEscherichia coliDL-phenyl-lactyl benzoylaminoacetate——0.19pH 8, 30 °CPMID 8042993Open
AmpC beta-lactamasevariant T316AEscherichia coliImipenem0.004—0.11pH 8, 30 °CPMID 8042993Open
AmpC beta-lactamasevariant T316AEscherichia coliNitrocefin6450.658980pH 8, 30 °CPMID 8042993Open
AmpC beta-lactamasevariant T316AEscherichia coliPhenoxymethylpenicillin380.01682.27 × 10³pH 8, 30 °CPMID 8042993Open
AmpC beta-lactamasevariant T316VEscherichia coli(3-Hydroxymethyl)phenoxymethylpenicillin1.130.00125904pH 8, 30 °CPMID 8042993Open
AmpC beta-lactamasevariant T316VEscherichia coliAmpicillin0.820.0026320pH 8, 30 °CPMID 8042993Open
AmpC beta-lactamasevariant T316VEscherichia coliAztreonam0.0026—104pH 8, 30 °CPMID 8042993Open
AmpC beta-lactamasevariant T316VEscherichia coliBenzylpenicillin390.01013.8 × 10³pH 8, 30 °CPMID 8042993Open
AmpC beta-lactamasevariant T316VEscherichia coliBenzylpenicillin methyl ester2.78 × 10⁻⁵3.4 × 10⁴pH 8, 30 °CPMID 8042993Open
AmpC beta-lactamasevariant T316VEscherichia coliCarbenicillin0.00310.00780.4pH 8, 30 °CPMID 8042993Open
AmpC beta-lactamasevariant T316VEscherichia coliCarbenicillin methyl ester0.00383 × 10⁻⁵110pH 8, 30 °CPMID 8042993Open
AmpC beta-lactamasevariant T316VEscherichia colicarboxymethyl benzoylaminothioacetate——0.24pH 8, 30 °CPMID 8042993Open
AmpC beta-lactamasevariant T316VEscherichia coliCefazolin——3pH 8, 30 °CPMID 8042993Open
AmpC beta-lactamasevariant T316VEscherichia coliCefotaxime0.0370.03281.1pH 8, 30 °CPMID 8042993Open
AmpC beta-lactamasevariant T316VEscherichia coliCefuroxime0.0250.0038.3pH 8, 30 °CPMID 8042993Open
AmpC beta-lactamasevariant T316VEscherichia coliCephalexin6.50.610.8pH 8, 30 °CPMID 8042993Open
AmpC beta-lactamasevariant T316VEscherichia coliCephaloridine——8pH 8, 30 °CPMID 8042993Open
AmpC beta-lactamasevariant T316VEscherichia coliCephalosporin C941.6557pH 8, 30 °CPMID 8042993Open
AmpC beta-lactamasevariant T316VEscherichia coliCephalothin462.541.8pH 8, 30 °CPMID 8042993Open
AmpC beta-lactamasevariant T316VEscherichia colideacetylcephalosporin C1520.34450pH 8, 30 °CPMID 8042993Open
AmpC beta-lactamasevariant T316VEscherichia coliDeacetylcephalosporin C lactone40.0061660pH 8, 30 °CPMID 8042993Open
AmpC beta-lactamasevariant T316VEscherichia coliDL-phenyl-lactyl benzoylaminoacetate——0.02pH 8, 30 °CPMID 8042993Open
AmpC beta-lactamasevariant T316VEscherichia coliImipenem0.003—0.034pH 8, 30 °CPMID 8042993Open
AmpC beta-lactamasevariant T316VEscherichia coliNitrocefin361.133pH 8, 30 °CPMID 8042993Open
AmpC beta-lactamasevariant T316VEscherichia coliPhenoxymethylpenicillin140.015910pH 8, 30 °CPMID 8042993Open
AmpC beta-lactamase of E. coli HKY28Escherichia coliampicillin0.430.006270pH 7, 37 °CPMID 15215122Open
AmpC beta-lactamase of E. coli HKY28Escherichia colicefepime10.04921pH 7, 37 °CPMID 15215122Open
AmpC beta-lactamase of E. coli HKY28Escherichia colicefotaxime0.370.03112pH 7, 37 °CPMID 15215122Open
AmpC beta-lactamase of E. coli HKY28Escherichia colicefoxitin0.0430.001238pH 7, 37 °CPMID 15215122Open
AmpC beta-lactamase of E. coli HKY28Escherichia colicefpirome1.50.02171pH 7, 37 °CPMID 15215122Open
AmpC beta-lactamase of E. coli HKY28Escherichia coliceftazidime0.0840.005715pH 7, 37 °CPMID 15215122Open
AmpC beta-lactamase of E. coli HKY28Escherichia colicephaloridine640.1640pH 7, 37 °CPMID 15215122Open
AmpC beta-lactamase of E. coli HKY28Gly286-Ser287-Asp288 insertion (revertant AmpCR)Escherichia coliampicillin40.013320pH 7, 37 °CPMID 15215122Open
AmpC beta-lactamase of E. coli HKY28Gly286-Ser287-Asp288 insertion (revertant AmpCR)Escherichia colicefepime0.210.21.1pH 7, 37 °CPMID 15215122Open
AmpC beta-lactamase of E. coli HKY28Gly286-Ser287-Asp288 insertion (revertant AmpCR)Escherichia colicefotaxime1.20.01397pH 7, 37 °CPMID 15215122Open
AmpC beta-lactamase of E. coli HKY28Gly286-Ser287-Asp288 insertion (revertant AmpCR)Escherichia colicefoxitin0.350.003991pH 7, 37 °CPMID 15215122Open
AmpC beta-lactamase of E. coli HKY28Gly286-Ser287-Asp288 insertion (revertant AmpCR)Escherichia colicefpirome0.210.121.8pH 7, 37 °CPMID 15215122Open
AmpC beta-lactamase of E. coli HKY28Gly286-Ser287-Asp288 insertion (revertant AmpCR)Escherichia coliceftazidime3.50.556.4pH 7, 37 °CPMID 15215122Open
AmpC beta-lactamase of E. coli HKY28Gly286-Ser287-Asp288 insertion (revertant AmpCR)Escherichia colicephaloridine3000.78390pH 7, 37 °CPMID 15215122Open
AmpC M19 beta-lactamaseMorganella morganiiAmpicillin0.068 × 10⁻⁵75030 °CPMID 16495258Open
AmpC M19 beta-lactamaseMorganella morganiiCefotaxime—5 × 10⁻⁴14030 °CPMID 16495258Open
AmpC M19 beta-lactamaseMorganella morganiiCephalothin140.04630030 °CPMID 16495258Open
AmpC M19 beta-lactamaseMorganella morganiiImipenem0.110.0042730 °CPMID 16495258Open
AmpC M29 beta-lactamaseMorganella morganiiAmpicillin0.0651.3 × 10⁻⁴50030 °CPMID 16495258Open
AmpC M29 beta-lactamaseMorganella morganiiBenzylpenicillin0.00742.5 × 10⁻⁴3030 °CPMID 16495258Open
AmpC M29 beta-lactamaseMorganella morganiiCefepime0.0080.0950.0830 °CPMID 16495258Open
AmpC M29 beta-lactamaseMorganella morganiiCefotaxime0.0322 × 10⁻⁵1.6 × 10³30 °CPMID 16495258Open
AmpC M29 beta-lactamaseMorganella morganiiCefoxitin0.0381.8 × 10⁻⁵2.1 × 10³30 °CPMID 16495258Open
AmpC M29 beta-lactamaseMorganella morganiiCeftazidime0.049 × 10⁻⁴4530 °CPMID 16495258Open
AmpC M29 beta-lactamaseMorganella morganiiCephalothin1400.1481 × 10³30 °CPMID 16495258Open
AmpC M29 beta-lactamaseMorganella morganiiImipenem0.070.0023530 °CPMID 16495258Open
AmpC M29 beta-lactamaseMorganella morganiiNitrocefin930.0253.8 × 10³30 °CPMID 16495258Open
AmpC M29 beta-lactamaseMorganella morganiiOxacillin0.0223 × 10⁻⁶7 × 10³30 °CPMID 16495258Open
AmpC M29 beta-lactamaseMorganella morganiiPiperacillin1.51.7 × 10⁻⁴9 × 10³30 °CPMID 16495258Open
AmpC M37 beta-lactamaseMorganella morganiiAmpicillin0.066 × 10⁻⁵1 × 10³30 °CPMID 16495258Open
AmpC M37 beta-lactamaseMorganella morganiiCefotaxime—9 × 10⁻⁵1 × 10³30 °CPMID 16495258Open
AmpC M37 beta-lactamaseMorganella morganiiCephalothin60.1066030 °CPMID 16495258Open
AmpC M37 beta-lactamaseMorganella morganiiImipenem0.070.0017030 °CPMID 16495258Open
AmpC-AEscherichia coliCefotaxime0.20.0258PMID 19001118Open
AmpC-AEscherichia coliCefoxitin0.30.001300PMID 19001118Open
AmpC-AEscherichia coliCeftazidime0.50.077PMID 19001118Open
AmpC-AEscherichia coliCephaloridine2300.65350PMID 19001118Open
AmpC-AEscherichia coliCephalothin5000.031.6 × 10⁴PMID 19001118Open
AmpC-AEscherichia coliImipenem0.10.0110PMID 19001118Open
AmpC-Avariant S287NEscherichia coliCefepime1.350.07520PMID 19001118Open
AmpC-Avariant S287NEscherichia coliCefotaxime0.081 × 10⁻⁴800PMID 19001118Open
AmpC-Avariant S287NEscherichia coliCefoxitin0.17 × 10⁻⁴100PMID 19001118Open
AmpC-Avariant S287NEscherichia coliCeftazidime0.24 × 10⁻⁴500PMID 19001118Open
AmpC-Avariant S287NEscherichia coliCephaloridine500.06800PMID 19001118Open
AmpC-Avariant S287NEscherichia coliCephalothin650.00551.2 × 10⁴PMID 19001118Open
AmpC-Avariant S287NEscherichia coliImipenem0.062 × 10⁻⁴300PMID 19001118Open
AmpC-B2Escherichia coliCefotaxime0.10.0452PMID 19001118Open
AmpC-B2Escherichia coliCefoxitin0.40.0015300PMID 19001118Open
AmpC-B2Escherichia coliCeftazidime0.30.271PMID 19001118Open
AmpC-B2Escherichia coliCephaloridine2400.95250PMID 19001118Open
AmpC-B2Escherichia coliCephalothin5400.0856 × 10³PMID 19001118Open
AmpC-B2Escherichia coliImipenem0.090.0323PMID 19001118Open
AmpC-B2variant S287NEscherichia coliCefepime0.250.0377PMID 19001118Open
AmpC-B2variant S287NEscherichia coliCefotaxime0.0450.00145PMID 19001118Open
AmpC-B2variant S287NEscherichia coliCefoxitin0.088 × 10⁻⁴100PMID 19001118Open
AmpC-B2variant S287NEscherichia coliCeftazidime0.010.001200PMID 19001118Open
AmpC-B2variant S287NEscherichia coliCephaloridine1120.13860PMID 19001118Open
AmpC-B2variant S287NEscherichia coliCephalothin100.045200PMID 19001118Open
AmpC-B2variant S287NEscherichia coliImipenem0.060.00230PMID 19001118Open
AsbM1 carbapenem-hydrolyzing metallo-beta-lactamaseAeromonas sobriaAmpicillin0.130.0652pH 7.2, 25 °CPMID 8998985Open
AsbM1 carbapenem-hydrolyzing metallo-beta-lactamaseAeromonas sobriaBenzylpenicillin1.20.167.5pH 7.2, 25 °CPMID 8998985Open
AsbM1 carbapenem-hydrolyzing metallo-beta-lactamaseAeromonas sobriaBiapenem1.50.169.4pH 7.2, 25 °CPMID 8998985Open
AsbM1 carbapenem-hydrolyzing metallo-beta-lactamaseAeromonas sobriaCarbenicillin0.440.02816pH 7.2, 25 °CPMID 8998985Open
AsbM1 carbapenem-hydrolyzing metallo-beta-lactamaseAeromonas sobriaImipenem710.23310pH 7.2, 25 °CPMID 8998985Open
AsbM1 carbapenem-hydrolyzing metallo-beta-lactamaseAeromonas sobriaMeropenem2200.63350pH 7.2, 25 °CPMID 8998985Open
AsbM1 carbapenem-hydrolyzing metallo-beta-lactamaseAeromonas sobriaSUN5555150.036420pH 7.2, 25 °CPMID 8998985Open
BcII metallo-beta-lactamase (Zn2+-beta-lactamase II)Bacillus cereusbenzylpenicillin2300.171.36 × 10³pH 7.5, 30 °CPMID 11964169Open
BcII metallo-beta-lactamase (Zn2+-beta-lactamase II)Bacillus cereuscefotaxime0.4 µM ZnSO4——820pH 7.5, 30 °CPMID 11964169Open
BcII metallo-beta-lactamase (Zn2+-beta-lactamase II)Bacillus cereuscefotaxime100 µM ZnSO4——1.3 × 10³pH 7.5, 30 °CPMID 11964169Open
BcII metallo-beta-lactamase (Zn2+-beta-lactamase II)Bacillus cereuscefoxitin——0.2pH 7.5, 30 °CPMID 11964169Open
BcII metallo-beta-lactamase (Zn2+-beta-lactamase II)Bacillus cereuscephaloridine0.4 µM ZnSO4——11.5pH 7.5, 30 °CPMID 11964169Open
BcII metallo-beta-lactamase (Zn2+-beta-lactamase II)Bacillus cereuscephaloridine100 µM ZnSO4——46pH 7.5, 30 °CPMID 11964169Open
BcII metallo-beta-lactamase (Zn2+-beta-lactamase II)Bacillus cereusimipenem0.4 µM ZnSO4——170pH 7.5, 30 °CPMID 11964169Open
BcII metallo-beta-lactamase (Zn2+-beta-lactamase II)Bacillus cereusimipenem100 µM ZnSO4——220pH 7.5, 30 °CPMID 11964169Open
BcII metallo-beta-lactamase (Zn2+-beta-lactamase II)Bacillus cereusnitrocefinno zinc added; [Zn2+] approx. 0.4 µM430.0094.9 × 10³pH 7.5, 30 °CPMID 11964169Open
BcII metallo-beta-lactamase (Zn2+-beta-lactamase II)Bacillus cereusnitrocefin[Zn2+] 0.4 µM——1.5 × 10³pH 7.5, 30 °CPMID 11964169Open
BcII metallo-beta-lactamase (Zn2+-beta-lactamase II)Bacillus cereusnitrocefin[Zn2+] 10 µM——2.3 × 10³pH 7.5, 30 °CPMID 11964169Open
BcII metallo-beta-lactamase (Zn2+-beta-lactamase II)Bacillus cereusnitrocefin[Zn2+] 100 µM——3.1 × 10³pH 7.5, 30 °CPMID 11964169Open
BcII metallo-beta-lactamase (Zn2+-beta-lactamase II)variant C221ABacillus cereuscefotaxime0.4 µM ZnSO4——0.65pH 7.5, 30 °CPMID 11964169Open
BcII metallo-beta-lactamase (Zn2+-beta-lactamase II)variant C221ABacillus cereuscefotaxime100 µM ZnSO4——200pH 7.5, 30 °CPMID 11964169Open
BcII metallo-beta-lactamase (Zn2+-beta-lactamase II)variant C221ABacillus cereuscephaloridine——11pH 7.5, 30 °CPMID 11964169Open
BcII metallo-beta-lactamase (Zn2+-beta-lactamase II)variant C221ABacillus cereusimipenem0.4 µM ZnSO4——0.4pH 7.5, 30 °CPMID 11964169Open
BcII metallo-beta-lactamase (Zn2+-beta-lactamase II)variant C221ABacillus cereusimipenem100 µM ZnSO4——4pH 7.5, 30 °CPMID 11964169Open
BcII metallo-beta-lactamase (Zn2+-beta-lactamase II)variant C221ABacillus cereusnitrocefin[Zn2+] 0.4 µM——1pH 7.5, 30 °CPMID 11964169Open
BcII metallo-beta-lactamase (Zn2+-beta-lactamase II)variant C221ABacillus cereusnitrocefin[Zn2+] 10 µM——87pH 7.5, 30 °CPMID 11964169Open
BcII metallo-beta-lactamase (Zn2+-beta-lactamase II)variant C221ABacillus cereusnitrocefin[Zn2+] 20 µM——87pH 7.5, 30 °CPMID 11964169Open
BcII metallo-beta-lactamase (Zn2+-beta-lactamase II)variant C221ABacillus cereusnitrocefin[Zn2+] 50 µM——110pH 7.5, 30 °CPMID 11964169Open
BcII metallo-beta-lactamase (Zn2+-beta-lactamase II)variant C221ABacillus cereusnitrocefin[Zn2+] 100 µM——280pH 7.5, 30 °CPMID 11964169Open
BcII metallo-beta-lactamase (Zn2+-beta-lactamase II)variant C221SBacillus cereusbenzylpenicillinno zinc added; [Zn2+] approx. 0.4 µM150.47531pH 7.5, 30 °CPMID 11964169Open
BcII metallo-beta-lactamase (Zn2+-beta-lactamase II)variant C221SBacillus cereusbenzylpenicillin100 µM Zn2+ (row "C221S (100 µM Zn2+)")2000.775262pH 7.5, 30 °CPMID 11964169Open
BcII metallo-beta-lactamase (Zn2+-beta-lactamase II)variant C221SBacillus cereuscefotaxime0.4 µM ZnSO4——1pH 7.5, 30 °CPMID 11964169Open
BcII metallo-beta-lactamase (Zn2+-beta-lactamase II)variant C221SBacillus cereuscefotaxime100 µM ZnSO4——130pH 7.5, 30 °CPMID 11964169Open
BcII metallo-beta-lactamase (Zn2+-beta-lactamase II)variant C221SBacillus cereuscephaloridine——6.6pH 7.5, 30 °CPMID 11964169Open
BcII metallo-beta-lactamase (Zn2+-beta-lactamase II)variant C221SBacillus cereusimipenem0.4 µM ZnSO4——1pH 7.5, 30 °CPMID 11964169Open
BcII metallo-beta-lactamase (Zn2+-beta-lactamase II)variant C221SBacillus cereusimipenem100 µM ZnSO4——16pH 7.5, 30 °CPMID 11964169Open
BcII metallo-beta-lactamase (Zn2+-beta-lactamase II)variant C221SBacillus cereusnitrocefinno zinc added; [Zn2+] approx. 0.4 µM1.30.008166pH 7.5, 30 °CPMID 11964169Open
BcII metallo-beta-lactamase (Zn2+-beta-lactamase II)variant C221SBacillus cereusnitrocefin100 µM Zn2+ (row "C221S (100 µM Zn2+)")630.0213 × 10³pH 7.5, 30 °CPMID 11964169Open
BcII metallo-beta-lactamase (Zn2+-beta-lactamase II)variant C221SBacillus cereusnitrocefin[Zn2+] 0.4 µM——2.5pH 7.5, 30 °CPMID 11964169Open
BcII metallo-beta-lactamase (Zn2+-beta-lactamase II)variant C221SBacillus cereusnitrocefin[Zn2+] 10 µM——340pH 7.5, 30 °CPMID 11964169Open
BcII metallo-beta-lactamase (Zn2+-beta-lactamase II)variant C221SBacillus cereusnitrocefin[Zn2+] 20 µM——340pH 7.5, 30 °CPMID 11964169Open
BcII metallo-beta-lactamase (Zn2+-beta-lactamase II)variant C221SBacillus cereusnitrocefin[Zn2+] 50 µM——370pH 7.5, 30 °CPMID 11964169Open
BcII metallo-beta-lactamase (Zn2+-beta-lactamase II)variant C221SBacillus cereusnitrocefin[Zn2+] 100 µM——680pH 7.5, 30 °CPMID 11964169Open
BcII metallo-beta-lactamase (Zn2+-beta-lactamase II)variant D120NBacillus cereusbenzylpenicillin3.50.447.9pH 7.5, 30 °CPMID 11964169Open
BcII metallo-beta-lactamase (Zn2+-beta-lactamase II)variant D120NBacillus cereusimipenem0.4 µM ZnSO4——2.5pH 7.5, 30 °CPMID 11964169Open
BcII metallo-beta-lactamase (Zn2+-beta-lactamase II)variant D120NBacillus cereusimipenem100 µM ZnSO4——2.8pH 7.5, 30 °CPMID 11964169Open
BcII metallo-beta-lactamase (Zn2+-beta-lactamase II)variant D120NBacillus cereusnitrocefin2.20.13316.5pH 7.5, 30 °CPMID 11964169Open
BcII metallo-beta-lactamase (Zn2+-beta-lactamase II)variant H116SBacillus cereusbenzylpenicillin470.5389pH 7.5, 30 °CPMID 11964169Open
BcII metallo-beta-lactamase (Zn2+-beta-lactamase II)variant H116SBacillus cereusnitrocefinno zinc added; [Zn2+] approx. 0.4 µM440.18227pH 7.5, 30 °CPMID 11964169Open
BcII metallo-beta-lactamase (Zn2+-beta-lactamase II)variant H116SBacillus cereusnitrocefin[Zn2+] 0.4 µM——240pH 7.5, 30 °CPMID 11964169Open
BcII metallo-beta-lactamase (Zn2+-beta-lactamase II)variant H116SBacillus cereusnitrocefin[Zn2+] 20 µM——300pH 7.5, 30 °CPMID 11964169Open
BcII metallo-beta-lactamase (Zn2+-beta-lactamase II)variant H116SBacillus cereusnitrocefin[Zn2+] 100 µM——330pH 7.5, 30 °CPMID 11964169Open
BcII metallo-beta-lactamase (Zn2+-beta-lactamase II)variant H118SBacillus cereusbenzylpenicillin362.312.2pH 7.5, 30 °CPMID 11964169Open
BcII metallo-beta-lactamase (Zn2+-beta-lactamase II)variant H118SBacillus cereusimipenem0.4 µM ZnSO4——5.3pH 7.5, 30 °CPMID 11964169Open
BcII metallo-beta-lactamase (Zn2+-beta-lactamase II)variant H118SBacillus cereusimipenem100 µM ZnSO4——8.8pH 7.5, 30 °CPMID 11964169Open
BcII metallo-beta-lactamase (Zn2+-beta-lactamase II)variant H118SBacillus cereusnitrocefinno zinc added; [Zn2+] approx. 0.4 µM50.2221.6pH 7.5, 30 °CPMID 11964169Open
BcII metallo-beta-lactamase (Zn2+-beta-lactamase II)variant H118SBacillus cereusnitrocefin[Zn2+] 0.4 µM——42pH 7.5, 30 °CPMID 11964169Open
BcII metallo-beta-lactamase (Zn2+-beta-lactamase II)variant H118SBacillus cereusnitrocefin[Zn2+] 10 µM——60pH 7.5, 30 °CPMID 11964169Open
BcII metallo-beta-lactamase (Zn2+-beta-lactamase II)variant H118SBacillus cereusnitrocefin[Zn2+] 20 µM——59pH 7.5, 30 °CPMID 11964169Open
BcII metallo-beta-lactamase (Zn2+-beta-lactamase II)variant H118SBacillus cereusnitrocefin[Zn2+] 100 µM——76pH 7.5, 30 °CPMID 11964169Open
BcII metallo-beta-lactamase (Zn2+-beta-lactamase II)variant H196SBacillus cereusbenzylpenicillin75.71.23pH 7.5, 30 °CPMID 11964169Open
BcII metallo-beta-lactamase (Zn2+-beta-lactamase II)variant H196SBacillus cereusbenzylpenicillin5 µM ZnSO4——0.1pH 5, 30 °CPMID 11964169Open
BcII metallo-beta-lactamase (Zn2+-beta-lactamase II)variant H196SBacillus cereusbenzylpenicillin10 µM ZnSO4——0.25pH 5, 30 °CPMID 11964169Open
BcII metallo-beta-lactamase (Zn2+-beta-lactamase II)variant H196SBacillus cereusbenzylpenicillin100 µM ZnSO4——0.43pH 5, 30 °CPMID 11964169Open
BcII metallo-beta-lactamase (Zn2+-beta-lactamase II)variant H196SBacillus cereusbenzylpenicillin1 mM ZnSO4——1.7pH 5, 30 °CPMID 11964169Open
BcII metallo-beta-lactamase (Zn2+-beta-lactamase II)variant H196SBacillus cereusbenzylpenicillin5 µM ZnSO4——2.2pH 7, 30 °CPMID 11964169Open
BcII metallo-beta-lactamase (Zn2+-beta-lactamase II)variant H196SBacillus cereusbenzylpenicillin10 µM ZnSO4——2.8pH 7, 30 °CPMID 11964169Open
BcII metallo-beta-lactamase (Zn2+-beta-lactamase II)variant H196SBacillus cereusbenzylpenicillin100 µM ZnSO4——3.7pH 7, 30 °CPMID 11964169Open
BcII metallo-beta-lactamase (Zn2+-beta-lactamase II)variant H196SBacillus cereusbenzylpenicillin1 mM ZnSO4——6.2pH 7, 30 °CPMID 11964169Open
BcII metallo-beta-lactamase (Zn2+-beta-lactamase II)variant H196SBacillus cereuscefotaxime0.4 µM ZnSO4——4pH 7.5, 30 °CPMID 11964169Open
BcII metallo-beta-lactamase (Zn2+-beta-lactamase II)variant H196SBacillus cereuscefotaxime100 µM ZnSO4——14.5pH 7.5, 30 °CPMID 11964169Open
BcII metallo-beta-lactamase (Zn2+-beta-lactamase II)variant H196SBacillus cereuscephaloridine0.4 µM ZnSO4——1.5pH 7.5, 30 °CPMID 11964169Open
BcII metallo-beta-lactamase (Zn2+-beta-lactamase II)variant H196SBacillus cereuscephaloridine100 µM ZnSO4——1.6pH 7.5, 30 °CPMID 11964169Open
BcII metallo-beta-lactamase (Zn2+-beta-lactamase II)variant H196SBacillus cereusimipenem0.4 µM ZnSO4——1.5pH 7.5, 30 °CPMID 11964169Open
BcII metallo-beta-lactamase (Zn2+-beta-lactamase II)variant H196SBacillus cereusimipenem100 µM ZnSO4——3pH 7.5, 30 °CPMID 11964169Open
BcII metallo-beta-lactamase (Zn2+-beta-lactamase II)variant H196SBacillus cereusnitrocefinno zinc added; [Zn2+] approx. 0.4 µM0.20.161.4pH 7.5, 30 °CPMID 11964169Open
BcII metallo-beta-lactamase (Zn2+-beta-lactamase II)variant H196SBacillus cereusnitrocefin[Zn2+] 0.4 µM——6.6pH 7.5, 30 °CPMID 11964169Open
BcII metallo-beta-lactamase (Zn2+-beta-lactamase II)variant H196SBacillus cereusnitrocefin[Zn2+] 10 µM——13pH 7.5, 30 °CPMID 11964169Open
BcII metallo-beta-lactamase (Zn2+-beta-lactamase II)variant H196SBacillus cereusnitrocefin[Zn2+] 20 µM——11pH 7.5, 30 °CPMID 11964169Open
BcII metallo-beta-lactamase (Zn2+-beta-lactamase II)variant H196SBacillus cereusnitrocefin[Zn2+] 100 µM——13.5pH 7.5, 30 °CPMID 11964169Open
BcII metallo-beta-lactamase (Zn2+-beta-lactamase II)variant H263SBacillus cereusbenzylpenicillin——2.6pH 7.5, 30 °CPMID 11964169Open
BcII metallo-beta-lactamase (Zn2+-beta-lactamase II)variant H263SBacillus cereuscefotaxime——2.5pH 7.5, 30 °CPMID 11964169Open
BcII metallo-beta-lactamase (Zn2+-beta-lactamase II)variant H263SBacillus cereuscephaloridine——0.19pH 7.5, 30 °CPMID 11964169Open
BcII metallo-beta-lactamase (Zn2+-beta-lactamase II)variant H263SBacillus cereusimipenem0.4 µM ZnSO4——2pH 7.5, 30 °CPMID 11964169Open
BcII metallo-beta-lactamase (Zn2+-beta-lactamase II)variant H263SBacillus cereusimipenem100 µM ZnSO4——2.4pH 7.5, 30 °CPMID 11964169Open
BcII metallo-beta-lactamase (Zn2+-beta-lactamase II)variant H263SBacillus cereusnitrocefinno zinc added; [Zn2+] approx. 0.4 µM1.30.3653.6pH 7.5, 30 °CPMID 11964169Open
BcII metallo-beta-lactamase (Zn2+-beta-lactamase II)variant H263SBacillus cereusnitrocefin[Zn2+] 0.4 µM——2.1pH 7.5, 30 °CPMID 11964169Open
BcII metallo-beta-lactamase (Zn2+-beta-lactamase II)variant H263SBacillus cereusnitrocefin[Zn2+] 10 µM——3.2pH 7.5, 30 °CPMID 11964169Open
BcII metallo-beta-lactamase (Zn2+-beta-lactamase II)variant H263SBacillus cereusnitrocefin[Zn2+] 20 µM——4.3pH 7.5, 30 °CPMID 11964169Open
BcII metallo-beta-lactamase (Zn2+-beta-lactamase II)variant H263SBacillus cereusnitrocefin[Zn2+] 100 µM——10pH 7.5, 30 °CPMID 11964169Open
BcII metallo-beta-lactamase (Zn2+-beta-lactamase II)variant N233YBacillus cereusimipenem0.4 µM ZnSO4——28pH 7.5, 30 °CPMID 11964169Open
BcII metallo-beta-lactamase (Zn2+-beta-lactamase II)variant N233YBacillus cereusimipenem100 µM ZnSO4——110pH 7.5, 30 °CPMID 11964169Open
BcII metallo-beta-lactamase (Zn2+-beta-lactamase II)variant N233YBacillus cereusnitrocefin60.017330pH 7.5, 30 °CPMID 11964169Open
BcII metallo-β-lactamaseBacillus cereusBenzylpenicillin1900.151.2 × 10³pH 7.5, 30 °CPMID 12725860Open
BcII metallo-β-lactamaseBacillus cereusCefotaxime1200.0245 × 10³pH 7.5, 30 °CPMID 12725860Open
BcII metallo-β-lactamaseBacillus cereusCefoxitin0.340.241.4pH 7.5, 30 °CPMID 12725860Open
BcII metallo-β-lactamaseBacillus cereuscephaloridine——300pH 7.5, 30 °CPMID 12725860Open
BcII metallo-β-lactamaseBacillus cereusImipenem1170.091.3 × 10³pH 7.5, 30 °CPMID 12725860Open
BcII metallo-β-lactamaseBacillus cereusNitrocefin270.012.7 × 10³pH 7.5, 30 °CPMID 12725860Open
BcII metallo-β-lactamasevariant BcIIΔIMP (BcII loop 60SFNGEA66 replaced by IMP-1 loop EVNGWGV)Bacillus cereusBenzylpenicillin2930.0329.2 × 10³pH 7.5, 30 °CPMID 12725860Open
BcII metallo-β-lactamasevariant BcIIΔIMP (BcII loop 60SFNGEA66 replaced by IMP-1 loop EVNGWGV)Bacillus cereusCefotaxime320.0074.6 × 10³pH 7.5, 30 °CPMID 12725860Open
BcII metallo-β-lactamasevariant BcIIΔIMP (BcII loop 60SFNGEA66 replaced by IMP-1 loop EVNGWGV)Bacillus cereusCefoxitin0.350.0635.5pH 7.5, 30 °CPMID 12725860Open
BcII metallo-β-lactamasevariant BcIIΔIMP (BcII loop 60SFNGEA66 replaced by IMP-1 loop EVNGWGV)Bacillus cereuscephaloridine1560.0473.3 × 10³pH 7.5, 30 °CPMID 12725860Open
BcII metallo-β-lactamasevariant BcIIΔIMP (BcII loop 60SFNGEA66 replaced by IMP-1 loop EVNGWGV)Bacillus cereusImipenem1040.0781.3 × 10³pH 7.5, 30 °CPMID 12725860Open
BcII metallo-β-lactamasevariant BcIIΔIMP (BcII loop 60SFNGEA66 replaced by IMP-1 loop EVNGWGV)Bacillus cereusNitrocefin680.00521.3 × 10⁴pH 7.5, 30 °CPMID 12725860Open
BcII metallo-β-lactamasevariant BcIIΔIMP W64A (IMP-1 loop in BcII, then W64A)Bacillus cereusBenzylpenicillin1430.154900pH 7.5, 30 °CPMID 12725860Open
BcII metallo-β-lactamasevariant BcIIΔIMP W64A (IMP-1 loop in BcII, then W64A)Bacillus cereusCefotaxime270.038700pH 7.5, 30 °CPMID 12725860Open
BcII metallo-β-lactamasevariant BcIIΔIMP W64A (IMP-1 loop in BcII, then W64A)Bacillus cereusCefoxitin0.660.930.7pH 7.5, 30 °CPMID 12725860Open
BcII metallo-β-lactamasevariant BcIIΔIMP W64A (IMP-1 loop in BcII, then W64A)Bacillus cereuscephaloridine570.56100pH 7.5, 30 °CPMID 12725860Open
BcII metallo-β-lactamasevariant BcIIΔIMP W64A (IMP-1 loop in BcII, then W64A)Bacillus cereusImipenem1800.9200pH 7.5, 30 °CPMID 12725860Open
BcII metallo-β-lactamasevariant BcIIΔIMP W64A (IMP-1 loop in BcII, then W64A)Bacillus cereusNitrocefin3.20.011300pH 7.5, 30 °CPMID 12725860Open
beta-lactamaseBacillus licheniformis3α-(hydroxymethyl)-2,2-dimethyl-6β-(phenoxyacetamido)penam1120.9120 calc.pH 8, 30 °CPMID 1974463Open
beta-lactamaseBacillus licheniformis3α-(hydroxymethyl)-2,2-dimethyl-6β-(phenoxyacetamido)penam650.28230 calc.pH 9, 30 °CPMID 1974463Open
beta-lactamaseBacillus licheniformis[2-[[p-(dimethylamino)phenyl]azo]pyridinio]cephalosporin6670.144.63 × 10³pH 7, 30 °CPMID 1974463Open
beta-lactamaseBacillus licheniformisampicillin22410.211.06 × 10⁴pH 7, 30 °CPMID 1974463Open
beta-lactamaseBacillus licheniformisbenzylpenicillin2.65 × 10³0.122.15 × 10⁴pH 7, 30 °CPMID 1974463Open
beta-lactamaseBacillus licheniformisnitrocefin10880.0412.64 × 10⁴pH 7, 30 °CPMID 1974463Open
beta-lactamaseBacillus licheniformisphenoxymethylpenicillin50 mM sodium phosphate; 0.15 M KCl25520.12.48 × 10⁴pH 7, 30 °CPMID 1974463Open
beta-lactamaseBacillus licheniformisphenoxymethylpenicillin50 mM sodium phosphate; 0 M KCl19360.0424.6 × 10⁴pH 7, 30 °CPMID 1974463Open
beta-lactamaseBacillus licheniformisphenoxymethylpenicillin50 mM sodium phosphate; 0.5 M KCl2.42 × 10³0.12.4 × 10⁴pH 7, 30 °CPMID 1974463Open
beta-lactamaseBacillus licheniformisphenoxymethylpenicillin50 mM sodium phosphate; 1.0 M KCl2.6 × 10³0.12.6 × 10⁴pH 7, 30 °CPMID 1974463Open
beta-lactamaseBacillus licheniformisphenoxymethylpenicillin50 mM sodium phosphate; 1.5 M KCl2.45 × 10³0.12.4 × 10⁴pH 7, 30 °CPMID 1974463Open
beta-lactamaseBacillus licheniformisphenoxymethylpenicillin11650.393.0 × 10³ calc.pH 4, 30 °CPMID 1974463Open
beta-lactamaseBacillus licheniformisphenoxymethylpenicillin2.4 × 10³0.327.5 × 10³ calc.pH 5, 30 °CPMID 1974463Open
beta-lactamaseBacillus licheniformisphenoxymethylpenicillin2.7 × 10³0.221.2 × 10⁴ calc.pH 6, 30 °CPMID 1974463Open
beta-lactamaseBacillus licheniformisphenoxymethylpenicillin40 mM buffer; 0.4 M KCl; 20% methanol2.7 × 10³0.161.7 × 10⁴ calc.pH 7, 30 °CPMID 1974463Open
beta-lactamaseBacillus licheniformisphenoxymethylpenicillin1.65 × 10³0.131.3 × 10⁴ calc.pH 8, 30 °CPMID 1974463Open
beta-lactamaseBacillus licheniformisphenoxymethylpenicillin4150.085.2 × 10³ calc.pH 9, 30 °CPMID 1974463Open
beta-lactamaseBacillus licheniformisphenoxymethylpenicillin——2.2 × 10⁴30 °CPMID 1974463Open
beta-lactamasevariant K234ABacillus licheniformis3α-(hydroxymethyl)-2,2-dimethyl-6β-(phenoxyacetamido)penam80.98.9 calc.pH 5, 30 °CPMID 1974463Open
beta-lactamasevariant K234ABacillus licheniformis[2-[[p-(dimethylamino)phenyl]azo]pyridinio]cephalosporin——0.32pH 7, 30 °CPMID 1974463Open
beta-lactamasevariant K234ABacillus licheniformisampicillin——0.89pH 7, 30 °CPMID 1974463Open
beta-lactamasevariant K234ABacillus licheniformisbenzylpenicillin——2.3pH 7, 30 °CPMID 1974463Open
beta-lactamasevariant K234ABacillus licheniformisnitrocefin——3.9pH 7, 30 °CPMID 1974463Open
beta-lactamasevariant K234ABacillus licheniformisphenoxymethylpenicillin0.15 M KCl——9.3pH 7, 30 °CPMID 1974463Open
beta-lactamasevariant K234ABacillus licheniformisphenoxymethylpenicillin0.70.125.8 calc.pH 4, 30 °CPMID 1974463Open
beta-lactamasevariant K234ABacillus licheniformisphenoxymethylpenicillin95616 calc.pH 8.5, 30 °CPMID 1974463Open
beta-lactamasevariant K234ABacillus licheniformisphenoxymethylpenicillin0.5 M KCl32.22.812pH 7, 30 °CPMID 1974463Open
beta-lactamasevariant K234ABacillus licheniformisphenoxymethylpenicillin1.5 M KCl30.3130pH 7, 30 °CPMID 1974463Open
beta-lactamasevariant K234ABacillus licheniformisphenoxymethylpenicillin1.20.139.2 calc.pH 5, 30 °CPMID 1974463Open
beta-lactamasevariant K234ABacillus licheniformisphenoxymethylpenicillin——1430 °CPMID 1974463Open
beta-lactamasevariant K234EBacillus licheniformis3α-(hydroxymethyl)-2,2-dimethyl-6β-(phenoxyacetamido)penam0.50.22.5 calc.pH 4, 30 °CPMID 1974463Open
beta-lactamasevariant K234EBacillus licheniformis3α-(hydroxymethyl)-2,2-dimethyl-6β-(phenoxyacetamido)penam4.10.75.9 calc.pH 5, 30 °CPMID 1974463Open
beta-lactamasevariant K234EBacillus licheniformis[2-[[p-(dimethylamino)phenyl]azo]pyridinio]cephalosporin3.21.22.7pH 7, 30 °CPMID 1974463Open
beta-lactamasevariant K234EBacillus licheniformisampicillin21.113.71.5pH 7, 30 °CPMID 1974463Open
beta-lactamasevariant K234EBacillus licheniformisbenzylpenicillin49.68.16.1pH 7, 30 °CPMID 1974463Open
beta-lactamasevariant K234EBacillus licheniformisnitrocefin24.73.37.6pH 7, 30 °CPMID 1974463Open
beta-lactamasevariant K234EBacillus licheniformisphenoxymethylpenicillin0.15 M KCl31.71.521pH 7, 30 °CPMID 1974463Open
beta-lactamasevariant K234EBacillus licheniformisphenoxymethylpenicillinKCl1.60.1213 calc.pH 4, 30 °CPMID 1974463Open
beta-lactamasevariant K234EBacillus licheniformisphenoxymethylpenicillin331.917 calc.pH 8.5, 30 °CPMID 1974463Open
beta-lactamasevariant K234EBacillus licheniformisphenoxymethylpenicillin0 M KCl2939.7pH 7, 30 °CPMID 1974463Open
beta-lactamasevariant K234EBacillus licheniformisphenoxymethylpenicillin0.3 M KCl37.31.231pH 7, 30 °CPMID 1974463Open
beta-lactamasevariant K234EBacillus licheniformisphenoxymethylpenicillin0.5 M KCl310.839pH 7, 30 °CPMID 1974463Open
beta-lactamasevariant K234EBacillus licheniformisphenoxymethylpenicillin1.0 M KCl27.80.469pH 7, 30 °CPMID 1974463Open
beta-lactamasevariant K234EBacillus licheniformisphenoxymethylpenicillin1.5 M KCl320.3110pH 7, 30 °CPMID 1974463Open
beta-lactamasevariant K234EBacillus licheniformisphenoxymethylpenicillinKCl (Table III conditions; no methanol)1.50.115 calc.pH 4, 30 °CPMID 1974463Open
beta-lactamasevariant K234EBacillus licheniformisphenoxymethylpenicillin2.30.1515 calc.pH 5, 30 °CPMID 1974463Open
beta-lactamasevariant K234EBacillus licheniformisphenoxymethylpenicillin70.2627 calc.pH 6, 30 °CPMID 1974463Open
beta-lactamasevariant K234EBacillus licheniformisphenoxymethylpenicillin——3430 °CPMID 1974463Open
beta-lactamaseMycobacterium tuberculosisAmoxicillin—0.095—pH 6, 37 °CPMID 9624479Open
beta-lactamaseMycobacterium tuberculosisAzlocillin—0.34—pH 6, 37 °CPMID 9624479Open
beta-lactamaseMycobacterium tuberculosisAzlocillinchromatofocusing peak 2 fraction (pI 4.9 beta-lactamase)—0.326—pH 6, 37 °CPMID 9624479Open
beta-lactamaseMycobacterium tuberculosisBenzylpenicillin—0.058—pH 6, 37 °CPMID 9624479Open
beta-lactamaseMycobacterium tuberculosisBenzylpenicillinchromatofocusing peak 2 fraction (pI 4.9 beta-lactamase)—0.074—pH 6, 37 °CPMID 9624479Open
beta-lactamaseMycobacterium tuberculosisCefamandole—0.282—pH 6, 37 °CPMID 9624479Open
beta-lactamaseMycobacterium tuberculosisCefamandolechromatofocusing peak 2 fraction (pI 4.9 beta-lactamase)—0.566—pH 6, 37 °CPMID 9624479Open
beta-lactamaseMycobacterium tuberculosisCefazolin—0.304—pH 6, 37 °CPMID 9624479Open
beta-lactamaseMycobacterium tuberculosisCephaloridine—0.54—pH 6, 37 °CPMID 9624479Open
beta-lactamaseMycobacterium tuberculosisCephalothin—0.218—pH 6, 37 °CPMID 9624479Open
beta-lactamaseMycobacterium tuberculosisCephapirin—0.319—pH 6, 37 °CPMID 9624479Open
beta-lactamaseMycobacterium tuberculosisNitrocefin—0.114—pH 6, 37 °CPMID 9624479Open
beta-lactamaseMycobacterium tuberculosisNitrocefinchromatofocusing peak 2 fraction (pI 4.9 beta-lactamase)—0.105—pH 6, 37 °CPMID 9624479Open
beta-lactamaseMycobacterium tuberculosisPhenoxymethylpenicillin—0.078—pH 6, 37 °CPMID 9624479Open
beta-lactamaseStreptomyces albusAmpicillin—0.9—pH 7, 30 °CPMID 1134377Open
beta-lactamaseStreptomyces albusbenzylpenicillin—0.74—pH 7, 30 °CPMID 1134377Open
beta-lactamaseStreptomyces albusCephalothin—1.33—pH 7, 30 °CPMID 1134377Open
beta-lactamaseStreptomyces albusCloxacillin—0.25—pH 7, 30 °CPMID 1134377Open
beta-lactamaseStreptomyces albusMethicillin—0.77—pH 7, 30 °CPMID 1134377Open
beta-lactamaseStreptomyces albusOxacillin—0.33—pH 7, 30 °CPMID 1134377Open
beta-lactamase (class A, TEM-type) encoded by H. ducreyi plasmid pCbHaemophilus ducreyiampicillin1.46 × 10³0.062.4 × 10⁴pH 7, 37 °CPMID 11570857Open
beta-lactamase (class A, TEM-type) encoded by H. ducreyi plasmid pCbHaemophilus ducreyibenzylpenicillin1.8 × 10³0.044.5 × 10⁴pH 7, 37 °CPMID 11570857Open
beta-lactamase (class A, TEM-type) encoded by H. ducreyi plasmid pCbHaemophilus ducreyicarbenicillin2600.261 × 10³pH 7, 37 °CPMID 11570857Open
beta-lactamase (class A, TEM-type) encoded by H. ducreyi plasmid pCbHaemophilus ducreyicefoperazone2000.141.4 × 10³pH 7, 37 °CPMID 11570857Open
beta-lactamase (class A, TEM-type) encoded by H. ducreyi plasmid pCbHaemophilus ducreyicephaloridine2.05 × 10³1.41.5 × 10³pH 7, 37 °CPMID 11570857Open
beta-lactamase (class A, TEM-type) encoded by H. ducreyi plasmid pCbHaemophilus ducreyicephalothin2800.45600pH 7, 37 °CPMID 11570857Open
beta-lactamase (class A, TEM-type) encoded by H. ducreyi plasmid pCbHaemophilus ducreyinitrocefin7600.051.5 × 10⁴pH 7, 37 °CPMID 11570857Open
beta-lactamase AmpC YRC-1Yersinia ruckeribenzylpenicillin450.065700pH 7, 30 °CPMID 16553832Open
beta-lactamase AmpC YRC-1Yersinia ruckericefotaxime0.3——pH 7, 30 °CPMID 16553832Open
beta-lactamase AmpC YRC-1Yersinia ruckericefoxitin0.3——pH 7, 30 °CPMID 16553832Open
beta-lactamase AmpC YRC-1Yersinia ruckericeftazidime10.52pH 7, 30 °CPMID 16553832Open
beta-lactamase AmpC YRC-1Yersinia ruckericefuroxime1——pH 7, 30 °CPMID 16553832Open
beta-lactamase AmpC YRC-1Yersinia ruckericephaloridin1200.43280pH 7, 30 °CPMID 16553832Open
beta-lactamase AmpC YRC-1Yersinia ruckericephalothin4000.058 × 10³pH 7, 30 °CPMID 16553832Open
beta-lactamase BCL-1Bacillus clausiiAmoxicillin850.0224 × 10³pH 7, 30 °CPMID 17846134Open
beta-lactamase BCL-1Bacillus clausiiBenzylpenicillin970.0128 × 10³pH 7, 30 °CPMID 17846134Open
beta-lactamase BCL-1Bacillus clausiiCefotaxime220.7930pH 7, 30 °CPMID 17846134Open
beta-lactamase BCL-1Bacillus clausiiCefpirome950.1361 × 10³pH 7, 30 °CPMID 17846134Open
beta-lactamase BCL-1Bacillus clausiiCeftriaxone300.9530pH 7, 30 °CPMID 17846134Open
beta-lactamase BCL-1Bacillus clausiiCefuroxime150.105100pH 7, 30 °CPMID 17846134Open
beta-lactamase BCL-1Bacillus clausiiCephaloridine1150.0452.5 × 10³pH 7, 30 °CPMID 17846134Open
beta-lactamase BCL-1Bacillus clausiiCephalothin220.0151.5 × 10³pH 7, 30 °CPMID 17846134Open
beta-lactamase BCL-1Bacillus clausiiImipenem0.060.035100pH 7, 30 °CPMID 17846134Open
beta-lactamase BCL-1Bacillus clausiiPiperacillin380.0212 × 10³pH 7, 30 °CPMID 17846134Open
beta-lactamase BCL-1Bacillus clausiiTicarcillin50.0061 × 10³pH 7, 30 °CPMID 17846134Open
beta-lactamase BEL-1Pseudomonas aeruginosaAmoxicillin100.03330pH 7, 30 °CPMID 16127048Open
beta-lactamase BEL-1Pseudomonas aeruginosaAztreonam100.1100pH 7, 30 °CPMID 16127048Open
beta-lactamase BEL-1Pseudomonas aeruginosaBenzylpenicillin30.02150pH 7, 30 °CPMID 16127048Open
beta-lactamase BEL-1Pseudomonas aeruginosaCefepime10.157pH 7, 30 °CPMID 16127048Open
beta-lactamase BEL-1Pseudomonas aeruginosaCefotaxime300.25120pH 7, 30 °CPMID 16127048Open
beta-lactamase BEL-1Pseudomonas aeruginosacefsulodin250.15170pH 7, 30 °CPMID 16127048Open
beta-lactamase BEL-1Pseudomonas aeruginosaCeftriaxone250.03820pH 7, 30 °CPMID 16127048Open
beta-lactamase BEL-1Pseudomonas aeruginosaCefuroxime100.04250pH 7, 30 °CPMID 16127048Open
beta-lactamase BEL-1Pseudomonas aeruginosaCephaloridine300.13230pH 7, 30 °CPMID 16127048Open
beta-lactamase BEL-1Pseudomonas aeruginosaCephalothin1500.28540pH 7, 30 °CPMID 16127048Open
beta-lactamase BEL-1Pseudomonas aeruginosaPiperacillin20.015130pH 7, 30 °CPMID 16127048Open
beta-lactamase BEL-1Pseudomonas aeruginosaTicarcillin60.008750pH 7, 30 °CPMID 16127048Open
beta-lactamase form I (pI 6.8)Citrobacter diversusAmpicillin1190.0225.4 × 10³pH 7.2, 30 °CPMID 3264152Open
beta-lactamase form I (pI 6.8)Citrobacter diversusBenzylpenicillin5700.0698.3 × 10³pH 7.2, 30 °CPMID 3264152Open
beta-lactamase form I (pI 6.8)Citrobacter diversusCarbenicillin580.1600pH 7.2, 30 °CPMID 3264152Open
beta-lactamase form I (pI 6.8)Citrobacter diversusCefazolin1660.028.3 × 10³pH 7.2, 30 °CPMID 3264152Open
beta-lactamase form I (pI 6.8)Citrobacter diversusCefuroxime540.07770pH 7.2, 30 °CPMID 3264152Open
beta-lactamase form I (pI 6.8)Citrobacter diversusCephaloridine9300.741.25 × 10³pH 7.2, 30 °CPMID 3264152Open
beta-lactamase form I (pI 6.8)Citrobacter diversusCephalosporin C410.126300pH 7.2, 30 °CPMID 3264152Open
beta-lactamase form I (pI 6.8)Citrobacter diversusCephalothin630.0481.3 × 10³pH 7.2, 30 °CPMID 3264152Open
beta-lactamase form I (pI 6.8)Citrobacter diversusCloxacillin0.04——pH 7.2, 30 °CPMID 3264152Open
beta-lactamase form I (pI 6.8)Citrobacter diversusImipenem0.0160.0240.66pH 7.2, 30 °CPMID 3264152Open
beta-lactamase form I (pI 6.8)Citrobacter diversusMethicillin—0.0055—pH 7.2, 30 °CPMID 3264152Open
beta-lactamase form I (pI 6.8)Citrobacter diversusOxacillin2060.23900pH 7.2, 30 °CPMID 3264152Open
beta-lactamase form II (pI 6.2)Citrobacter diversusAmpicillin550.0242.3 × 10³pH 7.2, 30 °CPMID 3264152Open
beta-lactamase form II (pI 6.2)Citrobacter diversusBenzylpenicillin1320.0443 × 10³pH 7.2, 30 °CPMID 3264152Open
beta-lactamase form II (pI 6.2)Citrobacter diversusCarbenicillin290.115250pH 7.2, 30 °CPMID 3264152Open
beta-lactamase form II (pI 6.2)Citrobacter diversusCefazolin570.0272.1 × 10³pH 7.2, 30 °CPMID 3264152Open
beta-lactamase form II (pI 6.2)Citrobacter diversusCefuroxime300.072400pH 7.2, 30 °CPMID 3264152Open
beta-lactamase form II (pI 6.2)Citrobacter diversusCephaloridine9300.741.25 × 10³pH 7.2, 30 °CPMID 3264152Open
beta-lactamase form II (pI 6.2)Citrobacter diversusCephalosporin C230.123190pH 7.2, 30 °CPMID 3264152Open
beta-lactamase form II (pI 6.2)Citrobacter diversusCephalothin550.0411.3 × 10³pH 7.2, 30 °CPMID 3264152Open
beta-lactamase form II (pI 6.2)Citrobacter diversusCloxacillin0.024——pH 7.2, 30 °CPMID 3264152Open
beta-lactamase form II (pI 6.2)Citrobacter diversusImipenem0.0710.0270.41pH 7.2, 30 °CPMID 3264152Open
beta-lactamase form II (pI 6.2)Citrobacter diversusMethicillin—0.0042—pH 7.2, 30 °CPMID 3264152Open
beta-lactamase form II (pI 6.2)Citrobacter diversusOxacillin1010.3330pH 7.2, 30 °CPMID 3264152Open
beta-lactamase IBacillus cereus6-aminopenicillanic acid2601.6170pH 7, 20 °CPMID 1980064Open
beta-lactamase IBacillus cereus6-aminopenicillanic acid227.41.604142pH 7, 20 °CPMID 7910734Open
beta-lactamase IBacillus cereus6beta-furylacryloylamidopenicillanic acid14910.04093.64 × 10⁴pH 7, 20 °CPMID 7910734Open
beta-lactamase IBacillus cereusampicillin5 × 10³0.252 × 10⁴pH 7, 20 °CPMID 1980064Open
beta-lactamase IBacillus cereusbenzylpenicillin45150.11843.81 × 10⁴pH 7, 20 °CPMID 7910734Open
beta-lactamase IBacillus cereuscarbenicillin4400.152.8 × 10³pH 7, 20 °CPMID 1980064Open
beta-lactamase IBacillus cereuscephalosporin C0.20.220.9pH 7, 20 °CPMID 1980064Open
beta-lactamase IBacillus cereusN-(2-furyl)acryloylpenicillin1.7 × 10³0.0354.9 × 10⁴pH 7, 20 °CPMID 1980064Open
beta-lactamase IBacillus cereusnitrocefin340.055618pH 7, 20 °CPMID 1980064Open
beta-lactamase IBacillus cereusNitrocefin49.20.0954516pH 7, 20 °CPMID 7910734Open
beta-lactamase IBacillus cereusphenoxymethylpenicillin45250.13293.41 × 10⁴pH 7, 20 °CPMID 7910734Open
beta-lactamase Ivariant E166ABacillus cereus6-aminopenicillanic acid—0.101—pH 7, 20 °CPMID 7910734Open
beta-lactamase Ivariant E166ABacillus cereus6beta-furylacryloylamidopenicillanic acid0.3560.0055963.7pH 7, 20 °CPMID 7910734Open
beta-lactamase Ivariant E166ABacillus cereusbenzylpenicillin1.620.018786.6pH 7, 20 °CPMID 7910734Open
beta-lactamase Ivariant E166ABacillus cereusNitrocefin0.01510.05970.25pH 7, 20 °CPMID 7910734Open
beta-lactamase Ivariant E166ABacillus cereusphenoxymethylpenicillin0.9230.01754.4pH 7, 20 °CPMID 7910734Open
beta-lactamase Ivariant E166CBacillus cereus6-aminopenicillanic acid—0.127—pH 7, 20 °CPMID 7910734Open
beta-lactamase Ivariant E166CBacillus cereus6beta-furylacryloylamidopenicillanic acid0.1450.010214.2pH 7, 20 °CPMID 7910734Open
beta-lactamase Ivariant E166CBacillus cereusbenzylpenicillin0.8180.018444.4pH 7, 20 °CPMID 7910734Open
beta-lactamase Ivariant E166CBacillus cereusNitrocefin0.01020.06460.16pH 7, 20 °CPMID 7910734Open
beta-lactamase Ivariant E166CBacillus cereusphenoxymethylpenicillin0.340.020316.7pH 7, 20 °CPMID 7910734Open
beta-lactamase Ivariant E166CmcBacillus cereus6-aminopenicillanic acid—0.219—pH 7, 20 °CPMID 7910734Open
beta-lactamase Ivariant E166CmcBacillus cereus6beta-furylacryloylamidopenicillanic acid0.170.010616pH 7, 20 °CPMID 7910734Open
beta-lactamase Ivariant E166CmcBacillus cereusbenzylpenicillin0.8630.01750.7pH 7, 20 °CPMID 7910734Open
beta-lactamase Ivariant E166CmcBacillus cereusNitrocefin0.00860.08470.1pH 7, 20 °CPMID 7910734Open
beta-lactamase Ivariant E166CmcBacillus cereusphenoxymethylpenicillin0.3620.010335.2pH 7, 20 °CPMID 7910734Open
beta-lactamase Ivariant E166DBacillus cereus6-aminopenicillanic acid1.80.812.2pH 7, 20 °CPMID 1980064Open
beta-lactamase Ivariant E166DBacillus cereusampicillin1400.46308pH 7, 20 °CPMID 1980064Open
beta-lactamase Ivariant E166DBacillus cereusbenzylpenicillin0.670.008677pH 7, 20 °CPMID 1980064Open
beta-lactamase Ivariant E166DBacillus cereuscarbenicillin240.2886pH 7, 20 °CPMID 1980064Open
beta-lactamase Ivariant E166DBacillus cereuscephalosporin C0.0110.380.028pH 7, 20 °CPMID 1980064Open
beta-lactamase Ivariant E166DBacillus cereusN-(2-furyl)acryloylpenicillin300.086343pH 7, 20 °CPMID 1980064Open
beta-lactamase Ivariant E166DBacillus cereusnitrocefin0.810.05216pH 7, 20 °CPMID 1980064Open
beta-lactamase Ivariant K73RBacillus cereus6-aminopenicillanic acid0.0490.120.4pH 7, 20 °CPMID 1980064Open
beta-lactamase Ivariant K73RBacillus cereusampicillin1.30.08216pH 7, 20 °CPMID 1980064Open
beta-lactamase Ivariant K73RBacillus cereusbenzylpenicillin550.101550pH 7, 20 °CPMID 1980064Open
beta-lactamase Ivariant K73RBacillus cereuscarbenicillin0.460.04610pH 7, 20 °CPMID 1980064Open
beta-lactamase Ivariant K73RBacillus cereuscephalosporin C0.1 M sodium phosphate buffer; 0.5 M NaCl; 0.01 mM EDTA0.0010.270.005pH 7, 20 °CPMID 1980064Open
beta-lactamase Ivariant K73RBacillus cereuscephalosporin Cburst progress curves fitted to eqn (3); followed at 260 nm——2.7pH 7, 20 °CPMID 1980064Open
beta-lactamase Ivariant K73RBacillus cereusN-(2-furyl)acryloylpenicillin0.20.006830pH 7, 20 °CPMID 1980064Open
beta-lactamase Ivariant K73RBacillus cereusnitrocefin0.210.0782.7pH 7, 20 °CPMID 1980064Open
beta-lactamase Ivariant K73R/E166DBacillus cereus6-aminopenicillanic acid0.0010.160.006pH 7, 20 °CPMID 1980064Open
beta-lactamase Ivariant K73R/E166DBacillus cereusampicillin1.40.188pH 7, 20 °CPMID 1980064Open
beta-lactamase Ivariant K73R/E166DBacillus cereusbenzylpenicillin0.470.0147pH 7, 20 °CPMID 1980064Open
beta-lactamase Ivariant K73R/E166DBacillus cereuscarbenicillin0.370.113.3pH 7, 20 °CPMID 1980064Open
beta-lactamase Ivariant K73R/E166DBacillus cereuscephalosporin C4 × 10⁻⁴0.180.002pH 7, 20 °CPMID 1980064Open
beta-lactamase Ivariant K73R/E166DBacillus cereusN-(2-furyl)acryloylpenicillin0.240.00455pH 7, 20 °CPMID 1980064Open
beta-lactamase Ivariant K73R/E166DBacillus cereusnitrocefin7 × 10⁻⁴0.00150.4pH 7, 20 °CPMID 1980064Open
beta-lactamase II (zinc-dependent class B beta-lactamase)Bacillus cereus6-beta-iodopenicillanic acid4507.4660pH 6, 30 °CPMID 8471035Open
beta-lactamase II (zinc-dependent class B beta-lactamase)Bacillus cereusAmpicillin11051.53720pH 6, 30 °CPMID 8471035Open
beta-lactamase II (zinc-dependent class B beta-lactamase)Bacillus cereusbenzylpenicillin6781.5450pH 6, 30 °CPMID 8471035Open
beta-lactamase II (zinc-dependent class B beta-lactamase)Bacillus cereusCarbenicillin7554.2180pH 6, 30 °CPMID 8471035Open
beta-lactamase II (zinc-dependent class B beta-lactamase)Bacillus cereusCefotaxime600.09670pH 6, 30 °CPMID 8471035Open
beta-lactamase II (zinc-dependent class B beta-lactamase)Bacillus cereusCefoxitin0.22.10.095pH 6, 30 °CPMID 8471035Open
beta-lactamase II (zinc-dependent class B beta-lactamase)Bacillus cereusCefuroxime350.045780pH 6, 30 °CPMID 8471035Open
beta-lactamase II (zinc-dependent class B beta-lactamase)Bacillus cereusCephalexin1.70.35.7pH 6, 30 °CPMID 8471035Open
beta-lactamase II (zinc-dependent class B beta-lactamase)Bacillus cereusCephaloglycin610.19320pH 6, 30 °CPMID 8471035Open
beta-lactamase II (zinc-dependent class B beta-lactamase)Bacillus cereuscephaloridine251.3519pH 6, 30 °CPMID 8471035Open
beta-lactamase II (zinc-dependent class B beta-lactamase)Bacillus cereusImipenem——120pH 6, 30 °CPMID 8471035Open
beta-lactamase II (zinc-dependent class B beta-lactamase)Bacillus cereusMoxalactam1.20.6441.9pH 6, 30 °CPMID 8471035Open
beta-lactamase II (zinc-dependent class B beta-lactamase)Bacillus cereusNitrocefin450.07640pH 6, 30 °CPMID 8471035Open
beta-lactamase II (zinc-dependent class B beta-lactamase)Bacillus cereusOxacillin3251.75190pH 6, 30 °CPMID 8471035Open
beta-lactamase II (zinc-dependent class B beta-lactamase)Bacillus cereusSulbactam105.21.9pH 6, 30 °CPMID 8471035Open
beta-lactamase OXA-229Acinetobacter bereziniaeAmoxicillin15.20.40538PMID 22508298Open
beta-lactamase OXA-229Acinetobacter bereziniaeAmpicillin10.1278PMID 22508298Open
beta-lactamase OXA-229Acinetobacter bereziniaeBenzylpenicillin110.07150PMID 22508298Open
beta-lactamase OXA-229Acinetobacter bereziniaeCephalothin0.20.1651PMID 22508298Open
beta-lactamase OXA-229Acinetobacter bereziniaeImipenem0.090.033PMID 22508298Open
beta-lactamase OXA-229Acinetobacter bereziniaeOxacillin4.21.852PMID 22508298Open
beta-lactamase OXA-229Acinetobacter bereziniaePiperacillin2.20.02980PMID 22508298Open
beta-lactamase OXA-229Acinetobacter bereziniaeTicarcillin1.70.3435PMID 22508298Open
beta-lactamase OXA-55Shewanella algaeAmpicillin80.515pH 7, 30 °CPMID 15105119Open
beta-lactamase OXA-55Shewanella algaeBenzylpenicillin40.025160pH 7, 30 °CPMID 15105119Open
beta-lactamase OXA-55Shewanella algaeCefpirome0.10.670.1pH 7, 30 °CPMID 15105119Open
beta-lactamase OXA-55Shewanella algaeCeftazidime24.70.5pH 7, 30 °CPMID 15105119Open
beta-lactamase OXA-55Shewanella algaeCephaloridine100.7515pH 7, 30 °CPMID 15105119Open
beta-lactamase OXA-55Shewanella algaeCephalothin0.60.0710pH 7, 30 °CPMID 15105119Open
beta-lactamase OXA-55Shewanella algaeCloxacillin0.50.193pH 7, 30 °CPMID 15105119Open
beta-lactamase OXA-55Shewanella algaeImipenem0.10.025pH 7, 30 °CPMID 15105119Open
beta-lactamase OXA-55Shewanella algaeMeropenem0.050.50.1pH 7, 30 °CPMID 15105119Open
beta-lactamase OXA-55Shewanella algaeOxacillin50.3910pH 7, 30 °CPMID 15105119Open
beta-lactamase OXA-55Shewanella algaePiperacillin30.1130pH 7, 30 °CPMID 15105119Open
beta-lactamase OXA-55Shewanella algaeTicarcillin10.0250pH 7, 30 °CPMID 15105119Open
beta-lactamase type AStaphylococcus aureusAmpicillin—0.255—pH 6, 37 °CPMID 1605608Open
beta-lactamase type AStaphylococcus aureusAmpicillinkcat calculated from the enzyme concentration308——pH 6, 37 °CPMID 1605608Open
beta-lactamase type AStaphylococcus aureusCefamandole—0.005—pH 6, 37 °CPMID 1605608Open
beta-lactamase type AStaphylococcus aureusCefamandolekcat calculated from the enzyme concentration0.057——pH 6, 37 °CPMID 1605608Open
beta-lactamase type AStaphylococcus aureusCefazolin—0.0184—pH 6, 37 °CPMID 1605608Open
beta-lactamase type AStaphylococcus aureusCefazolinkcat calculated from the enzyme concentration1.01——pH 6, 37 °CPMID 1605608Open
beta-lactamase type AStaphylococcus aureusCefuroxime—0.378—pH 6, 37 °CPMID 1605608Open
beta-lactamase type AStaphylococcus aureusCefuroximekcat calculated from the enzyme concentration0.009——pH 6, 37 °CPMID 1605608Open
beta-lactamase type AStaphylococcus aureusCephaloridineTable 1—0.0109—pH 6, 37 °CPMID 1605608Open
beta-lactamase type AStaphylococcus aureusCephaloridinekcat calculated from the enzyme concentration; Table 21.95——pH 6, 37 °CPMID 1605608Open
beta-lactamase type AStaphylococcus aureusCephaloridineTable 4——179pH 6, 37 °CPMID 1605608Open
beta-lactamase type AStaphylococcus aureusCephalothin—0.0068—pH 6, 37 °CPMID 1605608Open
beta-lactamase type AStaphylococcus aureusCephalothinkcat calculated from the enzyme concentration0.015——pH 6, 37 °CPMID 1605608Open
beta-lactamase type AStaphylococcus aureusCephapirin—0.0052—pH 6, 37 °CPMID 1605608Open
beta-lactamase type AStaphylococcus aureusCephapirinkcat calculated from the enzyme concentration0.36——pH 6, 37 °CPMID 1605608Open
beta-lactamase type AStaphylococcus aureusNitrocefin—0.0064—pH 6, 37 °CPMID 1605608Open
beta-lactamase type AStaphylococcus aureusNitrocefinkcat calculated from the enzyme concentration23.2——pH 6, 37 °CPMID 1605608Open
beta-lactamase type AStaphylococcus aureusPenicillin G—0.0511—pH 6, 37 °CPMID 1605608Open
beta-lactamase type AStaphylococcus aureusPenicillin Gkcat calculated from the enzyme concentration171——pH 6, 37 °CPMID 1605608Open
beta-lactamase type BStaphylococcus aureusAmpicillin—0.16—pH 6, 37 °CPMID 1605608Open
beta-lactamase type BStaphylococcus aureusAmpicillinkcat calculated from the enzyme concentration412——pH 6, 37 °CPMID 1605608Open
beta-lactamase type BStaphylococcus aureusCefamandole—0.006—pH 6, 37 °CPMID 1605608Open