CatLogenzyme kinetics catalog

EC 1.16.3.4: cuproxidase

OxidoreductasesOpen in Browse

CatLog read 32 records for EC 1.16.3.4 from 5 papers, for 3 organisms. Names in these papers: Fet3p (multicopper ferroxidase), CueO, CueO (rCueO, recombinant), Fet3 protein (Fet3p), multicopper ferroxidase and 3 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 24 records for EC 1.16.3.4 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 1.16.3.4 in Browse.

Papers

PaperOrganismsRecords
Structural basis of the ferrous iron specificity of the yeast ferroxidase, Fet3pSaccharomyces cerevisiae14
Structure and function of the engineered multicopper oxidase CueO from Escherichia coli--deletion of the methionine-rich helical region covering the substrate-binding siteEscherichia coli8
Cuprous oxidase activity of yeast Fet3p and human ceruloplasmin: implication for functionHomo sapiens, Saccharomyces cerevisiae4
Spectral and kinetic properties of the Fet3 protein from Saccharomyces cerevisiae, a multinuclear copper ferroxidase enzymeSaccharomyces cerevisiae4
A robust metallo-oxidase from the hyperthermophilic bacterium Aquifex aeolicusHomo sapiens2

Records

EnzymeOrganismSubstratekcat (s⁻¹)Km (mM)kcat/Km (mM⁻¹ s⁻¹)ConditionsPaper
ceruloplasminHomo sapienscopper(1+)0.250.0337.6 calc.pH 3.5, 40 °CPMID 17451433Open
ceruloplasminHomo sapiensiron(2+)0.130.0284.8 calc.pH 5, 40 °CPMID 17451433Open
ceruloplasmin (hCp)Homo sapienscopper(1+)0.3750.036810.2 calc.pH 5PMID 14623105Open
ceruloplasmin (hCp)Homo sapiensiron(2+)0.5050.008361 calc.pH 5PMID 14623105Open
CueOΔα5–7 (Pro357–His406 deleted, replaced by Gly-Gly linker)Escherichia coli2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)no added CuSO4—12—pH 5.5, 25 °CPMID 17804014Open
CueOΔα5–7 (Pro357–His406 deleted, replaced by Gly-Gly linker)Escherichia coli2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)with added 10 mM CuSO4 (excess Cu(II), Table 3 footnote a)—11—pH 5.5, 25 °CPMID 17804014Open
CueOΔα5–7 (Pro357–His406 deleted, replaced by Gly-Gly linker)Escherichia coli2,6-dimethoxyphenol—1.8—pH 5.5, 25 °CPMID 17804014Open
CueOΔα5–7 (Pro357–His406 deleted, replaced by Gly-Gly linker)Escherichia colip-phenylenediamine—90—25 °CPMID 17804014Open
CueO (rCueO, recombinant)Escherichia coli2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)no added CuSO4—6.5—pH 5.5, 25 °CPMID 17804014Open
CueO (rCueO, recombinant)Escherichia coli2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)with added 1 mM CuSO4 (excess Cu(II), Table 3 footnote a)—6.4—pH 5.5, 25 °CPMID 17804014Open
CueO (rCueO, recombinant)Escherichia coli2,6-dimethoxyphenol—2.5—pH 5.5, 25 °CPMID 17804014Open
CueO (rCueO, recombinant)Escherichia colip-phenylenediamine—375—25 °CPMID 17804014Open
Fet3 protein (Fet3p), multicopper ferroxidaseSaccharomyces cerevisiaedioxygenEndo H-treated; partially deglycosylated0.0380.001329 calc.pH 6, 25 °CPMID 9722559Open
Fet3 protein (Fet3p), multicopper ferroxidaseSaccharomyces cerevisiaedioxygennative; fully glycosylated (not Endo H-treated)0.0350.001132 calc.pH 6, 25 °CPMID 9722559Open
Fet3 protein (Fet3p), multicopper ferroxidaseSaccharomyces cerevisiaeiron(2+)Endo H-treated; partially deglycosylated0.1580.004833 calc.pH 6, 25 °CPMID 9722559Open
Fet3 protein (Fet3p), multicopper ferroxidaseSaccharomyces cerevisiaeiron(2+)native; fully glycosylated (not Endo H-treated)0.1380.004134 calc.pH 6, 25 °CPMID 9722559Open
Fet3pSaccharomyces cerevisiaecopper(1+)1.320.037934.8 calc.pH 5PMID 14623105Open
Fet3pSaccharomyces cerevisiaeiron(2+)1.0650.0054200 calc.pH 5PMID 14623105Open
Fet3p (multicopper ferroxidase)Saccharomyces cerevisiaeferrous ironTable 20.6680.0049140 calc.pH 6PMID 17042492Open
Fet3p (multicopper ferroxidase)Saccharomyces cerevisiaeferrous ironin the text——137pH 6PMID 17042492Open
Fet3p (multicopper ferroxidase)Saccharomyces cerevisiaehydroquinoneTable 32.18825.50.0858 calc.pH 6PMID 17042492Open
Fet3p (multicopper ferroxidase)Saccharomyces cerevisiaehydroquinonein the text——0.085pH 6PMID 17042492Open
Fet3p (multicopper ferroxidase)variant D283ASaccharomyces cerevisiaeferrous iron1.2620.019365.4 calc.pH 6PMID 17042492Open
Fet3p (multicopper ferroxidase)variant D283ASaccharomyces cerevisiaehydroquinone2.82519.30.146 calc.pH 6PMID 17042492Open
Fet3p (multicopper ferroxidase)variant D409ASaccharomyces cerevisiaeferrous iron0.8030.018842.7 calc.pH 6PMID 17042492Open
Fet3p (multicopper ferroxidase)variant D409ASaccharomyces cerevisiaehydroquinone2.32830.30.0768 calc.pH 6PMID 17042492Open
Fet3p (multicopper ferroxidase)variant E185ASaccharomyces cerevisiaeferrous iron0.4050.035611.4 calc.pH 6PMID 17042492Open
Fet3p (multicopper ferroxidase)variant E185ASaccharomyces cerevisiaehydroquinone1.52818.20.0840 calc.pH 6PMID 17042492Open
Fet3p (multicopper ferroxidase)variant E185A/D409ASaccharomyces cerevisiaeferrous ironTable 20.2323.9940.0580 calc.pH 6PMID 17042492Open
Fet3p (multicopper ferroxidase)variant E185A/D409ASaccharomyces cerevisiaeferrous ironin the text——0.058pH 6PMID 17042492Open
Fet3p (multicopper ferroxidase)variant E185A/D409ASaccharomyces cerevisiaehydroquinoneTable 32.21330.50.0726 calc.pH 6PMID 17042492Open
Fet3p (multicopper ferroxidase)variant E185A/D409ASaccharomyces cerevisiaehydroquinonein the text——0.073pH 6PMID 17042492Open