Values CatLog read from this paper

A metallo-beta-lactamase enzyme in action: crystal structures of the monozinc carbapenemase CphA and its complex with biapenem

PMID 15588826doi:10.1016/j.jmb.2004.10.070Open in Browse

The paper itself is not on this site: read it at the publisher. This page lists only the values CatLog read from it.

CatLog read 3 records (9 values) from this paper: CphA metallo-β-lactamase (subclass B2 carbapenemase) from Aeromonas hydrophila.

Read from the paper by an AI model and checked against the paper by a second, separate AI run; code converted the units. Values are in CatLog's units; each record opens in Browse with the line the paper prints and the checks.

EC 3.5.2.6

Records read from this paper
EnzymeOrganismSubstratekcat (s⁻¹)Km (mM)kcat/Km (mM⁻¹ s⁻¹)ConditionsOpen record
CphA metallo-β-lactamase (subclass B2 carbapenemase)Aeromonas hydrophilabiapenem3000.1661.8 × 10³pH 6.5, 30 °COpen record: CphA metallo-β-lactamase (subclass B2 carbapenemase), biapenem
CphA metallo-β-lactamase (subclass B2 carbapenemase)variant N220GAeromonas hydrophilabiapenem1600.1181.3 × 10³pH 6.5, 30 °COpen record: CphA metallo-β-lactamase (subclass B2 carbapenemase) variant N220G, biapenem
CphA metallo-β-lactamase (subclass B2 carbapenemase)variant N220GAeromonas hydrophilaimipenem3900.057.8 × 10³pH 6.5, 30 °COpen record: CphA metallo-β-lactamase (subclass B2 carbapenemase) variant N220G, imipenem