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Literature summary for 3.5.2.6 extracted from

  • Griffin, D.H.; Richmond, T.K.; Sanchez, C.; Moller, A.J.; Breece, R.M.; Tierney, D.L.; Bennett, B.; Crowder, M.W.
    Structural and kinetic studies on metallo-beta-lactamase IMP-1 (2011), Biochemistry, 50, 9125-9134.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli Serratia marcescens

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.028
-
nitrocefin pH 7.5, 25°C Serratia marcescens

Metals/Ions

Metals/Ions Comment Organism Structure
Co2+ UV-vis studies on IMP-1 containing 1 equivalent of Co(II) show a strong ligand-to-metal charge transition at 340 nm, and the intensity of this feature increases when the second equivalent of Co(II) is added to the enzyme Serratia marcescens
additional information metal-binding to metal-free IMP-1 follows a positive-cooperative mode Serratia marcescens
Zn2+ enzyme binds 2 equivalents of Zn2+ Serratia marcescens

Organism

Organism UniProt Comment Textmining
Serratia marcescens P52699
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
nitrocefin + H2O IMP-1 does not stabilize a nitrocefin-derived reaction intermediate, rather, the enzyme follows a simple Michaelis mechanism to hydrolyze nitrocefin Serratia marcescens (2R)-2-[(R)-carboxy[(thiophen-2-ylacetyl)amino]methyl]-5-[(E)-2-(2,4-dinitrophenyl)ethenyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
?

Synonyms

Synonyms Comment Organism
IMP-1
-
Serratia marcescens

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
135
-
nitrocefin pH 7.5, 25°C Serratia marcescens