Cloned (Comment) | Organism |
---|---|
expression in Escherichia coli | Serratia marcescens |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.028 | - |
nitrocefin | pH 7.5, 25°C | Serratia marcescens |
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 | UniProt | Comment | Textmining |
---|---|---|---|
Serratia marcescens | P52699 | - |
- |
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 | Comment | Organism |
---|---|---|
IMP-1 | - |
Serratia marcescens |
Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
135 | - |
nitrocefin | pH 7.5, 25°C | Serratia marcescens |