EC Number   |
KM Value [mM] |
KM Value Maximum [mM] |
Substrate |
Reference |
|---|
    4.2.1.84 | -999 |
- |
more |
- |
648435 |
| 4.2.1.84 | -999 |
- |
more |
comparisons of the steady state kinetic parameters of the single subunit variant to the heterotrimeric protein show that the additional subunits impart substrate specificity and catalytic efficiency |
729257 |
| 4.2.1.84 | -999 |
- |
more |
enzyme-ligand complex kinetic constants, overview |
697296 |
| 4.2.1.84 | -999 |
- |
more |
recombinant wild-type and mutant enzymes, kinetics analysis, overview |
714254 |
| 4.2.1.84 | -999 |
- |
more |
relative binding affinities of water, nitriles, and amides in a nitrile hydratase model, direct competition studies using ion complexes, e.g. five-coordinate iron dithiolate (N,N'-bis-(2'-methyl-2'-mercaptopropyl)-1-thia-4,7-diazacyclononane)iron(III) triflate or [LFe]OTf, detailed overview |
698273 |
| 4.2.1.84 | -999 |
- |
more |
single turnover stopped-flow experiments and multiple turnover experiments with methacrylonitrile suggest a three-step kinetic model that allows for the reversible binding of substrate, the presence of an intermediate, and the formation of product, identification of catalytic Fe3+-nitrile intermediate species, kinetics, detaiiled overview |
730013 |
| 4.2.1.84 | -999 |
- |
more |
the enzymatic in vitro enzyme assay Michaelis-Menten kinetics does not give satisfactory results both for Km and for Vmax as saturation of the enzyme is not reached before the substrate aeroplysinin-1 precipitated at concentrations higher than 36 mM |
730311 |
| 4.2.1.84 | -999 |
- |
more |
the wild-type enzyme shows significantly lower Km values for aromatic substrates than for aliphatic ones |
648457 |
| 4.2.1.84 | -999 |
- |
more |
thermodynamics |
697734 |
| 4.2.1.84 | -999 |
- |
more |
values for 12 different substrates, affinity increases as the side chain of the substrate becomes longer |
648426 |
