EC Number   |
KM Value [mM] |
KM Value Maximum [mM] |
Substrate |
Reference |
|---|
   3.5.1.93 | -999 |
- |
7-aminocephalosporanic acid |
estimated value: 9.43 mg/ml, pH 7.6, 34°C, Vmax: 7.65 U/ml |
711051 |
| 3.5.1.93 | -999 |
- |
more |
kinetics of wild-type and mutant enzymes with cephalosporin C, overview |
733836 |
| 3.5.1.93 | -999 |
- |
more |
Michaelis constant (Km) and maximum reaction velocity (Vmax) for the free and immobilized enzyme are calculated according to Lineweaver-Burk plots |
755927 |
| 3.5.1.93 | -999 |
- |
more |
Michaelis-Menten kinetics of free and immobilized wild-type and mutant enzymes, overview |
733139 |
| 3.5.1.93 | -999 |
- |
more |
substrate binding to the protein surface follows a Langmuir model resulting in binding constants K = 7.4 and 9.2 mM for wild-type and mutant M6 enzymes, respectively, which are similar to the experimentally determined Michaelis constants, thermodynamics, overview |
758446 |
| 3.5.1.93 | -999 |
- |
more |
the apparent Km value of CPC acylase increases and Vmax is almost unaffected in the presence of 7-aminocephalosporanic acid |
713590 |
| 3.5.1.93 | 0.016 |
- |
glutaryl-7-aminocephalosporanic acid |
pH 7.5, 37°C, mutant enzyme N266H |
662118 |
| 3.5.1.93 | 0.031 |
- |
glutaryl-7-aminocephalosporanic acid |
pH 7.5, 37°C, wild-type enzyme |
660863 |
| 3.5.1.93 | 0.031 |
- |
glutaryl-7-aminocephalosporanic acid |
wild-type enzyme |
661484 |
| 3.5.1.93 | 0.033 |
- |
glutaryl-7-aminocephalosporanic acid |
pH 7.5, 37°C, wild-type enzyme |
662118 |
