EC Number   |
KM Value [mM] |
KM Value Maximum [mM] |
Substrate |
Reference |
|---|
    2.8.4.1 | -999 |
- |
more |
steady-state and rapid kinetics, MCRred1-catalyzed cleavage of the C-S bond of methyl-SCoM requires the other substrate, HSCoB, even under single turnover conditions |
674693 |
| 2.8.4.1 | -999 |
- |
more |
steady-state kinetics of MCRred1 with brominated acids, overview |
672222 |
| 2.8.4.1 | -999 |
- |
more |
stopped flow kinetics, overview |
690930 |
| 2.8.4.1 | -999 |
- |
more |
transient kinetic, spectroscopic [ultraviolet-visible (UV-Vis), EPR, and MCD], and computational studies of the first step in the MCR catalytic mechanism are performed to trap and identify the key intermediates that differ between proposed mechanisms I and II, detailed overview. Rapid kinetic studies rule out methyl-Ni(III) and trap the MCRox1-silent intermediate |
762467 |
| 2.8.4.1 | -999 |
- |
more |
transient kinetics study, overview |
672222 |
| 2.8.4.1 | 0.0033 |
- |
methyl coenzyme M |
- |
393251 |
| 2.8.4.1 | 0.016 |
- |
HS-CoB8 |
pH 10.0, 25°C |
690930 |
| 2.8.4.1 | 0.023 |
- |
coenzyme B |
- |
393252 |
| 2.8.4.1 | 0.03 |
- |
CH3-S-CoM |
with SH-CoB6 as cosubstrate, pH not specified in the publication, at 25°C |
724279 |
| 2.8.4.1 | 0.059 |
- |
coenzyme B |
- |
393251 |
