EC Number   |
KM Value [mM] |
KM Value Maximum [mM] |
Substrate |
Reference |
|---|
    4.1.1.1 | -999 |
- |
more |
kinetics analysis of the wild-type enzyme with beta-hydroxypyruvate as substrate in the decarboxylation reaction |
678576 |
| 4.1.1.1 | -999 |
- |
more |
pH-dependent kinetic data of wild-type, C221E/C222A and C221A/C222A double mutant YPDC |
650152 |
| 4.1.1.1 | -999 |
- |
more |
pre-steady-state and steady-state kinetics of recombinant wild-type and mutant enzymes, overview |
678162 |
| 4.1.1.1 | -999 |
- |
more |
steady-state kinetic analysis, overview. The v/[S] plots display negative cooperativity and hence deviate from Michaelis-Menten kinetics in just the opposite way |
727473 |
| 4.1.1.1 | -999 |
- |
more |
steady-state kinetic parameters for beta-hydroxypyruvate |
678579 |
| 4.1.1.1 | -999 |
- |
more |
the isozyme shows sigmoidal kinetics with a Hill coefficient of 1.8 |
679569 |
| 4.1.1.1 | -999 |
- |
more |
the recombinant enzyme expressed in Geobacillus thermoglucosidasius shows normal Michaelis-Menten kinetics with pyruvate |
726787 |
| 4.1.1.1 | -999 |
- |
more |
transient state, pre-steady-state, and steady-state complex formations of substrate/intermediate and thiamine diphosphate cofactor and of kinetics of wild-type and mutant enzymes, overview |
727679 |
| 4.1.1.1 | -999 |
- |
more |
values for several C-terminal deletion mutants, kinetic model of the catalytic cycle |
650009 |
| 4.1.1.1 | 0.02 |
- |
pyruvate |
mutant enzyme A287G, at pH 6.0 and 30°C |
740088 |
