EC Number   |
KM Value [mM] |
KM Value Maximum [mM] |
Substrate |
Reference |
|---|
    2.5.1.65 | -999 |
- |
more |
- |
637385 |
| 2.5.1.65 | -999 |
- |
more |
kinetics |
655576 |
| 2.5.1.65 | -999 |
- |
more |
ping-pong bi-bi mechanism |
655576 |
| 2.5.1.65 | -999 |
- |
more |
steady-state kinetics, the Km value toward O-phospho-L-serine is not significantly different between the wild-type ApOPSS and the F225A mutant, the kcat value of the wild-type ApOPSS is 4.2fold higher toward O-phospho-L-serine and 15fold higher toward O-acetyl-L-erine than that of the F225A mutant, respectively |
738193 |
| 2.5.1.65 | -999 |
- |
more |
stopped-flow and Michaelis-Menten kinetic analysis, overview. The amino acrylate reaction intermediate is not stable and decomposes with a pseudo-first-order rate constant kobs of 0.12/s |
738534 |
| 2.5.1.65 | 0.044 |
- |
thiosulfate |
pH 7.0, 22°C, recombinant wild-type enzyme |
738534 |
| 2.5.1.65 | 0.135 |
- |
O-phospho-L-serine |
dephosphorylation, pH 7.0, 22°C, recombinant wild-type enzyme |
738534 |
| 2.5.1.65 | 0.2 |
- |
Sulfide |
below, pH 6.7 |
637385 |
| 2.5.1.65 | 0.214 |
- |
thiosulfate |
pH 7.0, 22°C, recombinant mutant R243A enzyme |
738534 |
| 2.5.1.65 | 0.25 |
- |
hydrogen sulfide |
pH 7.6, 60°C, with O-acetyl-L-serine |
655576 |
