EC Number   |
Turnover Number Minimum [1/s] |
Turnover Number Maximum [1/s] |
Substrate |
Reference |
|---|
   4.3.1.7 | -999 |
- |
more |
Comparison of the rates of steady-state turnover of coenzyme B12-dependent enzymes (kcat 10-100 1/s at 25°C) with the rate of cleavage of the cobalt-carbon bond of coenzyme B12 in solution reveals that the enzyme increases the cleavage rate more than 100000000000fold |
692764 |
| 4.3.1.7 | -999 |
- |
more |
mutant R160A displays no detectable catalytic turnover with ethanolamine as subtrate |
690960 |
| 4.3.1.7 | -999 |
- |
more |
the steady-state accumulation, and subsequent cryotrapping, of the Co2-substrate radical pair as the only detectable paramagnetic intermediate, suggest that the step after Co2-substrate radical pair formation is at least partially rate limiting for steady-state turnover |
691337 |
| 4.3.1.7 | 0.036 |
- |
ethanolamine |
run 1, pH 8, 37°C, mutant E287A |
729253 |
| 4.3.1.7 | 0.038 |
- |
ethanolamine |
run 2, pH 8, 37°C, mutant D362N |
729253 |
| 4.3.1.7 | 0.051 |
- |
ethanolamine |
run 2, pH 8, 37°C, mutant Q162K |
729253 |
| 4.3.1.7 | 0.066 |
- |
ethanolamine |
run 2, pH 8, 37°C, mutant E287H |
729253 |
| 4.3.1.7 | 0.067 |
- |
(R)-2-aminopropanol |
- |
680355 |
| 4.3.1.7 | 0.085 |
- |
ethanolamine |
run 1, pH 8, 37°C, mutant D362A |
729253 |
| 4.3.1.7 | 0.086 |
- |
ethanolamine |
run 2, pH 8, 37°C, mutant E287Q |
729253 |
