EC 1.1.1.381: 3-hydroxy acid dehydrogenase
This is an abbreviated version!
For detailed information about 3-hydroxy acid dehydrogenase, go to the full flat file.
Reaction
Synonyms
ydfG, YMR226c
ECTree
Advanced search results
| Results | in table |
|---|---|
| 2602 | AA Sequence |
| 2 | Cloned(Commentary) |
| 2 | Cofactor |
| 15 | kcat/KM [mM/s] |
| 16 | KM Value [mM] |
| 3 | Organism |
| 2 | Pathway |
| 2 | pH Optimum |
| 2 | pH Stability |
| 2 | Purification (Commentary) |
| 3 | Reaction |
| 3 | Reference |
| 2 | Specific Activity [micromol/min/mg] |
| 20 | Substrates and Products (Substrate) |
| 4 | Synonyms |
| 1 | Systematic Name |
| 2 | Temperature Optimum [°C] |
| 2 | Temperature Stability [°C] |
| 15 | Turnover Number [1/s] |
Systematic Name
Systematic Name on EC 1.1.1.381 - 3-hydroxy acid dehydrogenase
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
L-allo-threonine:NADP+ 3-oxidoreductase
The enzyme, purified from the bacterium Escherichia coli and the yeast Saccharomyces cerevisiae, shows activity with a range of 3- and 4-carbon 3-hydroxy acids. The highest activity is seen with L-allo-threonine and D-threonine. The enzyme from Escherichia coli also shows high activity with L-serine, D-serine, (S)-3-hydroxy-2-methylpropanoate and (R)-3-hydroxy-2-methylpropanoate. The enzyme has no activity with NAD+ or L-threonine (cf. EC 1.1.1.103, L-threonine 3-dehydrogenase).

results (
results (
top




