EC 1 - Oxidoreductases
EC 1.1 - Acting on the CH-OH group of donors
EC 1.1.1 - With NAD+ or NADP+ as acceptor
EC 1.1.1.381 - 3-hydroxy acid dehydrogenase
IntEnz view
ENZYME view
IntEnz Enzyme Nomenclature
EC 1.1.1.381
Names
Accepted name:
3-hydroxy acid dehydrogenase
Other
names:
ydfG (gene name)
YMR226c (gene name)
YMR226c (gene name)
Systematic name:
L-allo-threonine:NADP+ 3-oxidoreductase
Reactions
- (1) L-allo-threonine + NADP+ = aminoacetone + CO2 + NADPH + H+
- (1a) L-allo-threonine + NADP+ = L-2-amino-3-oxobutanoate + NADPH + H+
- (1b) L-2-amino-3-oxobutanoate = aminoacetone + CO2 (spontaneous)
Comments:
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 E. 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).
Links to other databases
UniProtKB/Swiss-Prot:
YDFG_ECO57
YDFG_ECOL6
YDFG_ECOLI
YDFG_SALTI
YDFG_SALTY
YDFG_SHIFL
YI13_SCHPO
YM71_YEAST
References
-
Characterization of short-chain dehydrogenase/reductase homologues of Escherichia coli (YdfG) and Saccharomyces cerevisiae (YMR226C).Biochim. Biophys. Acta 1645 : 89-94 (2003). [PMID: 12535615]
[EC 1.1.1.381 created 2014]