ENZYME entry: EC 1.1.1.381

Accepted Name
3-hydroxy acid dehydrogenase.
Reaction catalysed
L-allo-threonine + NADP(+) <=> aminoacetone + CO(2) + NADPH
Comment(s)
  • 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).
Cross-references
BRENDA1.1.1.381
EC2PDB1.1.1.381
ExplorEnz1.1.1.381
PRIAM enzyme-specific profiles1.1.1.381
KEGG Ligand Database for Enzyme Nomenclature1.1.1.381
IUBMB Enzyme Nomenclature1.1.1.381
IntEnz1.1.1.381
MEDLINEFind literature relating to 1.1.1.381
MetaCyc1.1.1.381
UniProtKB/Swiss-Prot
Q8X505, YDFG_ECO57;  Q8FHD2, YDFG_ECOL6;  P39831, YDFG_ECOLI;  
P69935, YDFG_SALTI;  P69936, YDFG_SALTY;  Q83RE8, YDFG_SHIFL;  
Q9P7B4, YI13_SCHPO;  Q05016, YM71_YEAST;  

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