Expasy logo

ENZYME

ENZYME entry: EC 1.1.1.381

PURL: https://purl.expasy.org/enzyme/EC/1.1.1.381
Accepted Name
3-hydroxy acid dehydrogenase
Reaction catalysed
L-allo-threonine + NADP(+) = aminoacetone + CO2 + 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
KEGG Ligand Database for Enzyme Nomenclature1.1.1.381
IUBMB Enzyme Nomenclature1.1.1.381
MEDLINEFind literature relating to 1.1.1.381
MetaCyc1.1.1.381
Rhea expert-curated reactions1.1.1.381
UniProtKB/Swiss-Prot
Q8X505, YDFG_ECO57Q8FHD2, YDFG_ECOL6P39831, YDFG_ECOLI
P69935, YDFG_SALTIP69936, YDFG_SALTYQ83RE8, YDFG_SHIFL
Q9P7B4, YI13_SCHPOQ05016, YM71_YEAST

View entry in original ENZYME format
View entry in raw text format (no links)
All UniProtKB/Swiss-Prot entries referenced in this entry, with possibility to download in different formats, align etc.
All ENZYME / UniProtKB/Swiss-Prot entries corresponding to 1.1.1.-
All ENZYME / UniProtKB/Swiss-Prot entries corresponding to 1.1.-.-
All ENZYME / UniProtKB/Swiss-Prot entries corresponding to 1.-.-.-