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Information on EC 1.1.1.381 - 3-hydroxy acid dehydrogenase

for references in articles please use BRENDA:EC1.1.1.381
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IUBMB 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 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).
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The enzyme appears in viruses and cellular organisms
Reaction Schemes
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Synonyms
ymr226c, 3-hydroxy acid dehydrogenase, more
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
L-2-amino-3-oxobutanoate = aminoacetone + CO2
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(1b), spontaneous
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0
L-allo-threonine + NADP+ = aminoacetone + CO2 + NADPH + H+
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overall reaction
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0
L-allo-threonine + NADP+ = L-2-amino-3-oxobutanoate + NADPH + H+
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(1a)
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0
PATHWAY SOURCE
PATHWAYS
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