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 expected taxonomic range for this enzyme is: Bacteria, Eukaryota
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SYSTEMATIC NAME
IUBMB Comments
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).
highest Vmax/Km value of all substrates tested. The hydroxyl group of L-allo-threonine is oxidized by the enzymes to yield L-2-amino-3-ketobutyrate, which is spontaneously decarboxylated into aminoacetone
highest Vmax/Km value of all substrates tested. The hydroxyl group of L-allo-threonine is oxidized by the enzymes to yield L-2-amino-3-oxobutyrate, which is spontaneously decarboxylated into aminoacetone
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Enzyme Nomenclature
1.1.1.381 3-hydroxy acid dehydrogenase
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