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Your query returned 4 entries. Printable version
EC | 1.1.1.381 | ||||||||||
Accepted name: | 3-hydroxy acid dehydrogenase | ||||||||||
Reaction: | L-allo-threonine + NADP+ = aminoacetone + CO2 + NADPH + H+ (overall reaction) (1a) L-allo-threonine + NADP+ = L-2-amino-3-oxobutanoate + NADPH + H+ (1b) L-2-amino-3-oxobutanoate = aminoacetone + CO2 (spontaneous) |
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Glossary: | L-allo-threonine = (2S,3S)-2-amino-3-hydroxybutanoic acid aminoacetone = 1-aminopropan-2-one L-2-amino-3-oxobutanoate = (2S)-2-amino-3-oxobutanoate |
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Other name(s): | ydfG (gene name); YMR226c (gene name) | ||||||||||
Systematic name: | L-allo-threonine:NADP+ 3-oxidoreductase | ||||||||||
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). | ||||||||||
Links to other databases: | BRENDA, EXPASY, KEGG, MetaCyc, PDB | ||||||||||
References: |
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EC | 4.1.2.5 | ||||||||||
Accepted name: | L-threonine aldolase | ||||||||||
Reaction: | L-threonine = glycine + acetaldehyde | ||||||||||
Other name(s): | L-threonine acetaldehyde-lyase | ||||||||||
Systematic name: | L-threonine acetaldehyde-lyase (glycine-forming) | ||||||||||
Comments: | A pyridoxal-phosphate protein. This enzyme is specific for L-threonine and can not utilize L-allo-threonine. Different from EC 4.1.2.49, L-allo-threonine aldolase, and EC 4.1.2.48, low-specificity L-threonine aldolase. | ||||||||||
Links to other databases: | BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 62213-23-4 | ||||||||||
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EC | 4.1.2.48 | ||||||||||
Accepted name: | low-specificity L-threonine aldolase | ||||||||||
Reaction: | (1) L-threonine = glycine + acetaldehyde (2) L-allo-threonine = glycine + acetaldehyde |
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Other name(s): | LtaE | ||||||||||
Systematic name: | L-threonine/L-allo-threonine acetaldehyde-lyase (glycine-forming) | ||||||||||
Comments: | Requires pyridoxal phosphate. The low-specificity L-threonine aldolase can act on both L-threonine and L-allo-threonine [1,2]. The enzyme from Escherichia coli can also act on L-threo-phenylserine and L-erythro-phenylserine [4]. The enzyme can also catalyse the aldol condensation of glycolaldehyde and glycine to form 4-hydroxy-L-threonine, an intermediate of pyridoxal phosphate biosynthesis [3]. Different from EC 4.1.2.5, L-threonine aldolase, and EC 4.1.2.49, L-allo-threonine aldolase. | ||||||||||
Links to other databases: | BRENDA, EXPASY, KEGG, MetaCyc, PDB | ||||||||||
References: |
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EC | 4.1.2.49 | ||||||||||
Accepted name: | L-allo-threonine aldolase | ||||||||||
Reaction: | L-allo-threonine = glycine + acetaldehyde | ||||||||||
Systematic name: | L-allo-threonine acetaldehyde-lyase (glycine-forming) | ||||||||||
Comments: | Requires pyridoxal phosphate. This enzyme, characterized from the bacterium Aeromonas jandaei, is specific for L-allo-threonine and can not act on either L-threonine or L-serine. Different from EC 4.1.2.5, L-threonine aldolase, and EC 4.1.2.48, low-specificity L-threonine aldolase. A previously listed enzyme with this name, EC 4.1.2.6, was deleted in 1971 after it was found to be identical to EC 2.1.2.1, glycine hydroxymethyltransferase. | ||||||||||
Links to other databases: | BRENDA, EXPASY, KEGG, MetaCyc, PDB | ||||||||||
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