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Your query returned 4 entries. Printable version
EC | 1.1.1.75 | ||||||||
Accepted name: | (R)-aminopropanol dehydrogenase | ||||||||
Reaction: | (R)-1-aminopropan-2-ol + NAD+ = aminoacetone + NADH + H+ | ||||||||
Other name(s): | L-aminopropanol dehydrogenase; 1-aminopropan-2-ol-NAD+ dehydrogenase; L(+)-1-aminopropan-2-ol:NAD+ oxidoreductase; 1-aminopropan-2-ol-dehydrogenase; DL-1-aminopropan-2-ol: NAD+ dehydrogenase; L(+)-1-aminopropan-2-ol-NAD/NADP oxidoreductase | ||||||||
Systematic name: | (R)-1-aminopropan-2-ol:NAD+ oxidoreductase | ||||||||
Comments: | Requires K+. | ||||||||
Links to other databases: | BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 37250-13-8 | ||||||||
References: |
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EC | 1.1.1.103 | ||||||||
Accepted name: | L-threonine 3-dehydrogenase | ||||||||
Reaction: | L-threonine + NAD+ = L-2-amino-3-oxobutanoate + NADH + H+ | ||||||||
Other name(s): | L-threonine dehydrogenase; threonine 3-dehydrogenase; threonine dehydrogenase; TDH | ||||||||
Systematic name: | L-threonine:NAD+ oxidoreductase | ||||||||
Comments: | This enzyme acts in concert with EC 2.3.1.29, glycine C-acetyltransferase, in the degradation of threonine to glycine. This threonine-degradation pathway is common to prokaryotic and eukaryotic cells and the two enzymes involved form a complex [2]. In aqueous solution, the product L-2-amino-3-oxobutanoate can spontaneously decarboxylate to form aminoacetone. | ||||||||
Links to other databases: | BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9067-99-6 | ||||||||
References: |
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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 | ||||||||
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EC | 2.3.1.29 | ||||||||
Accepted name: | glycine C-acetyltransferase | ||||||||
Reaction: | acetyl-CoA + glycine = CoA + L-2-amino-3-oxobutanoate | ||||||||
Other name(s): | 2-amino-3-ketobutyrate CoA ligase; 2-amino-3-ketobutyrate coenzyme A ligase; 2-amino-3-ketobutyrate-CoA ligase; glycine acetyltransferase; aminoacetone synthase; aminoacetone synthetase; KBL; AKB ligase | ||||||||
Systematic name: | acetyl-CoA:glycine C-acetyltransferase | ||||||||
Comments: | This is a pyridoxal-phosphate-dependent enzyme that acts in concert with EC 1.1.1.103, L-threonine 3-dehydrogenase, in the degradation of threonine to form glycine [3]. This threonine degradation pathway is common to prokaryotic and eukaryotic cells and the two enzymes involved form a complex [4]. | ||||||||
Links to other databases: | BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 37257-11-7 | ||||||||
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