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Your query returned 5 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 | ||||||||||||
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EC | 4.1.2.42 | ||||||||||||
Accepted name: | D-threonine aldolase | ||||||||||||
Reaction: | (1) D-threonine = glycine + acetaldehyde (2) D-allo-threonine = glycine + acetaldehyde |
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Glossary: | D-threonine = (2R,3S)-2-amino-3-hydroxybutanoic acid D-allo-threonine = (2R,3R)-2-amino-3-hydroxybutanoic acid |
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Other name(s): | D-TA; DTA; low specificity D-TA; low specificity D-threonine aldolase | ||||||||||||
Systematic name: | D-threonine acetaldehyde-lyase (glycine-forming) | ||||||||||||
Comments: | A pyridoxal-phosphate protein that is activated by divalent metal cations (e.g. Co2+, Ni2+, Mn2+ or Mg2+) [1,2]. The reaction is reversible, which can lead to the interconversion of D-threonine and D-allo-threonine [1]. Several other D-β-hydroxy-α-amino acids, such as D-β-phenylserine, D-β-hydroxy-α-aminovaleric acid and D-β-3,4-dihydroxyphenylserine, can also act as substrate [1]. | ||||||||||||
Links to other databases: | BRENDA, EXPASY, KEGG, MetaCyc, PDB | ||||||||||||
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EC | 4.1.3.41 | ||||||||||||
Accepted name: | 3-hydroxy-D-aspartate aldolase | ||||||||||||
Reaction: | (1) threo-3-hydroxy-D-aspartate = glycine + glyoxylate (2) D-erythro-3-hydroxyaspartate = glycine + glyoxylate |
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Other name(s): | D-3-hydroxyaspartate aldolase | ||||||||||||
Systematic name: | 3-hydroxy-D-aspartate glyoxylate-lyase (glycine-forming) | ||||||||||||
Comments: | A pyridoxal-phosphate protein. The enzyme, purified from the bacterium Paracoccus denitrificans IFO 13301, is strictly D-specific as to the α-position of the substrate, but accepts both the threo and erythro forms at the β-position. The erythro form is a far better substrate (about 100-fold). The enzyme can also accept D-allothreonine, D-threonine, erythro-3-phenyl-D-serine and threo-3-phenyl-D-serine. Different from EC 4.1.3.14, erythro-3-hydroxy-L-aspartate aldolase. Requires a divalent cation, such as Mg2+, Mn2+ or Co2+. | ||||||||||||
Links to other databases: | BRENDA, EXPASY, KEGG, MetaCyc, PDB | ||||||||||||
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EC | 4.3.1.18 | ||||||||||||
Accepted name: | D-serine ammonia-lyase | ||||||||||||
Reaction: | D-serine = pyruvate + NH3 (overall reaction) (1a) D-serine = 2-aminoprop-2-enoate + H2O (1b) 2-aminoprop-2-enoate = 2-iminopropanoate (spontaneous) (1c) 2-iminopropanoate + H2O = pyruvate + NH3 (spontaneous) |
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Other name(s): | D-hydroxyaminoacid dehydratase; D-serine dehydrase; D-hydroxy amino acid dehydratase; D-serine hydrolase; D-serine dehydratase (deaminating); D-serine deaminase; D-serine hydro-lyase (deaminating) | ||||||||||||
Systematic name: | D-serine ammonia-lyase (pyruvate-forming) | ||||||||||||
Comments: | A pyridoxal-phosphate protein. The enzyme cleaves a carbon-oxygen bond, releasing a water molecule (hence the enzyme’s original classification as EC 4.2.1.14, D-serine dehydratase) and an unstable enamine product that tautomerizes to an imine form, which undergoes a hydrolytic deamination to form pyruvate and ammonia. The latter reaction, which can occur spontaneously, can also be catalysed by EC 3.5.99.10, 2-iminobutanoate/2-iminopropanoate deaminase. Also acts, slowly, on D-threonine. | ||||||||||||
Links to other databases: | BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9015-88-7 | ||||||||||||
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EC | 5.1.1.6 | ||||||||||||
Accepted name: | threonine racemase | ||||||||||||
Reaction: | L-threonine = D-threonine | ||||||||||||
Glossary: | D-threonine = (2R,3S)-2-amino-3-hydroxybutanoic acid | ||||||||||||
Systematic name: | threonine racemase | ||||||||||||
Comments: | Inverts both chiral centres. | ||||||||||||
Links to other databases: | BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 9024-11-7 | ||||||||||||
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