1.1.1.290: 4-phosphoerythronate dehydrogenase
This is an abbreviated version!
For detailed information about 4-phosphoerythronate dehydrogenase, go to the full flat file.
Word Map on EC 1.1.1.290
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1.1.1.290
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2-hydroxyacid
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pyridoxine
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salvage
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dehydrogenases
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aeruginosa
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homodimeric
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pyridoxal
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5'-phosphate
- 1.1.1.290
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2-hydroxyacid
- pyridoxine
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salvage
- dehydrogenases
- aeruginosa
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homodimeric
- pyridoxal
- 5'-phosphate
Reaction
Synonyms
4-O-phosphoerythronate dehydrogenase, D-erythronate-4-phosphate dehydrogenase, erythronate-4-phosphate dehydrogenase, More, pdx gene product, PDXB, PdxB 4PE dehydrogenase, RdxB
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Substrates Products
Substrates Products on EC 1.1.1.290 - 4-phosphoerythronate dehydrogenase
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REACTION DIAGRAM
2-oxoglutarate + NADH + H+
L-2-hydroxyglutarate + NAD+
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stereospecific reaction
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?
4-phospho-D-erythronate + NAD+
2-oxo-3-hydroxy-4-phospho-butanoate + NADH + H+
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multiple turnovers requiring 2-oxo acids for re-oxidation of NADH bound to the enzyme PdxB a coupled assay with the enzymes SerC and PdxA following in the bioyntetic pathway, overview
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erythronate-4-phosphate + NAD+
(3R)-3-hydroxy-2-oxo-4-phosphonooxybutanoate + NADH
reaction in pathway leading from erythrose-4-phosphate and glutamate to nitrogen 1 and carbon 5,5', and 6 of the pyridoxine ring
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erythronate-4-phosphate + NAD+
3-hydroxy-4-phospho-hydroxy-alpha-ketobutyrate + NADH
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(3R)-3-hydroxy-2-oxo-4-phosphooxybutanoate + NADH
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4-phospho-D-erythronate + NAD+
(3R)-3-hydroxy-2-oxo-4-phosphooxybutanoate + NADH
the enzyme is involved in biosynthesis of pyridoxal-5'-phosphate
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?
2-oxo-3-hydroxy-4-phospho-butanoate + NADH
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4-phospho-D-erythronate + NAD+
2-oxo-3-hydroxy-4-phospho-butanoate + NADH
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?
3-hydroxy-2-oxo-4-(phosphonooxy)butanoate + NADH + H+
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r
4-phospho-D-erythronate + NAD+
3-hydroxy-2-oxo-4-(phosphonooxy)butanoate + NADH + H+
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r
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pdxB is the first gene in the pdxB-hisT operon
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additional information
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the enzyme mediates a step in the biosynthesis of the coenzyme pyridoxal 5'-phosphate. Transcription of pdxB gene is positively growth rate regulated. PdxB-specific transcript remains unchanged during amino acid starvation in wild-type and relA mutant strains
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additional information
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2,6-dichloroindolphenol, N-nitrosodimethylamine, and methylene blue cannot be reduced in the presence of the enzyme and 4-phospho-D-erythronate
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additional information
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2-oxoglutarate, oxaloacetic acid, and pyruvate are equally good subtrates for the enzyme
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additional information
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2,6-dichloroindolphenol, N-nitrosodimethylamine, and methylene blue cannot be reduced in the presence of the enzyme and 4-phospho-D-erythronate
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additional information
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2-oxoglutarate, oxaloacetic acid, and pyruvate are equally good subtrates for the enzyme
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additional information
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active site and ligand binding structure, overview
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additional information
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active site and ligand binding structure, overview
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