EC |
1.1.1.290 |
Accepted name: |
4-phosphoerythronate dehydrogenase |
Reaction: |
4-phospho-D-erythronate + NAD+ = (3R)-3-hydroxy-2-oxo-4-phosphooxybutanoate + NADH + H+ |
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For diagram of pyridoxal biosynthesis, click here |
Other name(s): |
PdxB; PdxB 4PE dehydrogenase; 4-O-phosphoerythronate dehydrogenase; 4PE dehydrogenase; erythronate-4-phosphate dehydrogenase |
Systematic name: |
4-phospho-D-erythronate:NAD+ 2-oxidoreductase |
Comments: |
This enzyme catalyses a step in a bacterial pathway for the biosynthesis of pyridoxal 5′-phosphate. The enzyme contains a tightly-bound NAD(H) cofactor that is not re-oxidized by free NAD+. In order to re-oxidize the cofactor and restore enzyme activity, the enzyme catalyses the reduction of a 2-oxo acid (such as 2-oxoglutarate, oxaloacetate, or pyruvate) to the respective (R)-hydroxy acid [6]. cf. EC 1.1.1.399, 2-oxoglutarate reductase. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 125858-75-5 |
References: |
1. |
Lam, H.M. and Winkler, M.E. Metabolic relationships between pyridoxine (vitamin B6) and serine
biosynthesis in Escherichia coli K-12. J. Bacteriol. 172 (1990) 6518–6528. [DOI] [PMID: 2121717] |
2. |
Pease, A.J., Roa, B.R., Luo, W. and Winkler, M.E. Positive growth rate-dependent regulation of the pdxA, ksgA, and pdxB genes of Escherichia coli K-12. J. Bacteriol. 184 (2002) 1359–1369. [DOI] [PMID: 11844765] |
3. |
Zhao, G. and Winkler, M.E. A novel α-ketoglutarate reductase activity of the serA-encoded 3-phosphoglycerate dehydrogenase of Escherichia coli K-12 and its possible implications for human 2-hydroxyglutaric aciduria. J. Bacteriol. 178 (1996) 232–239. [DOI] [PMID: 8550422] |
4. |
Grant, G.A. A new family of 2-hydroxyacid dehydrogenases. Biochem. Biophys. Res. Commun. 165 (1989) 1371–1374. [DOI] [PMID: 2692566] |
5. |
Schoenlein, P.V., Roa, B.B. and Winkler, M.E. Divergent transcription of pdxB and homology between the pdxB and serA gene products in Escherichia coli K-12. J. Bacteriol. 171 (1989) 6084–6092. [DOI] [PMID: 2681152] |
6. |
Rudolph, J., Kim, J. and Copley, S.D. Multiple turnovers of the nicotino-enzyme PdxB require α-keto acids as cosubstrates. Biochemistry 49 (2010) 9249–9255. [DOI] [PMID: 20831184] |
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[EC 1.1.1.290 created 2006, modified 2016] |
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