4-phosphoerythronate dehydrogenase
| 4-phosphoerythronate dehydrogenase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 1.1.1.290 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
In enzymology, a 4-phosphoerythronate dehydogenase (EC 1.1.1.290) is an enzyme that catalyzes the chemical reaction
- 4-phospho-D-erythronate + NAD+ (3R)-3-hydroxy-2-oxo-4-phosphonooxybutanoate + NADH + H+
Thus, the two substrates of this enzyme are 4-phospho-D-erythronate and NAD+, whereas its 3 products are (3R)-3-hydroxy-2-oxo-4-phosphonooxybutanoate, NADH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is 4-phospho-D-erythronate:NAD+ 2-oxidoreductase. Other names in common use include PdxB, PdxB 4PE dehydrogenase, and 4-O-phosphoerythronate dehydrogenase. This enzyme participates in vitamin B6 metabolism.
Structural studies[edit]
As of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code 2O4C.
References[edit]
- Lam HM, Winkler ME (1990). "Metabolic relationships between pyridoxine (vitamin B6) and serine biosynthesis in Escherichia coli K-12". J. Bacteriol. 172 (11): 6518–28. doi:10.1128/jb.172.11.6518-6528.1990. PMC 526841. PMID 2121717.
- Pease AJ, Roa BR, Luo W, Winkler ME (2002). "Positive growth rate-dependent regulation of the pdxA, ksgA, and pdxB genes of Escherichia coli K-12". J. Bacteriol. 184 (5): 1359–69. doi:10.1128/JB.184.5.1359-1369.2002. PMC 134838. PMID 11844765.
- Zhao G, Winkler ME (1996). "A novel alpha-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 (1): 232–9. doi:10.1128/jb.178.1.232-239.1996. PMC 177644. PMID 8550422.
- Grant GA (1989). "A new family of 2-hydroxyacid dehydrogenases". Biochem. Biophys. Res. Commun. 165 (3): 1371–4. doi:10.1016/0006-291X(89)92755-1. PMID 2692566.
- Schoenlein PV, Roa BB, Winkler ME (1989). "Divergent transcription of pdxB and homology between the pdxB and serA gene products in Escherichia coli K-12". J. Bacteriol. 171 (11): 6084–92. doi:10.1128/jb.171.11.6084-6092.1989. PMC 210475. PMID 2681152.
