4-phosphoerythronate dehydrogenase

From Wikipedia, the free encyclopedia

In enzymology, a 4-phosphoerythronate dehydogenase (EC 1.1.1.290) is an enzyme that catalyzes the chemical reaction

4-phospho-D-erythronate + NAD⁺ $\rightleftharpoons$ (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.

[edit] Structural studies

As of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code 2O4C.

[edit] References

IUBMB entry for 1.1.1.290
BRENDA references for 1.1.1.290 (Recommended.)
PubMed references for 1.1.1.290
PubMed Central references for 1.1.1.290
Google Scholar references for 1.1.1.290
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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: 1359–69. 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: 232–9. PMID 8550422.
Grant GA (1989). "A new family of 2-hydroxyacid dehydrogenases". Biochem. Biophys. Res. Commun. 165: 1371–4. 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: 6084–92. PMID 2681152.