“4-phosphoerythronate dehydrogenase”的意思、由来-开放百科全书

词条

4-phosphoerythronate dehydrogenase

释义

Structural studies
References

{{enzyme
| Name = 4-phosphoerythronate dehydrogenase
| EC_number = 1.1.1.290
| CAS_number =
| IUBMB_EC_number = 1/1/1/290
| GO_code =
| image =
| width =
| caption =
}}

In enzymology, a 4-phosphoerythronate dehydogenase ({{EC number|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

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

References

{{cite journal | vauthors = Lam HM, Winkler ME | date = 1990 | title = Metabolic relationships between pyridoxine (vitamin B6) and serine biosynthesis in Escherichia coli K-12 | journal = J. Bacteriol. | volume = 172 | pages = 6518–28 | pmid = 2121717 | issue = 11 | pmc = 526841 }}
{{cite journal | vauthors = Pease AJ, Roa BR, Luo W, Winkler ME | date = 2002 | title = Positive growth rate-dependent regulation of the pdxA, ksgA, and pdxB genes of Escherichia coli K-12 | journal = J. Bacteriol. | volume = 184 | pages = 1359–69 | pmid = 11844765 | doi = 10.1128/JB.184.5.1359-1369.2002 | issue = 5 | pmc = 134838 }}
{{cite journal | vauthors = Zhao G, Winkler ME | date = 1996 | title = 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 | journal = J. Bacteriol. | volume = 178 | pages = 232–9 | pmid = 8550422 | issue = 1 | pmc = 177644 }}
{{cite journal | author = Grant GA | date = 1989 | title = A new family of 2-hydroxyacid dehydrogenases | journal = Biochem. Biophys. Res. Commun. | volume = 165 | pages = 1371–4 | pmid = 2692566 | doi = 10.1016/0006-291X(89)92755-1 | issue = 3 }}
{{cite journal | vauthors = Schoenlein PV, Roa BB, Winkler ME | date = 1989 | title = Divergent transcription of pdxB and homology between the pdxB and serA gene products in Escherichia coli K-12 | journal = J. Bacteriol. | volume = 171 | pages = 6084–92 | pmid = 2681152 | issue = 11 | pmc = 210475 }}

3 : EC 1.1.1|NADH-dependent enzymes|Enzymes of known structure

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