4-hydroxythreonine-4-phosphate dehydrogenase
From Wikipedia, the free encyclopedia
In enzymology, a 4-hydroxythreonine-4-phosphate dehydrogenase (EC 1.1.1.262) is an enzyme that catalyzes the chemical reaction
- 4-phosphonooxy-L-threonine + NAD+ (2S)-2-amino-3-oxo-4-phosphonooxybutanoate + NADH + H+
Thus, the two substrates of this enzyme are 4-phosphonooxy-L-threonine and NAD+, whereas its 3 products are (2S)-2-amino-3-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-phosphonooxy-L-threonine:NAD+ oxidoreductase. Other names in common use include NAD+-dependent threonine 4-phosphate dehydrogenase, L-threonine 4-phosphate dehydrogenase, 4-(phosphohydroxy)-L-threonine dehydrogenase, PdxA, and 4-(phosphonooxy)-L-threonine:NAD+ oxidoreductase. This enzyme participates in vitamin b6 metabolism.
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[edit] Structural studies
As of late 2007, 6 structures have been solved for this class of enzymes, with PDB accession codes 1PS6, 1PS7, 1PTM, 1R8K, 1YXO, and 2HI1.
[edit] References
- IUBMB entry for 1.1.1.262
- BRENDA references for 1.1.1.262 (Recommended.)
- PubMed references for 1.1.1.262
- PubMed Central references for 1.1.1.262
- Google Scholar references for 1.1.1.262
- ID (1998). "Biosynthesis of vitamine B6: The oxidation of L-threonine 4-phosphate by PdxA". J. Am. Chem. Soc. 120: 1936–1937.
- Laber B, Maurer W, Scharf S, Stepusin K, Schmidt FS (1999). "Vitamin B6 biosynthesis: formation of pyridoxine 5'-phosphate from 4-(phosphohydroxy)-L-threonine and 1-deoxy-D-xylulose-5-phosphate by PdxA and PdxJ protein". FEBS. Lett. 449: 45–8. PMID 10225425.
- Sivaraman J, Li Y, Banks J, Cane DE, Matte A, Cygler M (2003). "Crystal structure of Escherichia coli PdxA, an enzyme involved in the pyridoxal phosphate biosynthesis pathway". J. Biol. Chem. 278: 43682–90. PMID 12896974.