In enzymology, a 4-hydroxythreonine-4-phosphate dehydrogenase (EC 1.1.1.262) is an enzyme that catalyzes the chemical reaction
| 4-hydroxythreonine-4-phosphate dehydrogenase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 1.1.1.262 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
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- 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.
Structural studies
editAs of late 2007, 6 structures have been solved for this class of enzymes, with PDB accession codes 1PS6, 1PS7, 1PTM, 1R8K, 1YXO, and 2HI1.
References
edit- ID; Hsiung, Yuju; Cornish, Julie A.; Robinson, J. Kenneth; Spenser, Ian D. (1998). "Biosynthesis of vitamine B6: The oxidation of L-threonine 4-phosphate by PdxA". J. Am. Chem. Soc. 120 (8): 1936–1937. doi:10.1021/ja9742085.1936-1937&rft.date=1998&rft_id=info:doi/10.1021/ja9742085&rft.au=ID&rft.au=Hsiung, Yuju&rft.au=Cornish, Julie A.&rft.au=Robinson, J. Kenneth&rft.au=Spenser, Ian D.&rfr_id=info:sid/en.wikipedia.org:4-hydroxythreonine-4-phosphate dehydrogenase" class="Z3988">
- 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 (1): 45–8. Bibcode:1999FEBSL.449...45L. doi:10.1016/S0014-5793(99)00393-2. PMID 10225425. S2CID 33542088.45-8&rft.date=1999&rft_id=info:doi/10.1016/S0014-5793(99)00393-2&rft_id=https://api.semanticscholar.org/CorpusID:33542088#id-name=S2CID&rft_id=info:pmid/10225425&rft_id=info:bibcode/1999FEBSL.449...45L&rft.aulast=Laber&rft.aufirst=B&rft.au=Maurer, W&rft.au=Scharf, S&rft.au=Stepusin, K&rft.au=Schmidt, FS&rft_id=https://doi.org/10.1016%2FS0014-5793%2899%2900393-2&rfr_id=info:sid/en.wikipedia.org:4-hydroxythreonine-4-phosphate dehydrogenase" class="Z3988">
- 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 (44): 43682–90. doi:10.1074/jbc.M306344200. PMID 12896974.43682-90&rft.date=2003&rft_id=info:doi/10.1074/jbc.M306344200&rft_id=info:pmid/12896974&rft.aulast=Sivaraman&rft.aufirst=J&rft.au=Li, Y&rft.au=Banks, J&rft.au=Cane, DE&rft.au=Matte, A&rft.au=Cygler, M&rft_id=https://doi.org/10.1074%2Fjbc.M306344200&rfr_id=info:sid/en.wikipedia.org:4-hydroxythreonine-4-phosphate dehydrogenase" class="Z3988">
