The Enzyme Database

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EC 1.4.3.5     
Accepted name: pyridoxal 5′-phosphate synthase
Reaction: (1) pyridoxamine 5′-phosphate + H2O + O2 = pyridoxal 5′-phosphate + NH3 + H2O2
(2) pyridoxine 5′-phosphate + O2 = pyridoxal 5′-phosphate + H2O2
For diagram of pyridoxal biosynthesis, click here
Glossary: pyridoxamine = 4-aminomethyl-3-hydroxy-5-hydroxymethyl-2-methylpyridine
Other name(s): pyridoxamine 5′-phosphate oxidase; pyridoxamine phosphate oxidase; pyridoxine (pyridoxamine)phosphate oxidase; pyridoxine (pyridoxamine) 5′-phosphate oxidase; pyridoxaminephosphate oxidase (EC 1.4.3.5: deaminating); PMP oxidase; pyridoxol-5′-phosphate:oxygen oxidoreductase (deaminating) (incorrect); pyridoxamine-phosphate oxidase; PdxH
Systematic name: pyridoxamine-5′-phosphate:oxygen oxidoreductase (deaminating)
Comments: A flavoprotein (FMN). In Escherichia coli, the coenzyme pyridoxal 5′-phosphate is synthesized de novo by a pathway that involves EC 1.2.1.72 (erythrose-4-phosphate dehydrogenase), EC 1.1.1.290 (4-phosphoerythronate dehydrogenase), EC 2.6.1.52 (phosphoserine transaminase), EC 1.1.1.262 (4-hydroxythreonine-4-phosphate dehydrogenase), EC 2.6.99.2 (pyridoxine 5′-phosphate synthase) and EC 1.4.3.5 (with pyridoxine 5′-phosphate as substrate). N4′-Substituted pyridoxamine derivatives are also oxidized in reaction (1) to form pyridoxal 5-phosphate and the corresponding primary amine.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9029-21-4
References:
1.  Choi, J.-D., Bowers-Komro, D.M., Davis, M.D., Edmondson, D.E. and McCormick, D.B. Kinetic properties of pyridoxamine (pyridoxine)-5′-phosphate oxidase from rabbit liver. J. Biol. Chem. 258 (1983) 840–845. [PMID: 6822512]
2.  Wada, H. and Snell, E.E. The enzymatic oxidation of pyridoxine and pyridoxamine phosphates. J. Biol. Chem. 236 (1961) 2089–2095. [PMID: 13782387]
3.  Notheis, C., Drewke, C. and Leistner, E. Purification and characterization of the pyridoxol-5′-phosphate:oxygen oxidoreductase (deaminating) from Escherichia coli. Biochim. Biophys. Acta 1247 (1995) 265–271. [PMID: 7696318]
4.  Laber, B., Maurer, W., Scharf, S., Stepusin, K. and Schmidt, F.S. 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 (1999) 45–48. [PMID: 10225425]
5.  Musayev, F.N., Di Salvo, M.L., Ko, T.P., Schirch, V. and Safo, M.K. Structure and properties of recombinant human pyridoxine 5′-phosphate oxidase. Protein Sci. 12 (2003) 1455–1463. [PMID: 12824491]
6.  Safo, M.K., Musayev, F.N. and Schirch, V. Structure of Escherichia coli pyridoxine 5′-phosphate oxidase in a tetragonal crystal form: insights into the mechanistic pathway of the enzyme. Acta Crystallogr. D Biol. Crystallogr. 61 (2005) 599–604. [PMID: 15858270]
7.  Zhang, Z. and McCormick, D.B. Uptake and metabolism of N-(4′-pyridoxyl)amines by isolated rat liver cells. Arch. Biochem. Biophys. 294 (1992) 394–397. [PMID: 1567194]
[EC 1.4.3.5 created 1961, modified 2006]
 
 


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