Pyridoxine 5'-phosphate synthase

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In enzymology, a pyridoxine 5'-phosphate synthase (EC 2.6.99.2) is an enzyme that catalyzes the chemical reaction

1-deoxy-D-xylulose 5-phosphate + 3-amino-2-oxopropyl phosphate $\rightleftharpoons$ pyridoxine 5'-phosphate + phosphate + 2 H₂O

Thus, the two substrates of this enzyme are 1-deoxy-D-xylulose 5-phosphate and 3-amino-2-oxopropyl phosphate, whereas its 3 products are pyridoxine 5'-phosphate, phosphate, and H₂O.

This enzyme belongs to the family of transferases, specifically those transferring nitrogenous groups transferring other nitrogenous groups. The systematic name of this enzyme class is 1-deoxy-D-xylulose-5-phosphate:3-amino-2-oxopropyl phosphate 3-amino-2-oxopropyltransferase (phosphate-hydrolysing; cyclizing). Other names in common use include pyridoxine 5-phosphate phospho lyase, PNP synthase, and PdxJ. This enzyme participates in vitamin b6 metabolism.

[edit] References

IUBMB entry for 2.6.99.2
BRENDA references for 2.6.99.2 (Recommended.)
PubMed references for 2.6.99.2
PubMed Central references for 2.6.99.2
Google Scholar references for 2.6.99.2
Garrido-Franco M (2003). "Pyridoxine 5'-phosphate synthase: de novo synthesis of vitamin B6 and beyond". Biochim. Biophys. Acta. 1647: 92–7. PMID 12686115.
Garrido-Franco M, Laber B, Huber R, Clausen T (2002). "Enzyme-ligand complexes of pyridoxine 5'-phosphate synthase: implications for substrate binding and catalysis". J. Mol. Biol. 321: 601–12. PMID 12206776.
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.
Franco MG, Laber B, Huber R, Clausen T (2001). "Structural basis for the function of pyridoxine 5'-phosphate synthase". Structure. 9: 245–53. PMID 11286891.