ExplorEnz: EC 2.6.99.2

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2.6.99.2

Accepted name:

pyridoxine 5′-phosphate synthase

Reaction:

1-deoxy-D-xylulose 5-phosphate + 3-amino-2-oxopropyl phosphate = pyridoxine 5′-phosphate + phosphate + 2 H₂O

For diagram of pyridoxal biosynthesis, click here

Other name(s):

pyridoxine 5-phosphate phospho lyase; PNP synthase; PdxJ

Systematic name:

1-deoxy-D-xylulose-5-phosphate:3-amino-2-oxopropyl phosphate 3-amino-2-oxopropyltransferase (phosphate-hydrolysing; cyclizing)

Comments:

In Escherichia coli, the cofactor 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). 1-Deoxy-D-xylulose cannot replace 1-deoxy-D-xylulose 5-phosphate as a substrate [3].

Links to other databases:

BRENDA, EXPASY, Gene, KEGG, MetaCyc, PDB, CAS registry number: 230310-47-1

References:

1.	Garrido-Franco, M. Pyridoxine 5′-phosphate synthase: de novo synthesis of vitamin B₆ and beyond. Biochim. Biophys. Acta 1647 (2003) 92–97. [DOI] [PMID: 12686115]
2.	Garrido-Franco, M., Laber, B., Huber, R. and Clausen, T. Enzyme-ligand complexes of pyridoxine 5′-phosphate synthase: implications for substrate binding and catalysis. J. Mol. Biol. 321 (2002) 601–612. [DOI] [PMID: 12206776]
3.	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. [DOI] [PMID: 10225425]
4.	Franco, M.G., Laber, B., Huber, R. and Clausen, T. Structural basis for the function of pyridoxine 5′-phosphate synthase. Structure 9 (2001) 245–253. [DOI] [PMID: 11286891]

[EC 2.6.99.2 created 2006]