The Enzyme Database

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Accepted name: 4-hydroxythreonine-4-phosphate dehydrogenase
Reaction: 4-phosphooxy-L-threonine + NAD+ = 3-amino-2-oxopropyl phosphate + CO2 + NADH + H+ (overall reaction)
(1a) 4-phosphooxy-L-threonine + NAD+ = (2S)-2-amino-3-oxo-4-phosphooxybutanoate + NADH + H+
(1b) (2S)-2-amino-3-oxo-4-phosphooxybutanoate = 3-amino-2-oxopropyl phosphate + CO2 (spontaneous)
For diagram of pyridoxal biosynthesis, click here
Other name(s): NAD+-dependent threonine 4-phosphate dehydrogenase; L-threonine 4-phosphate dehydrogenase; 4-(phosphohydroxy)-L-threonine dehydrogenase; PdxA; 4-(phosphonooxy)-L-threonine:NAD+ oxidoreductase; 4-phosphonooxy-L-threonine:NAD+ oxidoreductase
Systematic name: 4-phosphooxy-L-threonine:NAD+ oxidoreductase
Comments: The product of the reaction undergoes decarboxylation to give 3-amino-2-oxopropyl phosphate. The enzyme is part of the biosynthesis pathway of the coenzyme pyridoxal 5′-phosphate found in anaerobic bacteria.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 230310-36-8
1.  Cane, D.E., Hsiung, Y., Cornish, J.A., Robinson, J.K and Spenser, I.D. Biosynthesis of vitamine B6: The oxidation of L-threonine 4-phosphate by PdxA. J. Am. Chem. Soc. 120 (1998) 1936–1937.
2.  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]
3.  Sivaraman, J., Li, Y., Banks, J., Cane, D.E., Matte, A. and Cygler, M. Crystal structure of Escherichia coli PdxA, an enzyme involved in the pyridoxal phosphate biosynthesis pathway. J. Biol. Chem. 278 (2003) 43682–43690. [PMID: 12896974]
[EC created 2000, modified 2006]

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