ExplorEnz: EC 1.1.1.262

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1.1.1.262

Accepted name:

4-hydroxythreonine-4-phosphate dehydrogenase

Reaction:

4-phosphonooxy-L-threonine + NAD⁺ = 3-amino-2-oxopropyl phosphate + CO₂ + NADH + H⁺ (overall reaction)
(1a) 4-phosphonooxy-L-threonine + NAD⁺ = (2S)-2-amino-3-oxo-4-phosphonooxybutanoate + NADH + H⁺
(1b) (2S)-2-amino-3-oxo-4-phosphonooxybutanoate = 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

Systematic name:

4-phosphonooxy-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

References:

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 1.1.1.262 created 2000, modified 2006]