EC 1.1.1.262 - 4-hydroxythreonine-4-phosphate dehydrogenase

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IntEnz Enzyme Nomenclature
EC 1.1.1.262

Names

Accepted name:
4-hydroxythreonine-4-phosphate dehydrogenase
Other names:
4-(phosphohydroxy)-L-threonine dehydrogenase
L-threonine 4-phosphate dehydrogenase
NAD+-dependent threonine 4-phosphate dehydrogenase
PdxA
4-(phosphonooxy)-L-threonine:NAD+ oxidoreductase
Systematic name:
4-phosphonooxy-L-threonine:NAD+ oxidoreductase

Reactions

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

Enzymes and pathways: NC-IUBMB , BRENDA , DIAGRAM , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , UniPathway
Structural data: CSA , EC2PDB
Gene Ontology: GO:0050570
UniProtKB/Swiss-Prot: (138) [show] [UniProt]

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: 1936-1937 (1998).
  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: 45-48 (1999). [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: 43682-43690 (2003). [PMID: 12896974]

[EC 1.1.1.262 created 2000, modified 2006]