Histidinol-phosphate transaminase

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In enzymology, a histidinol-phosphate transaminase (EC 2.6.1.9) is an enzyme that catalyzes the chemical reaction

L-histidinol phosphate + 2-oxoglutarate $\rightleftharpoons$ 3-(imidazol-4-yl)-2-oxopropyl phosphate + L-glutamate

Thus, the two substrates of this enzyme are L-histidinol phosphate and 2-oxoglutarate, whereas its two products are 3-(imidazol-4-yl)-2-oxopropyl phosphate and L-glutamate.

This enzyme belongs to the family of transferases, specifically the transaminases, which transfer nitrogenous groups. The systematic name of this enzyme class is L-histidinol-phosphate:2-oxoglutarate aminotransferase. Other names in common use include imidazolylacetolphosphate transaminase, glutamic-imidazoleacetol phosphate transaminase, histidinol phosphate aminotransferase, imidazoleacetol phosphate transaminase, L-histidinol phosphate aminotransferase, histidine:imidazoleacetol phosphate transaminase, IAP transaminase, and imidazolylacetolphosphate aminotransferase. This enzyme participates in 5 metabolic pathways: histidine metabolism, tyrosine metabolism, phenylalanine metabolism, phenylalanine, tyrosine and tryptophan biosynthesis, and novobiocin biosynthesis. It employs one cofactor, pyridoxal phosphate.

1 Structural studies
2 References
3 External links
- 3.1 Gene Ontology (GO) codes

[edit] Structural studies

As of late 2007, 11 structures have been solved for this class of enzymes, with PDB accession codes 1FG3, 1FG7, 1GEW, 1GEX, 1GEY, 1H1C, 1IJI, 1UU0, 1UU1, 1UU2, and 2F8J.

[edit] References

IUBMB entry for 2.6.1.9
BRENDA references for 2.6.1.9 (Recommended.)
PubMed references for 2.6.1.9
PubMed Central references for 2.6.1.9
Google Scholar references for 2.6.1.9
AMES BN, HORECKER BL (1956). "The biosynthesis of histidine: imidazoleacetol phosphate transaminase". J. Biol. Chem. 220: 113–28. PMID 13319331.
Martin RG and Goldberger RF (1963). "Imidazolylacetolphosphate:L-glutamate aminotransferase. Purification and properties". J. Biol. Chem. 242: 1168–1174.