Histidinol-phosphate transaminase (EC 2.6.1.9) is an enzyme that catalyzes the reversible chemical reaction
The enzyme first characterised from Neurospora crassa converts 3-(imidazol-4-yl)-2-oxopropyl phosphate to L-histidinol phosphate (a precursor to the amino acid histidine) using L-glutamic acid as the source of the amino group that is transferred. It uses pyridoxal phosphate as a cofactor and has also been found in Salmonella typhimurium. This enzyme is a transferase, specifically a transaminase, 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. It participates in five metabolic pathways: histidine metabolism, tyrosine metabolism, phenylalanine metabolism, phenylalanine, tyrosine and tryptophan biosynthesis, and novobiocin biosynthesis.
Structural studies As of late 2007, 11 structures have been solved for this class of enzymes, with PDB accession codes PDB: 1FG3, PDB: 1FG7, PDB: 1GEW, PDB: 1GEX, PDB: 1GEY, PDB: 1H1C, PDB: 1IJI, PDB: 1UU0, PDB: 1UU1, PDB: 1UU2, and PDB: 2F8J.
References






