1h1c: Difference between revisions
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[[Category: histidine biosynthesis]] | [[Category: histidine biosynthesis]] | ||
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Revision as of 16:20, 30 October 2007
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HISTIDINOL-PHOSPHATE AMINOTRANSFERASE (HISC) FROM THERMOTOGA MARITIMA
OverviewOverview
In histidine biosynthesis, histidinol-phosphate aminotransferase catalyzes, the transfer of the amino group from glutamate to imidazole, acetol-phosphate producing 2-oxoglutarate and histidinol phosphate. In, some organisms such as the hyperthermophile Thermotoga maritima, specific, tyrosine and aromatic amino acid transaminases have not been identified to, date, suggesting an additional role for histidinol-phosphate, aminotransferase in other transamination reactions generating aromatic, amino acids. To gain insight into the specific function of this, transaminase, we have determined its crystal structure in the absence of, any ligand except phosphate, in the presence of covalently bound pyridoxal, 5'-phosphate, of the coenzyme histidinol phosphate adduct, and of, pyridoxamine ... [(full description)]
About this StructureAbout this Structure
1H1C is a [Single protein] structure of sequence from [Thermotoga maritima] with PLP as [ligand]. Active as [Histidinol-phosphate transaminase], with EC number [2.6.1.9]. Structure known Active Site: AC1. Full crystallographic information is available from [OCA].
ReferenceReference
Structural studies of the catalytic reaction pathway of a hyperthermophilic histidinol-phosphate aminotransferase., Fernandez FJ, Vega MC, Lehmann F, Sandmeier E, Gehring H, Christen P, Wilmanns M, J Biol Chem. 2004 May 14;279(20):21478-88. Epub 2004 Mar 8. PMID:15007066
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