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B6db activities: 2.6.1.9

2.6.1.9
Description Histidinol-phosphate aminotransferase.
Alternative names Imidazolylacetolphosphate aminotransferase;
Imidazole acetol-phosphate transaminase.
Catalyzed reaction L-histidinol-phosphate + 2-oxoglutarate = 3-(imidazol-4-yl)-2- oxopropyl phosphate + L-glutamate.
Cofactor Pyridoxal-phosphate.
Prosite PROSITE; PDOC00518;
PDB 1FG7; 1GEW; 1IJI; 1H1C;
Organisms -Eubacteria -Archea -Plants -Fungi
 

Family 

2.6.1.9 (30)
 
Links Enzyme (activities) 2.6.1.9
BRENDA (activities) 2.6.1.9
KEGG (pathways) 2.6.1.9
PLPMDB (PLP mutants) 2.6.1.9
 
References
 Fernandez FJ, Vega MC, Lehmann F, Sandmeier E, Gehring H, Christen P, Wilmanns M. (2004) Structural studies of the catalytic reaction pathway of a hyperthermophilic histidinol-phosphate aminotransferase. J Biol Chem 279 21478-88.

 Mizuguchi H, Hayashi H, Miyahara I, Hirotsu K, Kagamiyama H. (2003) Characterization of histidinol phosphate aminotransferase from Escherichia coli Biochim Biophys Acta. 1647 321-4.

 Sivaraman, J.; Li, Y.; Larocque, R.; Schrag, J. D.; Cygler, M.; Matte, A. (2001) Crystal structure of histidinol phosphate aminotransferase (HisC) from Escherichia coli, and its covalent complex with pyridoxal-5'-phosphate and l-histidinol phosphate J Mol Biol 311 761-76.

 El Malki, F.; Frankard, V.; Jacobs, M. (1998) Molecular cloning and expression of a cDNA sequence encoding histidinol phosphate aminotransferase from Nicotiana tabacum Plant Mol Biol 37 1013-22.

 Gu, W.; Zhao, G.; Eddy, C.; Jensen, R. A. (1995) Imidazole acetol phosphate aminotransferase in Zymomonas mobilis: molecular genetic, biochemical, and evolutionary analyses J Bacteriol 177 1576-84.

 Hsu, L. C.; Okamoto, M.; Snell, E. E. (1989) L-Histidinol phosphate aminotransferase from Salmonella typhimurium. Kinetic behavior and sequence at the pyridoxal-P binding site Biochimie 71 477-89.

Articles on 2.6.1.9
 
last changed 2010/02/02 10:24

B6db activities