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2.6.1.9 |
Activity |
2.6.1.9 |
Description |
Histidinol-phosphate aminotransferase |
PDB |
1FG7;1GEW;1IJI;1H1C; |
PLP Fold Type |
I |
PLP-dependent Domain |
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Number of sequences |
30 |
Sequences in seed alignment |
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Reference sequence |
HIS8_THEMA |
Domain interval |
19-331 |
Catalytic site |
202 K |
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References |
Nasir N, Anant A, Vyas R, Biswal BK
(2016) Crystal structures of Mycobacterium tuberculosis HspAT and ArAT reveal structural basis of their distinct substrate specificities Sci Rep 6 18880. 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. 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 |
2014/07/10 20:34 |
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