Aminotransferase
From Proteopedia
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== Structural highlights == | == Structural highlights == | ||
| - | The <scene name='72/721044/Cv/ | + | The <scene name='72/721044/Cv/3'>active site of histidinol-phosphate aminotransferase contains PLP</scene>.<ref>PMID:11294630</ref> |
Revision as of 12:26, 2 May 2018
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3D structures of aminotransferase
Updated on 02-May-2018
References
- ↑ Mizuguchi H, Hayashi H, Miyahara I, Hirotsu K, Kagamiyama H. Characterization of histidinol phosphate aminotransferase from Escherichia coli. Biochim Biophys Acta. 2003 Apr 11;1647(1-2):321-4. PMID:12686152
- ↑ Kirsch JF, Eichele G, Ford GC, Vincent MG, Jansonius JN, Gehring H, Christen P. Mechanism of action of aspartate aminotransferase proposed on the basis of its spatial structure. J Mol Biol. 1984 Apr 15;174(3):497-525. PMID:6143829 doi:http://dx.doi.org/10.1016/0022-2836(84)90333-4
- ↑ Kirsch JF, Eichele G, Ford GC, Vincent MG, Jansonius JN, Gehring H, Christen P. Mechanism of action of aspartate aminotransferase proposed on the basis of its spatial structure. J Mol Biol. 1984 Apr 15;174(3):497-525. PMID:6143829 doi:http://dx.doi.org/10.1016/0022-2836(84)90333-4
- ↑ Haruyama K, Nakai T, Miyahara I, Hirotsu K, Mizuguchi H, Hayashi H, Kagamiyama H. Structures of Escherichia coli histidinol-phosphate aminotransferase and its complexes with histidinol-phosphate and N-(5'-phosphopyridoxyl)-L-glutamate: double substrate recognition of the enzyme. Biochemistry. 2001 Apr 17;40(15):4633-44. PMID:11294630
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