Aminotransferase
From Proteopedia
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<StructureSection load='1gew' size='340' side='right' caption='E. coli Histidinol-phosphate aminotransferase complex with PLP (PDB code [[1gew]])' scene=''> | <StructureSection load='1gew' size='340' side='right' caption='E. coli Histidinol-phosphate aminotransferase complex with PLP (PDB code [[1gew]])' scene=''> | ||
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== Function == | == Function == | ||
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'''Phosphoserine aminotransferase''' (PSAT) catalyzes the intercorversion of phosphoserine and oxoglutarate to phosphonooxypyruvate and glutamate. For details on PSAT see [[Phosphoserine aminotransferase]].<ref>PMID:6143829</ref> | '''Phosphoserine aminotransferase''' (PSAT) catalyzes the intercorversion of phosphoserine and oxoglutarate to phosphonooxypyruvate and glutamate. For details on PSAT see [[Phosphoserine aminotransferase]].<ref>PMID:6143829</ref> | ||
| - | + | '''Alanine glyoxylate aminotransferase''' (AGA) catalyzes the intercorversion of alanine and glyoxate to methyloxopropanoate and glycine. | |
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| + | '''D-amino acid aminotransferase''' (AAT) catalyzes the intercorversion of D-alanine and oxoglutarate to pyruvate and D-glutamate. | ||
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| + | '''Aromatic amino acid aminotransferase''' (AROAT) catalyzes the intercorversion of aromatic amino acid and oxoglutarate to aromatic oxo acid and glutamate. | ||
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| + | '''Lysine aminotransferase''' (LYSAT) catalyzes the intercorversion of lysine and oxoglutarate to aminoadipate semialdeyde and glutamate. | ||
== Relevance == | == Relevance == | ||
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| + | Elevated levels of alanine aminotransferase and aspartate aminotransferase are indicators of liver damage. | ||
== Structural highlights == | == Structural highlights == | ||
Revision as of 13:38, 29 December 2015
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3D structures of aminotransferase
Updated on 29-December-2015
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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