Crystallization (Comment) | Organism |
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the crystals of AspATs reconstituted with phosphopyridoxyl-L-Glu, phosphopyridoxyl-D-Glu, and phosphopyridoxal-2-methyl-L-glutamate are obtained by the hanging drop vapor diffusion method using ammonium sulfate as the precipitant. Crystals of suitable size for diffraction experiments are obtained within a week. The crystal structures of the complexes of aspartate aminotransferase with phosphopyridoxyl derivatives of L-glutamate, D-glutamate, and 2-methyl-L-glutamate are solved as the models for the external aldimine and ketimine complexes of L-glutamate. All the structures are in the closed form, and the two carboxylate groups and the arginine residues binding them are superimposable on the external aldimine complex with 2-methyl-L-aspartate | Escherichia coli |
Organism | UniProt | Comment | Textmining |
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Escherichia coli | P00509 | - |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
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L-glutamate + 2-oxoglutarate | binding of L-Glu to aspartate aminotransferase to form the Michaelis complex does not induce a conformational change in the enzyme. The conformational change to the closed form occurs during the transaldimination step. The hydrophobic residues of the entrance of the active site, including Tyr70, are considered to be important for promoting the transaldimination process and hence the recognition of the C5 substrate | Escherichia coli | 2-oxoglutarate + L-glutamate | - |
? |
Synonyms | Comment | Organism |
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aspartate:2-oxoglutarate amino-transferase | - |
Escherichia coli |
AspAT | - |
Escherichia coli |