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2. Kinetics and equilibria for the reactions of coenzymes with wild type and the Y70F mutant of Escherichia coli aspartate aminotransferase. Toney MD, Kirsch JF. Biochemistry; 1991 Jul 30; 30(30):7461-6. PubMed ID: 1677270 [Abstract] [Full Text] [Related]
3. Reaction of aspartate aminotransferase with L-erythro-3-hydroxyaspartate: involvement of Tyr70 in stabilization of the catalytic intermediates. Hayashi H, Kagamiyama H. Biochemistry; 1995 Jul 25; 34(29):9413-23. PubMed ID: 7626611 [Abstract] [Full Text] [Related]
4. Role of Asp222 in the catalytic mechanism of Escherichia coli aspartate aminotransferase: the amino acid residue which enhances the function of the enzyme-bound coenzyme pyridoxal 5'-phosphate. Yano T, Kuramitsu S, Tanase S, Morino Y, Kagamiyama H. Biochemistry; 1992 Jun 30; 31(25):5878-87. PubMed ID: 1610831 [Abstract] [Full Text] [Related]
10. [Arg292----Val] or [Arg292----Leu] mutation enhances the reactivity of Escherichia coli aspartate aminotransferase with aromatic amino acids. Hayashi H, Kuramitsu S, Inoue Y, Morino Y, Kagamiyama H. Biochem Biophys Res Commun; 1989 Feb 28; 159(1):337-42. PubMed ID: 2564274 [Abstract] [Full Text] [Related]
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18. Crystal structures of true enzymatic reaction intermediates: aspartate and glutamate ketimines in aspartate aminotransferase. Malashkevich VN, Toney MD, Jansonius JN. Biochemistry; 1993 Dec 14; 32(49):13451-62. PubMed ID: 7903048 [Abstract] [Full Text] [Related]
19. Binding of C5-dicarboxylic substrate to aspartate aminotransferase: implications for the conformational change at the transaldimination step. Islam MM, Goto M, Miyahara I, Ikushiro H, Hirotsu K, Hayashi H. Biochemistry; 2005 Jun 14; 44(23):8218-29. PubMed ID: 15938611 [Abstract] [Full Text] [Related]