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6. Tyr225 in aspartate aminotransferase: contribution of the hydrogen bond between Tyr225 and coenzyme to the catalytic reaction. Inoue K, Kuramitsu S, Okamoto A, Hirotsu K, Higuchi T, Morino Y, Kagamiyama H. J Biochem; 1991 Apr; 109(4):570-6. PubMed ID: 1869510 [Abstract] [Full Text] [Related]
7. Active-site Arg --> Lys substitutions alter reaction and substrate specificity of aspartate aminotransferase. Vacca RA, Giannattasio S, Graber R, Sandmeier E, Marra E, Christen P. J Biol Chem; 1997 Aug 29; 272(35):21932-7. PubMed ID: 9268327 [Abstract] [Full Text] [Related]
8. Strain is more important than electrostatic interaction in controlling the pKa of the catalytic group in aspartate aminotransferase. Mizuguchi H, Hayashi H, Okada K, Miyahara I, Hirotsu K, Kagamiyama H. Biochemistry; 2001 Jan 16; 40(2):353-60. PubMed ID: 11148029 [Abstract] [Full Text] [Related]
15. The tyrosine-225 to phenylalanine mutation of Escherichia coli aspartate aminotransferase results in an alkaline transition in the spectrophotometric and kinetic pKa values and reduced values of both kcat and Km. Goldberg JM, Swanson RV, Goodman HS, Kirsch JF. Biochemistry; 1991 Jan 08; 30(1):305-12. PubMed ID: 1988027 [Abstract] [Full Text] [Related]