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3. 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]
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]
12. Role of an active site residue analyzed by combination of mutagenesis and coenzyme analog. Yano T, Hinoue Y, Chen VJ, Metzler DE, Miyahara I, Hirotsu K, Kagamiyama H. J Mol Biol; 1993 Dec 20; 234(4):1218-29. PubMed ID: 8263922 [Abstract] [Full Text] [Related]
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17. The imine-pyridine torsion of the pyridoxal 5'-phosphate Schiff base of aspartate aminotransferase lowers its pKa in the unliganded enzyme and is crucial for the successive increase in the pKa during catalysis. Hayashi H, Mizuguchi H, Kagamiyama H. Biochemistry; 1998 Oct 27; 37(43):15076-85. PubMed ID: 9790670 [Abstract] [Full Text] [Related]