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N-(5′-Phosphopyridoxyl)glutamic acid and N-(5′-phosphopyridoxyl)-2-oxopyrrolidine-5-carboxylic acid and their action on the apoenzyme of aspartate aminotransferase

R M. Khomutov, H B. F. Dixon, L V. Vdovina, M P. Kirpichnikov, Y V. Morozov, E S. Severin, E N. Khurs
Biochemical Journal Aug 01, 1971, 124 (1) 99-106; DOI: 10.1042/bj1240099
R M. Khomutov
Institute of Molecular Biology of the Academy of Sciences of the U.S.S.R., Moscow B-312, U.S.S.R.
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H B. F. Dixon
Department of Biochemistry, University of Cambridge, Tennis Court Road, Cambridge CB2 1QW, U.K.
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L V. Vdovina
Institute of Molecular Biology of the Academy of Sciences of the U.S.S.R., Moscow B-312, U.S.S.R.
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M P. Kirpichnikov
Institute of Molecular Biology of the Academy of Sciences of the U.S.S.R., Moscow B-312, U.S.S.R.
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Y V. Morozov
Institute of Molecular Biology of the Academy of Sciences of the U.S.S.R., Moscow B-312, U.S.S.R.
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E S. Severin
Institute of Molecular Biology of the Academy of Sciences of the U.S.S.R., Moscow B-312, U.S.S.R.
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E N. Khurs
Institute of Molecular Biology of the Academy of Sciences of the U.S.S.R., Moscow B-312, U.S.S.R.
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Abstract

1. N-(5′-Phosphopyridoxyl)-l-glutamic acid (P-Pxy-Glu, compound I) is readily converted at pH3 into a substance (P-Pxy-Glp, compound II) characterized as N-(5′-phosphopyridoxyl)-2-oxopyrrolidine-5-carboxylic acid. 2. The u.v., i.r. and fluorescence spectra of P-Pxy-Glu and P-Pxy-Glp have been determined; from the u.v. spectra their pK values have been found and compared. 3. The apoenzyme of aspartate aminotransferase is rapidly and irreversibly inactivated by P-Pxy-Glu, but is inactivated more slowly by P-Pxy-Glp. The complex with P-Pxy-Glp is stable enough to be isolated, but it is slowly reactivated in the presence of excess of pyridoxal phosphate. 4. The u.v. spectrum of the complex of apoenzyme and P-Pxy-Glp suggests that it contains a hydrogen bond between the phenolic hydroxyl group and the pyrrolidone nitrogen; this specifies the conformation of most of the molecule of P-Pxy-Glp. This conformation is similar to that previously postulated for the enzyme–glutamate complex except for the side chain of glutamate. Hence both the affinity of P-Pxy-Glp for the apoenzyme and the fact that it is more easily removed than P-Pxy-Glu are explicable.

  • © 1971 London: The Biochemical Society
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August 1971

Volume: 124 Issue: 1

Biochemical Journal: 124 (1)
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N-(5′-Phosphopyridoxyl)glutamic acid and N-(5′-phosphopyridoxyl)-2-oxopyrrolidine-5-carboxylic acid and their action on the apoenzyme of aspartate aminotransferase
R M. Khomutov, H B. F. Dixon, L V. Vdovina, M P. Kirpichnikov, Y V. Morozov, E S. Severin, E N. Khurs
Biochemical Journal Aug 1971, 124 (1) 99-106; DOI: 10.1042/bj1240099
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N-(5′-Phosphopyridoxyl)glutamic acid and N-(5′-phosphopyridoxyl)-2-oxopyrrolidine-5-carboxylic acid and their action on the apoenzyme of aspartate aminotransferase
R M. Khomutov, H B. F. Dixon, L V. Vdovina, M P. Kirpichnikov, Y V. Morozov, E S. Severin, E N. Khurs
Biochemical Journal Aug 1971, 124 (1) 99-106; DOI: 10.1042/bj1240099

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