NUCLEAR MAGNETIC-RESONANCE STUDIES OF D2O-SUBSTRATE EXCHANGE-REACTIONS CATALYZED BY GLUTAMIC PYRUVIC AND GLUTAMIC OXALOACETIC TRANSAMINASES

被引：28

作者：

BABU, UM ^{[1
]}

JOHNSTON, RB ^{[1
]}

机构：

[1] UNIV NEBRASKA, DEPT CHEM, LINCOLN, NE 68588 USA

来源：

BIOCHEMISTRY | 1976年 / 15卷 / 25期

关键词：

D O I：

10.1021/bi00670a037

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

NMR studies in D2O (> 90%) with glutamic pyruvate transaminase (GTP) (2.6.1.2) demonstrate that this enzyme catalyzes the rapid exchange of both the .alpha. and .beta. H of L-alanine, the exchange of only one .alpha. H of glycine, and the .beta. H of pyruvate and fluoropyruvate. When the .beta. H of L-alanine undergo the enzyme-catalyzed exchange, the product may have 1, 2 or 3 of .beta. H exchanged. The exchange is stimulated by the addition of catalytic amounts of copartner of transaminations reaction. A mechanism is proposed for an extention of the conjugated system to include the .alpha. and .beta. C to explain the labilization of the .beta. H.

引用

页码：5671 / 5677

页数：7

共 24 条

[1]

BABU U M, 1974, Federation Proceedings, V33, P1379

[2] D2O-ALANINE EXCHANGE-REACTIONS CATALYZED BY ALANINE RACEMASE AND GLUTAMIC PYRUVIC TRANSAMINASE [J].