利用质子磁共振波谱对大肠杆菌天冬氨酸转氨酶使氨基酸发生特定α-氘代反应进行的动力学研究。
Kinetic studies with the use of proton-magnetic-resonance spectroscopy of the specific alpha-deuteration of amino acids by Escherichia coli aspartate aminotransferase.
作者信息
Gout E, Chesne S, Beguin C G, Pelmont J
出版信息
Biochem J. 1978 Jun 1;171(3):719-23. doi: 10.1042/bj1710719.
Abstract
Escherichia coli aspartate aminotransferase was exposed to aspartate or phenylalanine without oxo acid in buffered 2H2O. The alpha-hydrogen of the amino acids underwent first-order exchange with respect to both substrate and enzyme. P.m.r. spectroscopy gave consistent reaction-rate constants. The deuterium-exchange rate was only moderately increased by addition of oxo acids and was of the same order as the transamination rate. No beta-deuteration was observed. The C(alpha)-H-bond-breaking step is discussed as a part of the entire transamination mechanism.
摘要
在缓冲的重水（2H₂O）中，将大肠杆菌天冬氨酸转氨酶暴露于无酮酸的天冬氨酸或苯丙氨酸中。氨基酸的α-氢与底物和酶均发生一级交换。核磁共振光谱给出了一致的反应速率常数。加入酮酸后，氘交换速率仅适度增加，且与转氨速率处于同一量级。未观察到β-氘化现象。讨论了C(α)-H键断裂步骤作为整个转氨机制的一部分。
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