LOCATION OF HYDROGEN TRANSFER STEPS IN MECHANISM OF REDUCTION OF L-AMINO ACID OXIDASE

被引：17

作者：

PORTER, DJT

BRIGHT, HJ

机构：

[1] Department of Biochemistry, School of Medicine University of Pennsylvania, Philadelphia

来源：

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 1969年 / 36卷 / 02期

关键词：

D O I：

10.1016/0006-291X(69)90316-7

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：

We show by means of a specific kinetic isotope effect that the bond between hydrogen and the 2-carbon of the substrate is broken in forming the 540 mμ complex of L-amino acid oxidase. In addition, this process is considerably slowed in 2H2O. The conversion of the 540 mμ complex to the fully reduced enzyme appears not to involve the rate-limiting transfer of a species of hydrogen of any kind. © 1969.

引用

页码：209 / &

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