KINETIC MECHANISM OF KETOREDUCTASE ACTIVITY OF PROSTAGLANDIN-F SYNTHASE FROM BOVINE LUNG

被引：3

作者：

BARSKI, OA ^{[1
]}

WATANABE, K ^{[1
]}

机构：

[1] OSAKA BIOSCI INST,DEPT ENZYME & METAB,6-2-4 FURUEDAI,SUITA,OSAKA 565,JAPAN

来源：

FEBS LETTERS | 1993年 / 320卷 / 02期

关键词：

PING-PONG MECHANISM; KINETICS; PROSTAGLANDIN-F SYNTHASE; BINDING CONSTANT; ALDO-KETO REDUCTASE; NADPH;

D O I：

10.1016/0014-5793(93)80072-3

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：

The kinetic mechanism of ketoreductase activity of bovine lung prostaglandin F synthase, expressed in E. coli, was investigated. Data on initial velocity and radioisotope exchange between [H-3]prostaglandin D2 and 9alpha,11beta-prostaglandin F2 suggest that the enzyme obeys the ping-pong mechanism. Using a fluorescence technique we obtained a binding constant of 3 muM for NADPH. This is in close correlation with the kinetically determined intrinsic Michaelis constant for NADPH. Activation energy of the redox process was determined from the temperature dependence of maximal velocities for nitrobenzaldehyde and menadione and was found to be 119 and 96 kJ/mol, respectively.

引用

页码：107 / 110

页数：4

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