Inactivation of an NADPH‐dependent succinic semialdehyde reductase by o‐phthalaldehyde

FEBS Letters

Choi, Soo Young²  Hong, Joung Woo²  Lee, Su Jin²  Cho, Sung-Woo¹ 

[1] Department of Biochemistry, College of Medicine, University of Ulsan, Seoul 138-040, South Korea;Department of Genetic Engineering, Hallym University, Chuncheon 200-702, South Korea

关键词: Succinic semialdehyde reductase;    o-Phthalaldehyde;    Brain;   

DOI  :  10.1016/0014-5793(96)00170-6

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Incubation of an NADPH-dependent succinic semialdehyde reductase from bovine brain with o-phthalaldehyde resulted in a time-dependent loss of enzyme activity. The inactivation followed pseudo first-order kinetics with the second-order rate constant of 28 M⁻¹ s⁻¹. The inactivation was prevented by preincubation of the enzyme with NADPH, but not by succinic semialdehyde. There was a linear relationship between isoindole formation and the loss of enzyme activity. Spectrophotometric studies indicated that complete inactivation of the enzyme resulted from the formation of one isoindole derivative per molecule of enzyme, which was formed from the reaction of cysteine and lysine residues with o-phthalaldehyde at or near the enzyme active site.

【 授权许可】

Unknown