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Korean Society for Biochemistry and Molecular Biology (생화학분자생물학회)
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Inactivation of Brain Succinic Semialdehyde Reductase by o-Phthalaldehyde

  • Choi, Soo-Young (Department of Genetic Engineering, College of Natural Sciences, Hallym University) ;
  • Song, Min-Sun (Department of Genetic Engineering, College of Natural Sciences, Hallym University) ;
  • Lee, Byung-Ryong (Department of Genetic Engineering, College of Natural Sciences, Hallym University) ;
  • Jang, Sang-Ho (Department of Genetic Engineering, College of Natural Sciences, Hallym University) ;
  • Lee, Su-Jin (Department of Biochemistry, College of Medicine, Yonsei University) ;
  • Park, Jin-Seu (Department of Genetic Engineering, College of Natural Sciences, Hallym University) ;
  • Choe, Joon-Ho (Department of Life Science, Korea Advanced Institute of Sience and Technology) ;
  • Cho, Sung-Woo (Department of Biochemistry, College of Medicine, University of Ulsan)
  • Received : 1994.09.29
  • Published : 1995.03.31
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Abstract

Succinic semialdehyde reductase was inactivated by o-phthalaldehyde. The inactivation followed pseudo-first order kinetics, and the second-order rate constant for the inactivation process was 28 $M^{-1}s^{-1}$ at pH 7.4 and $25^{\circ}C$. The absorption spectrum ($\lambda_{max}$ 337 nm) and fluorescence excitation ($\lambda_{max}$ 340 nm) and fluorescence emission spectra ($\lambda_{max}$ 409 nm) were consistent with the formation of an isoindole derivative in the catalytic site between a cysteine and a lysine residue approximately about 3 $\AA$ apart. The substrate, succinic semialdehyde, did not protect enzymatic activity against inactivation, whereas the coenzyme NADPH protected against o-phthaladehyde induced inactivation of the enzyme. About 1 isoindole group per mol of the enzyme was formed following complete loss of enzymatic activity. These results suggest that the amino acid residues of the enzyme participating in a reaction with o-phthalaldehyde are cysteinyl and lysyl residues at or near the NADPH binding site.

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