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J. Biochem, 1988, Vol. 103, No. 4 585-588
© 1988 Japanese Biochemical Society

research-article

Kinetic Studies on the Binding of Gostatin, a Suicide Substrate for Aspartate Aminotransferase, with the Isoenzymes from Porcine Heart Mitochondria and Cytosol1

Keiko Kitagishi, Faculty of Agriculture*, Keitaro Hiromi*,2, Sumio Tanase**, Fujio Nagashima**, Yoshimasa Morino**, Toyokazu Nishino*** and Sawao Murao***

* Kyoto University Sakyo-ku, Kyoto, Kyoto 606
** Kumamoto University Medical School Kumamoto, Kumamoto 860
*** College of Agriculture, University of Osaka Prefecture Sakai, Osaka 591

2To whom correspondence should be addressed.

The reaction of pig heart mitochondrial and cytosolic aspartate aminotransferases (abbreviated to mAspAT and cAspAT, respectively) with an enzyme-suicide substrate (mechanism-based inhibitor), gostatin (5-amino-2-carboxyl-4-oxo-1,4,5,6-tetrahydropyridine-3-acetic acid) was studied kinetically, by following the spectral change with a micro-stopped-flow apparatus, as well as the inactivation of the enzyme activity. No significant difference in kinetic behavior was observed between mAspAT and cAspAT. From the analysis of time-dependent spectral change, no positive evidence for the existence of spectrophotometrically distinguishable intermediates was obtained. Both the spectral change and the inactivation followed, at least in appearance, simple bimolecular association kinetics, under the conditions studied. However, the second-order rate constant of the spectral change was found to be 1.5 to 2 times as large as that of the inactivation. The effects of pH and temperature on kon (the second-order rate constant of the spectral change) were also studied.

1 This work was supported in part by Grants-in-Aid for Scientific Research from the Ministry of Education, Science and Culture of Japan.

Present addresses: K. Kitagishi, Department of Biochemistry and Biophysics, School of Medicine, University of Pennsilvania, PA 19104, U.S.A.; T. Nishino, Kurabo Industries Ltd., Neyagawa, Osaka 572; S. Murao, Department of Applied Microbial Technology, Kumamoto Institute of Technology, Kumamoto, Kumamoto 860.


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