Mechanistic studies of the inactivation of crotonase by (methylenecyclopropyl)formyl-CoA

Journal of the American Chemical Society

Volumn 118, Issue 1, 1996, Pages 275-276

  Li, Ding ^a   Guo, Zhihong ^a   Liu, Hung Wen ^a  

^a University of Minnesota   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

EID: 0030021888     PISSN: 00027863     EISSN: None     Source Type: Journal    
DOI: 10.1021/ja952621b     Document Type: Article

References (32)

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2. There are three types of enoyl-CoA hydratase in higher animals, two in mitochondria as short-chain enoyl-CoA hydratase (crotonase) and trifunctional protein (Uchida. Y : Izai. K.; Orii. T.; Hashimoto, T. J. Biol. Chem 1992, 267, 1034) and one in peroxisomes as bifunctional protein (Osumi, T.; Hashimoto, T. Arch. Biochem. Biophys. 1980, 203, 372).
3. 3c rat liver (Furuta, S., Miyazawa, S.; Osumi, T.; Hashimoto, T.; Ui. N. J. Biochem. 1980, 88, 1059). pig heart ( Fong, J. C.: Schulz, H. Methods Enzymol. 1981, 71. 390). and pig kidney ( Buettner, H. Ph.D. Thesis, University of Konstanz, 1988).
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19. 2 The specific activity of the purified enzyme is 293 units/mg (1 unit = 1 μmol of product formation per minute).
20. The kinetic parameters of inactivation were derived from plotting the apparent inactivation rate, obtained by incubating crotonase (9 μM. 6.3 nmol) with 2 of varied concentration (9-600 μM), versus inhibitor concentration. Unless otherwise specified. 50 mM potassium phosphate buffer, pH 7.5. was used in all experiments.
21. 10b
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