Inactivation of Succinate Dehydrogenase by N-Ethylmaleimide
نویسندگان
چکیده
منابع مشابه
Inactivation of succinate dehydrogenase by 3-nitropropionate.
This paper examines proposals in the literature that 3-nitropropionate is a suicide inactivator of succinate dehydrogenase and that it acts by nucleophilic addition to N-5 of the covalently bound flavin component of the enzyme. With purified, soluble preparations of the enzyme, the inhibition developed slowly, and nearly complete inactivation occurred with a stoichiometric amount of 3-nitroprop...
متن کاملThe reaction of N-ethylmaleimide at the active site of succinate dehydrogenase.
Since 1938 mammalian succinate dehydrogenase has been thought to contain thiol groups at the active site. This hypothesis was questioned recently, because irreversible inhibition by bromopyruvate and N-ethylmaleimide appeared not to satisfy the requisite criteria for reaction at the active site. These recent observations of incomplete inactivation of succinate dehydrogenase by N-ethylmaleimide ...
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Since 1938 mammalian succinate dehydrogenase has been thought to contain thiol groups at the active site. This hypothesis was questioned recently, because irreversible inhibition by bromopyruvate and ZV-ethylmaleimide appeared not to satisfy the requisite criteria for reaction at the active site. These recent observations of incomplete inactivation of succinate dehydrogenase by N-ethylmaleimide...
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Since the experiments of KEARNEY 1 it has been known that both particle-bound and soluble succinate dehydrogenase can be activated by its substrate succinate and by competitive inhibitors such as fumarate, malonate and phosphate. Binding at the active centre apparently brings the enzyme in an active conformation. GUTMAN et al. 2) 3 have recently reported that NADH is as effective as succinate i...
متن کاملMolecular aspects of the inactivation of tryptophanyl transfer ribonucleic acid synthetase by N-ethylmaleimide.
The tryptic maps of tryptophanyl-tRNA synthetase from beef pancreas show that the 8 cysteinyl residues of the enzyme subunit are located, 2 by 2, on four different peptides. The kinetics of the incorporation of radioactivity from N-[ethyl-14C]ethylmaleimide into these peptides are compared in this paper with the kinetics of the changes of the catalytic properties of the enzyme occurring during ...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1972
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(19)45020-5