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来自多重抑制研究的关于柠檬酸合酶的等排体和别构核苷酸抑制作用的证据。

Evidence of isosteric and allosteric nucleotide inhibition of citrate synthease from multiple-inhibition studies.

作者信息

Harford S, Weitzman P D

出版信息

Biochem J. 1975 Nov;151(2):455-8. doi: 10.1042/bj1510455.

Abstract

Citrate synthases from diverse organisms are inhibited by ATP and NADH. Evidence is presented, from multiple-inhibition studies on various citrate synthases, that ATP acts in all cases as an isosteric inhibitor at the acetyl-CoA site. On the other hand, NADH also acts isosterically with eukaryotic and Gram-positive bacterial citrate synthases, but behaves as an allosteric inhibitor specifically in the case of the Gram-negative bacterial enzyme. After desensitization to this allosteric inhibition, only the isosteric nucleotide inhibition, as found in other citrate syntheases, is observed.

摘要

来自不同生物体的柠檬酸合酶受到ATP和NADH的抑制。通过对各种柠檬酸合酶的多重抑制研究表明,在所有情况下,ATP在乙酰辅酶A位点作为等构抑制剂起作用。另一方面,NADH对真核生物和革兰氏阳性细菌的柠檬酸合酶也起等构作用,但仅在革兰氏阴性细菌酶的情况下表现为别构抑制剂。在对这种别构抑制脱敏后,只观察到如在其他柠檬酸合酶中发现的等构核苷酸抑制作用。

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