Harford S, Weitzman P D
Biochem J. 1975 Nov;151(2):455-8. doi: 10.1042/bj1510455.
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.
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。