胆碱乙酰转移酶辅酶A结合位点存在精氨酸残基的证据。
Evidence for presence of an arginine residue in the coenzyme A binding site of choline acetyltransferase.
作者信息
Mautner H G, Pakula A A, Merrill R E
出版信息
Proc Natl Acad Sci U S A. 1981 Dec;78(12):7449-52. doi: 10.1073/pnas.78.12.7449.
Choline acetyltransferase (acetyl-CoA:choline O-acetyltransferase, EC 2.3.1.6) may be inactivated by arginine-specific reagents such as butanedione, phenylglyoxal, and camphorquinone-10-sulfonic acid. The enantiomers of the latter compound were prepared, but inactivation was not stereospecific. Protection against inactivation by the arginine-specific reagents was provided by CoA and, to a lesser extent, by 3'-dephospho-CoA. No protection was provided by choline, NAD+, NADH, NADP+, or NADPH. Sodium chloride could protect, to some extent, against inactivation by arginine-specific reagents; this protection showed no cation or anion specificity. The data are compatible with the postulate that the salt anion competes with the attachment of the 3'-phospho group of CoA to an active site arginine residue.
胆碱乙酰转移酶（乙酰辅酶A：胆碱O-乙酰转移酶，EC 2.3.1.6）可能会被精氨酸特异性试剂如丁二酮、苯乙二醛和樟脑醌-10-磺酸失活。制备了后一种化合物的对映体，但失活并非立体特异性的。辅酶A能保护该酶不被精氨酸特异性试剂失活，3'-去磷酸辅酶A在较小程度上也有保护作用。胆碱、NAD⁺、NADH、NADP⁺或NADPH均无保护作用。氯化钠在一定程度上可以保护该酶不被精氨酸特异性试剂失活；这种保护没有阳离子或阴离子特异性。这些数据与盐阴离子与辅酶A的3'-磷酸基团附着于活性位点精氨酸残基相竞争的假设相符。
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