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电鳐和眼镜蛇毒中乙酰胆碱酯酶催化中心的阴离子亚位点。

Anionic subsites of the catalytic center of acetylcholinesterase from Torpedo and from cobra venom.

作者信息

Kreienkamp H J, Weise C, Raba R, Aaviksaar A, Hucho F

机构信息

Institut für Biochemie, Freie Universität Berlin, Federal Republic of Germany.

出版信息

Proc Natl Acad Sci U S A. 1991 Jul 15;88(14):6117-21. doi: 10.1073/pnas.88.14.6117.

Abstract

A peptide of acetylcholinesterase (AcChoEase; acetylcholine acetylhydrolase, EC 3.1.1.7) from the venom of the cobra Naja naja oxiana labeled by the affinity reagent N,N-dimethyl-2-phenylaziridinium (DPA) has been identified. The sequence is Gly-Ala-Glu-Met-Trp-Asn-Pro-Asn. In AcChoEase from Torpedo californica, a homologous peptide was labeled and isolated. Its sequence is Ser-Gly-Ser-Glu-Met-Trp-Asn-Pro-Asn, representing positions 79 through 87. In both cases labeling can be prevented by 0.1 mM edrophonium, indicating that the respective peptides form part of the anionic subsite of the catalytic center. The modified residue was tryptophan (Trp-84 in Torpedo AcChoEase) in both enzymes. In contrast to AcChoEase from Torpedo, the enzyme from cobra venom does not contain a peripheral anionic binding site.

摘要

已鉴定出一种来自眼镜蛇中亚眼镜蛇毒液的乙酰胆碱酯酶(AcChoEase;乙酰胆碱乙酰水解酶,EC 3.1.1.7)肽段,该肽段用亲和试剂N,N-二甲基-2-苯基氮丙啶(DPA)进行了标记。其序列为甘氨酸-丙氨酸-谷氨酸-甲硫氨酸-色氨酸-天冬酰胺-脯氨酸-天冬酰胺。在来自电鳐的AcChoEase中,一个同源肽段被标记并分离出来。其序列为丝氨酸-甘氨酸-丝氨酸-谷氨酸-甲硫氨酸-色氨酸-天冬酰胺-脯氨酸-天冬酰胺,对应第79至87位。在这两种情况下,0.1 mM依酚氯铵均可阻止标记,表明各自的肽段构成催化中心阴离子亚位点的一部分。两种酶中被修饰的残基均为色氨酸(电鳐AcChoEase中的Trp-84)。与来自电鳐的AcChoEase不同,眼镜蛇毒液中的酶不含有外周阴离子结合位点。

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本文引用的文献

1
The enzymic hydrolysis and synthesis of acetylcholine.乙酰胆碱的酶促水解与合成
Adv Enzymol Relat Subj Biochem. 1951;12:259-339. doi: 10.1002/9780470122570.ch5.
3
Spectral evidence for the presence of tryptophan in the binding site of acetylcholinesterase.
FEBS Lett. 1973 Feb 15;30(1):125-128. doi: 10.1016/0014-5793(73)80633-7.

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