人类胆碱酯酶、电鳐乙酰胆碱酯酶和白地霉脂肪酶的序列相似性是否揭示了活性位点丝氨酸残基？ - Suppr

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超能文献

Does sequence similarity of human choline esterase, Torpedo acetylcholine esterase and Geotrichum candidum lipase reveal the active site serine residue?

作者信息

Slabas A R, Windust J, Sidebottom C M

出版信息

Biochem J. 1990 Jul 1;269(1):279-80. doi: 10.1042/bj2690279.

DOI:10.1042/bj2690279

PMID:2115773

原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC1131568/

Abstract

摘要

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/5020/1131568/c65e3cd22b39/biochemj00180-0267-a.jpg

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Does sequence similarity of human choline esterase, Torpedo acetylcholine esterase and Geotrichum candidum lipase reveal the active site serine residue?人类胆碱酯酶、电鳐乙酰胆碱酯酶和白地霉脂肪酶的序列相似性是否揭示了活性位点丝氨酸残基？

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Modification of carboxyl groups in Geotrichum candidum lipase.

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Relationship between sequence conservation and three-dimensional structure in a large family of esterases, lipases, and related proteins.一大类酯酶、脂肪酶及相关蛋白质中序列保守性与三维结构之间的关系。

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本文引用的文献

Primary structures of the catalytic subunits from two molecular forms of acetylcholinesterase. A comparison of NH2-terminal and active center sequences.两种分子形式的乙酰胆碱酯酶催化亚基的一级结构。氨基末端和活性中心序列的比较。

J Biol Chem. 1985 Oct 5;260(22):12185-9.

Complete amino acid sequence of human serum cholinesterase.人血清胆碱酯酶的完整氨基酸序列

J Biol Chem. 1987 Jan 15;262(2):549-57.

Crystallization and preliminary X-ray diffraction analysis of 11 S acetylcholinesterase.11S 乙酰胆碱酯酶的结晶及初步 X 射线衍射分析

J Biol Chem. 1988 Jul 15;263(20):9795-800.

cDNA sequences of Torpedo marmorata acetylcholinesterase: primary structure of the precursor of a catalytic subunit; existence of multiple 5'-untranslated regions.电鳐乙酰胆碱酯酶的cDNA序列：催化亚基前体的一级结构；多个5'-非翻译区的存在

EMBO J. 1987 Jul;6(7):1865-73. doi: 10.1002/j.1460-2075.1987.tb02445.x.

cDNA molecular cloning of Geotrichum candidum lipase.白地霉脂肪酶的cDNA分子克隆

J Biochem. 1989 Sep;106(3):383-8. doi: 10.1093/oxfordjournals.jbchem.a122862.

Low resolution crystal structure of lipase from Geotrichum candidum (ATCC34614).

J Biochem. 1979 Dec;86(6):1821-7. doi: 10.1093/oxfordjournals.jbchem.a132704.

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