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以去-Nα1-乙酰-α-促黑素为底物的蛋白质氨基末端酶促乙酰化的模型研究。

Model studies of enzymatic NH2-terminal acetylation of porteins with des-Nalpha1-acetyl-alpha-melanotropin as a substrate.

作者信息

Granger M, Tesser G I, De Jong W W, Bloemendal H

出版信息

Proc Natl Acad Sci U S A. 1976 Sep;73(9):3010-4. doi: 10.1073/pnas.73.9.3010.

Abstract

The present study describes the acetylation by an enzyme present in calf lens of a synthetic tridecapeptide [analogous to alpha-melanotropin (alpha-melanocyte stimulating hormone) but lacking the naturally occurring NH2-terminal acetyl group: des-Nalpha1-Ac-alpha-melanotropin]. The reaction is specific for the alpha-amino group of the NH2-terminal amino acid. The minimum length required for the substrate to become acetylated appears to be a sequence of five to eight amino acid residues. Modification of the internal lysine decreases the incorporation of acetate, irrespective of the size of the blocking group.

摘要

本研究描述了小牛晶状体中存在的一种酶对一种合成十三肽[类似于α-促黑素(α-黑素细胞刺激激素),但缺乏天然存在的NH2-末端乙酰基:去-Nα1-Ac-α-促黑素]的乙酰化作用。该反应对NH2-末端氨基酸的α-氨基具有特异性。底物被乙酰化所需的最短长度似乎是五到八个氨基酸残基的序列。内部赖氨酸的修饰会降低乙酸盐的掺入,而与封闭基团的大小无关。

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本文引用的文献

2
RAT LIVER ENZYME DOES NOT ACTIVATE ACETYLAMINO ACIDS.大鼠肝脏酶不会激活乙酰氨基酸。
J Biochem. 1965 Feb;57:176-83. doi: 10.1093/oxfordjournals.jbchem.a128074.
4
Nonenzymatic acetylation of histones with acetyl-CoA.组蛋白与乙酰辅酶A的非酶促乙酰化作用。
Biochim Biophys Acta. 1970 Aug 8;213(2):513-22. doi: 10.1016/0005-2787(70)90058-4.
7
N-terminal acetylation of the nascent chains of alpha-crystallin.
Biochem Biophys Res Commun. 1974 Jun 4;58(3):876-84. doi: 10.1016/s0006-291x(74)80498-5.
8
Synthesis of lens protein in vitro. N-terminal acetylation of alpha-crystallin.
Eur J Biochem. 1973 Sep 21;38(1):79-85. doi: 10.1111/j.1432-1033.1973.tb03036.x.

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