Granger M, Tesser G I, De Jong W W, Bloemendal H
Proc Natl Acad Sci U S A. 1976 Sep;73(9):3010-4. doi: 10.1073/pnas.73.9.3010.
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.
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。