Jones W M, Manning J M
Biochem Biophys Res Commun. 1985 Jan 31;126(2):933-40. doi: 10.1016/0006-291x(85)90275-x.
Acylpeptide hydrolase, which cleaves the NH2-terminal acetylated or formylated amino acid from a blocked peptide, has been purified to apparent homogeneity from human erythrocytes. The enzyme catalyzes the hydrolysis of a diverse number of peptides and displays different pH optima for certain substrates in doing so. Zinc inhibits to the same extent the hydrolysis of both the most efficient and the least efficient substrates. This enzyme may play a pivotal role in the processing of polypeptide chains during biosynthesis.
酰基肽水解酶可从封闭的肽中裂解出NH2末端乙酰化或甲酰化氨基酸，已从人红细胞中纯化至表观均一。该酶催化多种肽的水解，并且在这样做时对某些底物表现出不同的最适pH值。锌对最有效和最无效底物的水解抑制程度相同。这种酶可能在生物合成过程中多肽链的加工中起关键作用。
