Jones W M, Manning J M
Rockefeller University, New York, NY 10021.
Biochim Biophys Acta. 1988 Apr 14;953(3):357-60. doi: 10.1016/0167-4838(88)90045-3.
An acylaminopeptidase purified from human red cells cleaves acetylated dipeptides in the decreasing order of acetyl-Ala, acetyl-Met, acetyl-Ser, acetyl-Gly and acetyl-Val. In addition, it was also found that the nature of the second amino-acid residue influenced the rate of cleavage of the blocked N-terminus: charged residues at the second position lead to reduced rates of cleavage. The possible use of this enzyme for structural studies on blocked peptide or protein substrates is evaluated.
从人红细胞中纯化得到的一种酰基氨基肽酶，按照乙酰 - 丙氨酸、乙酰 - 甲硫氨酸、乙酰 - 丝氨酸、乙酰 - 甘氨酸和乙酰 - 缬氨酸的顺序，以递减的速率切割乙酰化二肽。此外，还发现第二个氨基酸残基的性质会影响封闭的N - 末端的切割速率：第二个位置的带电荷残基会导致切割速率降低。对该酶在封闭肽或蛋白质底物结构研究中的可能用途进行了评估。
