Toffoletto O, Metters K M, Oliveira E B, Camargo A C, Rossier J
Serviço de Farmacologia Instituto Butantan, Universidade de Sao Paulo, Cidade Universitaria, Brasil.
Biochem J. 1988 May 15;252(1):35-8. doi: 10.1042/bj2520035.
It has been previously reported that both the cysteinyl-endo-oligopeptidase A and the metalloendopeptidase EC 3.4.24.15 are able to generate enkephalin from a number of enkephalin-containing peptides, including dynorphin A1-8. The present study shows that only endo-oligopeptidase A is able to generate [Leu5]enkephalin and [Met5]enkephalin from dynorphin A1-8 and from metorphamide respectively. It is also shown that endo-oligopeptidase A neither hydrolyses the specific EC 3.4.24.15 substrate alpha-N-benzoyl-Gly-Ala-Ala-Phe p-aminobenzoate, nor is inhibited by the specific EC 3.4.24.15 inhibitor N-[1(RS)-carboxy-2-phenylethyl]-alpha-Ala-Ala-Phe p-aminobenzoate.
先前已有报道称，半胱氨酰内肽酶A和金属内肽酶EC 3.4.24.15均能够从多种含脑啡肽的肽类（包括强啡肽A1-8）中生成脑啡肽。本研究表明，只有内肽酶A能够分别从强啡肽A1-8和甲硫啡肽中生成亮氨酸脑啡肽和甲硫氨酸脑啡肽。还表明，内肽酶A既不水解特异性的EC 3.4.24.15底物α-N-苯甲酰基-甘氨酰-丙氨酰-丙氨酰-苯丙氨酸对氨基苯甲酸酯，也不受特异性的EC 3.4.24.15抑制剂N-[1(RS)-羧基-2-苯乙基]-α-丙氨酰-丙氨酰-苯丙氨酸对氨基苯甲酸酯的抑制。
