Shimamura M, Hazato T, Katayama T
Biochim Biophys Acta. 1983 Mar 31;756(2):223-9. doi: 10.1016/0304-4165(83)90095-8.
A membrane-bound aminopeptidase which cleaves the tyrosine-glycine bond of enkephalin was purified about 1600-fold from monkey brain. This aminopeptidase hydrolyzed Leu-enkephalin with a Km value of 35 microM and also hydrolyzed basic, neutral and aromatic amino acid beta-naphthylamides. An apparently homogeneous enzyme consisted of a single polypeptide chain with a molecular weight of approx. 100 000. The optimum pH was in the neutral region. From the analysis of the reaction products, only aminopeptidase activity was detected. The enzyme was inactivated by metal chelators, but the activity could be restored by the addition of divalent cations, such as Co2+, Mg2+ and Zn2+. Puromycin, bestatin and amastatin, which are aminopeptidase inhibitors derived from microorganism, showed strong competitive inhibition of the enzyme, the most potent being amastatin, with a Ki value of 0.02 microM.
一种能裂解脑啡肽酪氨酸 - 甘氨酸键的膜结合氨肽酶从猴脑中纯化出来，纯化倍数约为1600倍。这种氨肽酶水解亮氨酸脑啡肽的Km值为35微摩尔，还能水解碱性、中性和芳香族氨基酸β - 萘酰胺。一种明显均一的酶由一条分子量约为100000的单一多肽链组成。最适pH在中性区域。通过对反应产物的分析，仅检测到氨肽酶活性。该酶被金属螯合剂灭活，但通过添加二价阳离子如Co2 +、Mg2 +和Zn2 +可恢复其活性。嘌呤霉素、贝司他汀和抑氨肽酶素是源自微生物的氨肽酶抑制剂，它们对该酶表现出强烈的竞争性抑制作用，其中抑氨肽酶素最有效，Ki值为0.02微摩尔。
