Alkaline serine protease produced by Streptomyces sp. degrades PrP(Sc).
Alkaline serine protease produced by Streptomyces sp. degrades PrP(Sc).
复制标题
DOI：
10.1016/j.bbrc.2004.06.100
复制
发表时间：
2004-08
影响因子：
3.1
通讯作者：
Z. Hui;Hiroyasu Doi;H. Kanouchi;Y. Matsuura;S. Mohri;Y. Nonomura;T. Oka
中科院分区：
文献类型：
--
作者：
Z. Hui;Hiroyasu Doi;H. Kanouchi;Y. Matsuura;S. Mohri;Y. Nonomura;T. Oka
从链霉菌培养基中分离到一种PrPSc降解酶。以高氯酸可溶性蛋白(PSP)为底物。对500个菌种的培养基进行筛选，获得PSP降解酶。菌株99-GP-2D-5分泌的蛋白酶对PSP的降解活性最高。根据菌株99-GP-2D-5的形态特征和化学分类特征，确定其为链霉菌属。当以羊痒病病毒为底物时，其被酶完全消化。该酶的氨基酸序列与碱性丝氨酸蛋白酶I的C末端氨基酸序列一致，可能是该酶的前体，该酶可能是成熟型的丝氨酸蛋白酶。在60℃、pH 11条件下，该酶的活性最高，在最适条件下3min内可降解羊肚菌蛋白。
A PrPSc-degrading enzyme was isolated from the culture medium of Streptomyces sp. using perchloric acid-soluble protein (PSP) as a substrate. The media of 500 microbial species were screened to obtain the PSP-degrading enzyme. The medium containing the protease secreted from strain 99-GP-2D-5 showed the highest PSP-degrading activity. Strain 99-GP-2D-5 was assigned as the genus Streptomyces by its morphological and chemotaxonomic characteristics. When scrapie prion was used as the substrate, it was completely digested by the enzyme. The amino acid sequence of the enzyme was identical to that of the C-terminal region of alkaline serine protease (ASP) I. ASP I may be the precursor of the enzyme, and the enzyme seems to be the mature type of ASP I. The maximal activity of the enzyme was observed at 60°C and pH 11, and the scrapie prion was degraded within 3min under the optimum conditions.