Substrate specificity of two chymotrypsin-like proteases from rat mast cells. Studies with peptide 4-nitroanilides and comparison with cathepsin G.
Substrate specificity of two chymotrypsin-like proteases from rat mast cells. Studies with peptide 4-nitroanilides and comparison with cathepsin G.
复制标题
来自大鼠肥大细胞的两种胰凝乳蛋白酶样蛋白酶的底物特异性。
DOI：
10.1021/bi00566a021
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发表时间：
1980
期刊：
影响因子：
2.9
通讯作者：
J. Powers
中科院分区：
文献类型：
--
作者：
N. Yoshida;M. Everitt;H. Neurath;R. Woodbury;J. Powers
Norio Yoshida, Michael T. Everitt, Hans Neurath, Richard G. Woodbury, andJames C. Powers* abstract: The substrate specificity of chymotrypsin-like enzymes from typical mast cells, rat mast cell protease I (RMCP I), and from atypical mast cells, rat mast cell protease II (RMCP II), has been investigated with peptide 4-nitro-anilide (NA) substrates and peptide chloromethyl ketone inhibitors. Suc-Phe-Pro-Phe-NA and Suc-Phe-Leu-Phe-NA are the best substrates for both RMCP I and RMCP II. In the case of RMCP II, both the P3 (Phe) and the P4 [succinyl (Sue)] groups are important. Succinyl tetrapeptides with nearly the same sequence were not as sensitive to either rat protease. The pH optimum of the hydrolysis of Suc-Phe-Leu-Phe-NA by RMCP II was pH 6.6 and by RMCP I was ca. pH 8.5. The S2 subsite of RMCP II prefers Thr over either Leu or Pro. The subsite specificity of RMCP II may be explained on the basis of interaction with Asn-86 in S2, a hydrophobic S3 subsite due to the presence of Phe-178, and at pH 6.6, an interaction with a cationic His-200 in the S4 subsite. Suc-Phe-Pro-Phe-NA is the best 4-nitroanilide sub-
