期刊
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS
卷 512, 期 3, 页码 623-628出版社
ACADEMIC PRESS INC ELSEVIER SCIENCE
DOI: 10.1016/j.bbrc.2019.03.064
关键词
Subtilisin E-S7; Crystal structure; Structural comparisons; ACE-inhibitor; NLN-inhibitor
资金
- National Natural Science Foundation of China [31470160]
- Program for Changjiang Scholars and Innovative Research Team in University [IRT_15R26]
- US National Institutes of Health [R35 GM118047]
- China Scholarship Council fund
The X-ray crystallographic structure of the mature form of subtilisin E-S7 (SES7) at 1.90 A resolution is reported here. Structural comparisons between the previously reported propeptide-subtilisin E complex (1SCJ) and our mature form subtilisin E-S7 (6044) provide insight into active site adjustments involved in catalysis and specificity. To further investigate the protease substrate selectivity mechanism, we used SES7 to hydrolyze skim milk and analyzed the hydrolysates by LC-MS for peptide identification. The cleavage pattern suggests a high preference for proline at substrate P2 position. The results based on the peptide analysis are consistent with our structural observations, which is instrumental in future protein engineering by rational design. Furthermore, the ACE-inhibitor and NLN-inhibitor activity of the hydrolysates were determined to assess the utility of SES7 for further industrial applications; IC50-ACE = 67 +/- 0.92 mu g/mL and IC50-NLN = 263 +/- 13 mu g/mL. (C) 2019 Published by Elsevier Inc.
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