Structural highlights
Function
SUBT_BACSU Subtilisin is an extracellular alkaline serine protease, it catalyzes the hydrolysis of proteins and peptide amides.
Publication Abstract from PubMed
The X-ray crystallographic structure of the mature form of subtilisin E-S7 (SES7) at 1.90A resolution is reported here. Structural comparisons between the previously reported propeptide-subtilisin E complex (1SCJ) and our mature form subtilisin E-S7 (6O44) 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+/-0.92mug/mL and IC50-NLN=263+/-13mug/mL.
Insight into subtilisin E-S7 cleavage pattern based on crystal structure and hydrolysates peptide analysis.,Tang H, Zhang J, Shi K, Aihara H, Du G Biochem Biophys Res Commun. 2019 Mar 23. pii: S0006-291X(19)30447-4. doi:, 10.1016/j.bbrc.2019.03.064. PMID:30914195[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Tang H, Zhang J, Shi K, Aihara H, Du G. Insight into subtilisin E-S7 cleavage pattern based on crystal structure and hydrolysates peptide analysis. Biochem Biophys Res Commun. 2019 Mar 23. pii: S0006-291X(19)30447-4. doi:, 10.1016/j.bbrc.2019.03.064. PMID:30914195 doi:http://dx.doi.org/10.1016/j.bbrc.2019.03.064
