Streptomyces erythraeus Trypsin Inactivates α1-Antitrypsin
| Autor: | Masaru Miyagi, Krishna Vukoti, Chandra Sekhar Rao Kadiyala |
|---|---|
| Jazyk: | angličtina |
| Rok vydání: | 2011 |
| Předmět: |
congenital
hereditary and neonatal diseases and abnormalities Erythraeus Biophysics lac operon Serpin Biochemistry Streptomyces Article 03 medical and health sciences chemistry.chemical_compound Structural Biology Genetics medicine Trypsin Molecular Biology Polyacrylamide gel electrophoresis 030304 developmental biology Streptomyces erythraeus trypsin (SET) Serine protease 0303 health sciences biology Chemistry Hydrolysis 030302 biochemistry & molecular biology Cell Biology biology.organism_classification digestive system diseases 3. Good health respiratory tract diseases α1-Antitrypsin alpha 1-Antitrypsin biology.protein Biocatalysis Soybeans PMSF Trypsin Inhibitors medicine.drug Saccharopolyspora |
| Popis: | Streptomyces erythraeus trypsin (SET) is a serine protease that is secreted extracellularly by S. erythraeus. We investigated the inhibitory effect of α1-antitrypsin on the catalytic activity of SET. Intriguingly, we found that SET is not inhibited by α1-antitrypsin. Our investigations into the molecular mechanism underlying this observation revealed that SET hydrolyzes the Met–Ser bond in the reaction center loop of α1-antitrypsin. However, SET somehow avoids entrapment by α1-antitrypsin. We also confirmed that α1-antitrypsin loses its inhibitory activity after incubation with SET. Thus, our study demonstrates that SET is not only resistant to α1-antitrypsin but also inactivates α1-antitrypsin.Structured summary of protein interactionsBT cleaves alpha1 antitrypsin by protease assay (View interaction)alpha1 antitrypsin and BT bind by comigration in non denaturing gel electrophoresis (View interaction)SET cleaves alpha1 antitrypsin by protease assay (View interaction) |
| Databáze: | OpenAIRE |
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