A chymosin-like extracellular acidic endoprotease fromMyxococcus xanthusDK101
| Autor: | Yves Cenatiempo, Joel Raingeaud, Nathalie Lucas, J.R. Carias, Catherine Mazaud, Raymond Julien, Gilles Vachon |
|---|---|
| Rok vydání: | 1990 |
| Předmět: |
food.ingredient
medicine.medical_treatment Rennin Biophysics k-Casein Tripartite protein Biochemistry food Structural Biology Casein K-Casein Genetics medicine Chymosin Myxococcus Myxococcus xanthus Molecular Biology chemistry.chemical_classification Protease biology Myxobacteria Cell Biology Protein engineering biology.organism_classification Enzyme chemistry (Myxococcus xanthus DK101) biology.protein |
| Zdroj: | FEBS Letters. 262:97-100 |
| ISSN: | 0014-5793 |
| DOI: | 10.1016/0014-5793(90)80162-c |
| Popis: | SDS-PAGE and N-tenninal sequence analysis of hydrolysis products from 3 substrates containing a unique sensitive bond usually recognized by chymosin (k-casein, a synthetic hexapeptide and a recombinant tripartite protein) revealed that a 45 kDa endoprotease of Myxococcus xanthus DK101 cleaved the same characteristic Phe-Met bond with high specificity. Such an enzyme, easy to obtain from culture supernatant and to use in acidic conditions, could be a new tool for protein engineering. |
| Databáze: | OpenAIRE |
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