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A chymosin‐like extracellular acidic endoprotease from Myxococcus xanthus DK101
Author(s) -
Carias Jean-Robert,
Raingeaud Joël,
Mazaud Catherine,
Vachon Gilles,
Lucas Nathalie,
Cenatiempo Yves,
Julien Raymond
Publication year - 1990
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(90)80162-c
Subject(s) - myxococcus xanthus , chymosin , biochemistry , casein , chemistry , enzyme , hydrolysis , recombinant dna , extracellular , protein engineering , gene , mutant
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.