Abstract:
:An extracellular serine protease produced by a mutant, M1, derived from Streptomyces albogriseolus S-3253 that no longer produces a protease inhibitor (Streptomyces subtilisin inhibitor [SSI]) was isolated. A 20-kDa protein was purified by its affinity for SSI and designated SAM-P20. The amino acid sequence of the amino-terminal region of SAM-P20 revealed high homology with the sequences of Streptomyces griseus proteases A and B, and the gene sequence confirmed the relationships. The sequence also revealed a putative amino acid signal sequence for SAM-P20 that apparently functioned to allow secretion of SAM-P20 from Escherichia coli carrying the recombinant gene. SAM-P20 produced by E. coli cells was shown to be sensitive to SSI inhibition.
journal_name
Appl Environ Microbioljournal_title
Applied and environmental microbiologyauthors
Taguchi S,Odaka A,Watanabe Y,Momose Hdoi
10.1128/AEM.61.1.180-186.1995subject
Has Abstractpub_date
1995-01-01 00:00:00pages
180-6issue
1eissn
0099-2240issn
1098-5336journal_volume
61pub_type
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