The trypsin-like enzyme from Streptomyces griseus (pronase)

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The specificity of proteinases from Streptomyces griseus (pronase).

Purification of pronase by ion-exchange chromatography gave four proteolytically active fractions. Fraction A(2) contained an endopeptidase that attacks poly l-valine. Fraction B contained an endopeptidase, an aminopeptidase and carboxypeptidases. The activities against hippuryl-l-arginine and hippuryl-l-phenylalanine could be inhibited to a considerable extent by di-isopropyl phosphorofluorida...

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Oxidation of Meloxicam by Streptomyces griseus

The aim of the present investigation was to biotransform the anti-inflammatory compound meloxicam by enzymes present in whole cells of five actinomycete cultures to produce novel bioactive derivatives. Among the actinomycetes screened, Streptomyces griseus NCIM 2622 was found to possess the enzyme system(s) that oxidize meloxicam into two metabolites whereas that present in S. griseus NCIM 2623...

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Improved Production of Active Streptomyces griseus Trypsin with a Novel Auto-Catalyzed Strategy

N-terminal sequences play crucial roles in regulating expression, translation, activation and enzymatic properties of proteins. To reduce cell toxicity of intracellular trypsin and increase secretory expression, we developed a novel auto-catalyzed strategy to produce recombinant trypsin by engineering the N-terminus of mature Streptomyces griseus trypsin (SGT). The engineered N-terminal peptide...

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Transcriptional control by A-factor of two trypsin genes in Streptomyces griseus.

AdpA is the key transcriptional activator for a number of genes of various functions in the A-factor regulatory cascade in Streptomyces griseus, forming an AdpA regulon. Trypsin-like activity was detected at a late stage of growth in the wild-type strain but not in an A-factor-deficient mutant. Consistent with these observations, two trypsin genes, sprT and sprU, in S. griseus were found to be ...

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ژورنال

عنوان ژورنال: Biochemical Journal

سال: 1968

ISSN: 0306-3283

DOI: 10.1042/bj1090475