PMID: 3548827Mar 19, 1987

Purification and properties of a pepstatin-insensitive carboxyl proteinase from a gram-negative bacterium

Biochimica Et Biophysica Acta
K OdaS Murao

Abstract

A carboxyl proteinase was found in the culture filtrate of a Gram-negative bacterium. The optimum for the action of the purified enzyme was approx. pH 3 and its caseinolytic activity was not inhibited by carboxyl proteinase inhibitors, such as pepstatin, Streptomyces pepsin inhibitor and diazoacetyl-DL-norleucine methyl ester. 1,2-epoxy-3-(p-nitrophenoxy)propane modified the enzyme with concomitant loss of its enzyme activity. The enzymatic and physicochemical properties of the enzyme were compared with those of known pepstatin- and diazoacetyl-DL-norleucine methyl ester-insensitive carboxyl proteinases previously reported. To our knowledge, this is the first carboxyl proteinase isolated from bacteria.

References

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Citations

Dec 1, 1973·Proceedings of the National Academy of Sciences of the United States of America·J TangJ P Lanier
May 1, 1959·Archives of Biochemistry and Biophysics·G L ELLMAN
Dec 21, 2011·Infection and Immunity·Kol A ZaremberDavid E Greenberg

Related Concepts

Antibiotic Resistance, Microbial
Proteinase inhibitors, antifibrinolytic
Aspartic Acid Endopeptidases
Peptide Hydrolases
Streptomyces pepsin inhibitor
Oligopeptides
Endopeptidases
Pepstatins
Proteolytic Enzyme
Gram-Negative Bacteria

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