The study of Escherichia coli proteases. Intracellular serine protease of E. coli-an analogue of bacillus proteases. 1979

A Y Strongin, and D I Gorodetsky, and V M Stepanov

Two serine proteases in extracts of Escherichia coli grown to stationary phase were purified to homogeneity using affinity chromatography on gramicidin S-Sepharose 4B. One enzyme was closely related to, if not identical with, the 'trypsin-like' protease II of E. coli. The other was capable of cleaving the subtilisin chromogenic substrate N-carbobenzoxy-L-alanyl-L-alanyl-L-leucine-p-nitroanilide and resembled the intracellular serine proteases of Bacillus spp. The amino acid composition of this E. coli protease was similar to that of the Bacillus licheniformis enzyme. These data indicate a relationship between proteolytic enzymes of evolutionary distant Gram-negative Enterobacteriaceae and Gram-positive spore-forming Bacillus.

UI MeSH Term Description Entries
D008970 Molecular Weight The sum of the weight of all the atoms in a molecule. Molecular Weights,Weight, Molecular,Weights, Molecular
D010447 Peptide Hydrolases Hydrolases that specifically cleave the peptide bonds found in PROTEINS and PEPTIDES. Examples of sub-subclasses for this group include EXOPEPTIDASES and ENDOPEPTIDASES. Peptidase,Peptidases,Peptide Hydrolase,Protease,Proteases,Proteinase,Proteinases,Proteolytic Enzyme,Proteolytic Enzymes,Esteroproteases,Enzyme, Proteolytic,Hydrolase, Peptide
D002847 Chromatography, Agarose A method of gel filtration chromatography using agarose, the non-ionic component of agar, for the separation of compounds with molecular weights up to several million. Chromatography, Sepharose,Agarose Chromatography,Sepharose Chromatography,Agarose Chromatographies,Chromatographies, Agarose,Chromatographies, Sepharose,Sepharose Chromatographies
D004591 Electrophoresis, Polyacrylamide Gel Electrophoresis in which a polyacrylamide gel is used as the diffusion medium. Polyacrylamide Gel Electrophoresis,SDS-PAGE,Sodium Dodecyl Sulfate-PAGE,Gel Electrophoresis, Polyacrylamide,SDS PAGE,Sodium Dodecyl Sulfate PAGE,Sodium Dodecyl Sulfate-PAGEs
D004926 Escherichia coli A species of gram-negative, facultatively anaerobic, rod-shaped bacteria (GRAM-NEGATIVE FACULTATIVELY ANAEROBIC RODS) commonly found in the lower part of the intestine of warm-blooded animals. It is usually nonpathogenic, but some strains are known to produce DIARRHEA and pyogenic infections. Pathogenic strains (virotypes) are classified by their specific pathogenic mechanisms such as toxins (ENTEROTOXIGENIC ESCHERICHIA COLI), etc. Alkalescens-Dispar Group,Bacillus coli,Bacterium coli,Bacterium coli commune,Diffusely Adherent Escherichia coli,E coli,EAggEC,Enteroaggregative Escherichia coli,Enterococcus coli,Diffusely Adherent E. coli,Enteroaggregative E. coli,Enteroinvasive E. coli,Enteroinvasive Escherichia coli
D000596 Amino Acids Organic compounds that generally contain an amino (-NH2) and a carboxyl (-COOH) group. Twenty alpha-amino acids are the subunits which are polymerized to form proteins. Amino Acid,Acid, Amino,Acids, Amino
D001407 Bacillus A genus of BACILLACEAE that are spore-forming, rod-shaped cells. Most species are saprophytic soil forms with only a few species being pathogenic. Bacillus bacterium
D012694 Serine A non-essential amino acid occurring in natural form as the L-isomer. It is synthesized from GLYCINE or THREONINE. It is involved in the biosynthesis of PURINES; PYRIMIDINES; and other amino acids. L-Serine,L Serine
D013379 Substrate Specificity A characteristic feature of enzyme activity in relation to the kind of substrate on which the enzyme or catalytic molecule reacts. Specificities, Substrate,Specificity, Substrate,Substrate Specificities

Related Publications

A Y Strongin, and D I Gorodetsky, and V M Stepanov
July 1977, Biochemical and biophysical research communications,
A Y Strongin, and D I Gorodetsky, and V M Stepanov
January 1991, Archives of microbiology,
A Y Strongin, and D I Gorodetsky, and V M Stepanov
January 2000, Advances in experimental medicine and biology,
A Y Strongin, and D I Gorodetsky, and V M Stepanov
September 1982, Journal of bacteriology,
A Y Strongin, and D I Gorodetsky, and V M Stepanov
January 1987, Journal of bacteriology,
A Y Strongin, and D I Gorodetsky, and V M Stepanov
January 1988, Journal of bacteriology,
A Y Strongin, and D I Gorodetsky, and V M Stepanov
January 2022, Frontiers in immunology,
A Y Strongin, and D I Gorodetsky, and V M Stepanov
July 1981, Biokhimiia (Moscow, Russia),
A Y Strongin, and D I Gorodetsky, and V M Stepanov
August 2020, Current microbiology,
Copied contents to your clipboard!