|
Glutamyl Endopeptidase I
Glutamyl endopeptidase I is a family of extracellular bacterial serine proteases. The proteases within this family have been identified in species of ''Staphylococcus'', ''Bacillus'', and ''Streptomyces'', among others. The two former are more closely related, while the ''Streptomyces''-type is treated as a separate family, glutamyl endopeptidase II. Identified proteases ''Staphylococcus'' * ''Staphylococcus aureus, S. aureus'' glutamyl endopeptidase GluV8 : The first discovered enzyme of this family, and the most well characterized, was isolated from the ''Staphylococcus aureus'' strain V8, and hence better known as "V8 protease". Other common references to this protease are staphylococcal serine protease, and SspA from its corresponding gene. * ''Staphylococcus epidermidis, S. epidermidis'' glutamyl endopeptidase GluSE : Also called ''S. epidermidis'' serine protease (Esp). * ''Staphylococcus warneri, S. warneri'' glutamyl endopeptidase GluSW : Also referred to as PROM. ''B ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Bacteria
Bacteria (; singular: bacterium) are ubiquitous, mostly free-living organisms often consisting of one biological cell. They constitute a large domain of prokaryotic microorganisms. Typically a few micrometres in length, bacteria were among the first life forms to appear on Earth, and are present in most of its habitats. Bacteria inhabit soil, water, acidic hot springs, radioactive waste, and the deep biosphere of Earth's crust. Bacteria are vital in many stages of the nutrient cycle by recycling nutrients such as the fixation of nitrogen from the atmosphere. The nutrient cycle includes the decomposition of dead bodies; bacteria are responsible for the putrefaction stage in this process. In the biological communities surrounding hydrothermal vents and cold seeps, extremophile bacteria provide the nutrients needed to sustain life by converting dissolved compounds, such as hydrogen sulphide and methane, to energy. Bacteria also live in symbiotic and parasitic relationsh ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Bacillus Subtilis
''Bacillus subtilis'', known also as the hay bacillus or grass bacillus, is a Gram-positive, catalase-positive bacterium, found in soil and the gastrointestinal tract of ruminants, humans and marine sponges. As a member of the genus ''Bacillus'', ''B. subtilis'' is rod-shaped, and can form a tough, protective endospore, allowing it to tolerate extreme environmental conditions. ''B. subtilis'' has historically been classified as an obligate aerobe, though evidence exists that it is a facultative anaerobe. ''B. subtilis'' is considered the best studied Gram-positive bacterium and a model organism to study bacterial chromosome replication and cell differentiation. It is one of the bacterial champions in secreted enzyme production and used on an industrial scale by biotechnology companies. Description ''Bacillus subtilis'' is a Gram-positive bacterium, rod-shaped and catalase-positive. It was originally named ''Vibrio subtilis'' by Christian Gottfried Ehrenberg, and renamed ''B ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Proteolysis
Proteolysis is the breakdown of proteins into smaller polypeptides or amino acids. Uncatalysed, the hydrolysis of peptide bonds is extremely slow, taking hundreds of years. Proteolysis is typically catalysed by cellular enzymes called proteases, but may also occur by intra-molecular digestion. Proteolysis in organisms serves many purposes; for example, digestive enzymes break down proteins in food to provide amino acids for the organism, while proteolytic processing of a polypeptide chain after its synthesis may be necessary for the production of an active protein. It is also important in the regulation of some physiological and cellular processes including apoptosis, as well as preventing the accumulation of unwanted or misfolded proteins in cells. Consequently, abnormality in the regulation of proteolysis can cause disease. Proteolysis can also be used as an analytical tool for studying proteins in the laboratory, and it may also be used in industry, for example in food proc ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Biofilm
A biofilm comprises any syntrophic consortium of microorganisms in which cells stick to each other and often also to a surface. These adherent cells become embedded within a slimy extracellular matrix that is composed of extracellular polymeric substances (EPSs). The cells within the biofilm produce the EPS components, which are typically a polymeric conglomeration of extracellular polysaccharides, proteins, lipids and DNA. Because they have three-dimensional structure and represent a community lifestyle for microorganisms, they have been metaphorically described as "cities for microbes". Biofilms may form on living or non-living surfaces and can be prevalent in natural, industrial, and hospital settings. They may constitute a microbiome or be a portion of it. The microbial cells growing in a biofilm are physiologically distinct from planktonic cells of the same organism, which, by contrast, are single cells that may float or swim in a liquid medium. Biofilms can form ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Aureolysin
Aureolysin (, ''protease III, staphylococcal metalloprotease,'' ''Staphylococcus aureus neutral proteinase'') is an extracellular metalloprotease expressed by ''Staphylococcus aureus''. This protease is a major contributor to the bacterium's virulence, or ability to cause disease, by cleaving host factors of the innate immune system as well as regulating S. aureus secreted toxins and cell wall proteins. To catalyze its enzymatic activities, aureolysin requires zinc and calcium which it obtains from the extracellular environment within the host. Genetics Aureolysin is expressed from the gene ''aur'', which is located on a monocistronic operon. The gene exists in two allelic forms but the sequence is highly conserved with 89% homology between the two. The gene contains a coding sequence of 1,527 nucleotides that translates into a pre-pro-form of the enzyme that is 509 amino acids long. Of the 509 amino acids, only 301 denote the mature form of aureolysin. After translation, the pre- ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Metalloproteinase
A metalloproteinase, or metalloprotease, is any protease enzyme whose catalytic mechanism involves a metal. An example is ADAM12 which plays a significant role in the fusion of muscle cells during embryo development, in a process known as myogenesis. Most metalloproteases require zinc, but some use cobalt. The metal ion is coordinated to the protein via three ligands. The ligands coordinating the metal ion can vary with histidine, glutamate, aspartate, lysine, and arginine. The fourth coordination position is taken up by a labile water molecule. Treatment with chelating agents such as EDTA leads to complete inactivation. EDTA is a metal chelator that removes zinc, which is essential for activity. They are also inhibited by the chelator orthophenanthroline. Classification There are two subgroups of metalloproteinases: * Exopeptidases, metalloexopeptidases ( EC number: 3.4.17). * Endopeptidases, metalloendopeptidases (3.4.24). Well known metalloendopeptidases include ADAM pr ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Zymogen
In biochemistry, a zymogen (), also called a proenzyme (), is an inactive precursor of an enzyme. A zymogen requires a biochemical change (such as a hydrolysis reaction revealing the active site, or changing the configuration to reveal the active site) for it to become an active enzyme. The biochemical change usually occurs in Golgi bodies, where a specific part of the precursor enzyme is cleaved in order to activate it. The inactivating piece which is cleaved off can be a peptide unit, or can be independently-folding domains comprising more than 100 residues. Although they limit the enzyme's ability, these N-terminal extensions of the enzyme or a “prosegment” often aid in the stabilization and folding of the enzyme they inhibit. The pancreas secretes zymogens partly to prevent the enzymes from digesting proteins in the cells in which they are synthesised. Enzymes like pepsin are created in the form of pepsinogen, an inactive zymogen. Pepsinogen is activated when chief ce ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Enterococcus Faecalis
''Enterococcus faecalis'' – formerly classified as part of the group D ''Streptococcus'' system – is a Gram-positive, commensal bacterium inhabiting the gastrointestinal tracts of humans. Like other species in the genus ''Enterococcus'', ''E. faecalis'' is found in healthy humans and can be used as a probiotic. The probiotic strains such as Symbioflor1 and EF-2001 are characterized by the lack of specific genes related to drug resistance and pathogenesis. As an opportunistic pathogen, ''E. faecalis'' can cause life-threatening infections, especially in the nosocomial (hospital) environment, where the naturally high levels of antibiotic resistance found in ''E. faecalis'' contribute to its pathogenicity. ''E. faecalis'' has been frequently found in reinfected, root canal-treated teeth in prevalence values ranging from 30% to 90% of the cases. Re-infected root canal-treated teeth are about nine times more likely to harbor ''E. faecalis'' than cases of primary infections. Physi ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Enterococcus
''Enterococcus'' is a large genus of lactic acid bacteria of the phylum Bacillota. Enterococci are gram-positive cocci that often occur in pairs (diplococci) or short chains, and are difficult to distinguish from streptococci on physical characteristics alone. Two species are common commensal organisms in the intestines of humans: '' E. faecalis'' (90–95%) and '' E. faecium'' (5–10%). Rare clusters of infections occur with other species, including ''E. casseliflavus'', '' E. gallinarum'', and ''E. raffinosus''. Physiology and classification Enterococci are facultative anaerobic organisms, i.e., they are capable of cellular respiration in both oxygen-rich and oxygen-poor environments. Though they are not capable of forming spores, enterococci are tolerant of a wide range of environmental conditions: extreme temperature (10–45 °C), pH (4.6–9.9), and high sodium chloride concentrations. Enterococci typically exhibit gamma-hemolysis on sheep's blood agar. History ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Staphylococcus Warneri
''Staphylococcus warneri'' is a member of the bacterial genus ''Staphylococcus'', consisting of Gram-positive bacteria with spherical cells appearing in clusters. It is catalase-positive, oxidase-negative, and coagulase-negative, and is a common commensal organism found as part of the skin flora on humans and animals. Like other coagulase-negative staphylococci, ''S. warneri'' rarely causes disease, but may occasionally cause infection in patients whose immune system is compromised. Identification Colonies of ''S. warneri'' on trypticase soy agar are usually beige, tan, or yellow, sometimes with an orange rim and about 2–4 mm in diameter after 48 hours' incubation at 35 °C. Optimal growth temperature is 30-40 °C. Clinical importance ''Staphylococcus warneri'' has been suggested as a cause of spontaneous abortion in cattle and humans.Barigye R, Schaan L, Gibbs PS, Schamber E, Dyer, NW (2007). Diagnostic evidence of ''Staphylococcus warneri'' as a possible cause ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Serine Protease
Serine proteases (or serine endopeptidases) are enzymes that cleave peptide bonds in proteins. Serine serves as the nucleophilic amino acid at the (enzyme's) active site. They are found ubiquitously in both eukaryotes and prokaryotes. Serine proteases fall into two broad categories based on their structure: chymotrypsin-like (trypsin-like) or subtilisin-like. Classification The MEROPS protease classification system counts 16 superfamilies (as of 2013) each containing many families. Each superfamily uses the catalytic triad or dyad in a different protein fold and so represent convergent evolution of the catalytic mechanism. The majority belong to the S1 family of the PA clan (superfamily) of proteases. For superfamilies, P: superfamily, containing a mixture of nucleophile class families, S: purely serine proteases. superfamily. Within each superfamily, families are designated by their catalytic nucleophile, (S: serine proteases). Substrate specificity Serine ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Staphylococcus Epidermidis
''Staphylococcus epidermidis'' is a Gram-positive bacterium, and one of over 40 species belonging to the genus '' Staphylococcus''. It is part of the normal human microbiota, typically the skin microbiota, and less commonly the mucosal microbiota and also found in marine sponges. It is a facultative anaerobic bacteria. Although ''S. epidermidis'' is not usually pathogenic, patients with compromised immune systems are at risk of developing infection. These infections are generally hospital-acquired. ''S. epidermidis'' is a particular concern for people with catheters or other surgical implants because it is known to form biofilms that grow on these devices. Being part of the normal skin microbiota, ''S. epidermidis'' is a frequent contaminant of specimens sent to the diagnostic laboratory. Some strains of ''S. epidermidis'' are highly salt tolerant and commonly found in marine environment. S.I. Paul et al. (2021) isolated and identified salt tolerant strains of ''S. epiderm ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
