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Subtilisin
Subtilisin is a protease (a protein-digesting enzyme) initially obtained from ''Bacillus subtilis''. Subtilisins belong to subtilases, a group of serine proteases that – like all serine proteases – initiate the nucleophilic attack on the peptide (amide) bond through a serine residue at the active site. Subtilisins typically have molecular weights 27kDa. They can be obtained from certain types of soil bacteria, for example, '' Bacillus amyloliquefaciens'' from which they are secreted in large amounts. Nomenclature "Subtilisin" does not refer to a single protein, but to an entire clade under subtilases containing the classical subtilisins. The clade can be further divided into four groups: "true subtilisins" (containing the classical members), "high-alkaline subtilisins", "intracellular subtilisins", and "phylogenetically intermediate subtilisins" (PIS). Notable subtilisins include: Other non-commercial names include ''ALK-enzyme'', ''bacillopeptidase'', ''Bacillus ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Subtilase
Subtilases are a protein family, family of subtilisin-like serine proteases. They appear to have independently and convergently evolved an Aspartate, Asp/Serine, Ser/Histidine, His catalytic triad, like in the trypsin, trypsin serine proteases. The structure of proteins in this family shows that they have an alpha/beta fold containing a 7-stranded parallel beta sheet. The subtilisin family is the second largest serine protease family characterised to date. Over 200 subtilases are presently known, more than 170 of which with their complete amino acid sequence. Subtilase is widespread, being found in eubacteria, archaebacteria, eukaryotes and viruses. The vast majority of the family are endopeptidases, although there is an exopeptidase, tripeptidyl peptidase. Structures have been determined for several members of the subtilisin family showing that subtilisins exploit the same catalytic triad as the chymotrypsins although the residues occur in a different order (His/Asp/Ser in chymotr ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Catalytic Triad
A catalytic triad is a set of three coordinated amino acid residues that can be found in the active site of some enzymes. Catalytic triads are most commonly found in hydrolase and transferase enzymes (e.g. proteases, amidases, esterases, aminoacylase, acylases, lipases and β-lactamases). An acid-base (chemistry), base-nucleophile triad is a common motif for generating a nucleophilic residue for covalent catalysis. The residues form a charge-relay network to polarise and activate the nucleophile, which attacks the Substrate (chemistry), substrate, forming a covalent intermediate which is then hydrolysed to release the Product (chemistry), product and regenerate free enzyme. The nucleophile is most commonly a serine or cysteine, but occasionally threonine or even selenocysteine. The Protein tertiary structure, 3D structure of the enzyme brings together the triad residues in a precise orientation, even though they may be far apart in the sequence (Protein primary structure, primary ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Proteolysis
Proteolysis is the breakdown of proteins into smaller polypeptides or amino acids. Protein degradation is a major regulatory mechanism of gene expression and contributes substantially to shaping mammalian proteomes. 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 diseases. Proteolysis can also ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Convergent Evolution
Convergent evolution is the independent evolution of similar features in species of different periods or epochs in time. Convergent evolution creates analogous structures that have similar form or function but were not present in the last common ancestor of those groups. The cladistic term for the same phenomenon is Cladogram#Homoplasies, homoplasy. The recurrent evolution of flight is a classic example, as flying pterygota, insects, birds, pterosaurs, and bats have independently evolved the useful capacity of flight. Functionally similar features that have arisen through convergent evolution are ''analogous'', whereas ''homology (biology), homologous'' structures or traits have a common origin but can have dissimilar functions. Bird, bat, and pterosaur wings are analogous structures, but their forelimbs are homologous, sharing an ancestral state despite serving different functions. The opposite of convergence is divergent evolution, where related species evolve different trai ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Alpha-helix
An alpha helix (or α-helix) is a sequence of amino acids in a protein that are twisted into a coil (a helix). The alpha helix is the most common structural arrangement in the secondary structure of proteins. It is also the most extreme type of local structure, and it is the local structure that is most easily predicted from a sequence of amino acids. The alpha helix has a right-handed helix conformation in which every backbone N−H group hydrogen bonds to the backbone C=O group of the amino acid that is four residues earlier in the protein sequence. Other names The alpha helix is also commonly called a: * Pauling–Corey–Branson α-helix (from the names of three scientists who described its structure) * 3.613-helix because there are 3.6 amino acids in one ring, with 13 atoms being involved in the ring formed by the hydrogen bond (starting with amidic hydrogen and ending with carbonyl oxygen) Discovery In the early 1930s, William Astbury showed that there were d ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Bacillus Amyloliquefaciens
''Bacillus amyloliquefaciens'' is a species of bacterium in the genus ''Bacillus'' that is the source of the BamHI restriction enzyme. It also synthesizes a natural antibiotic protein barnase, a widely studied ribonuclease that forms a famously tight complex with its intracellular inhibitor barstar, and plantazolicin, an antibiotic with selective activity against ''Bacillus anthracis''. It is used in agriculture, aquaculture, and hydroponics to fight root pathogens such as ''Ralstonia solanacearum,'' ''Pythium'', ''Rhizoctonia solani'', ''Alternaria tenuissima'' and ''Fusarium'' as well improve root tolerance to salt stress. They are considered a growth-promoting rhizobacteria and have the ability to quickly colonize roots. Discovery and name ''Bacillus amyloliquefaciens'' was first isolated from the soil 1943 by the Japanese scientist Juichiro Fukumoto, who gave the bacterium its name because it produced (''faciens'') a liquifying (''lique'') amylase (''amylo''). Uses Alpha a ... [...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 protein superfamily, superfamilies (as of 2013) each containing many protein family, 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 protein superfamily, superfamilies, P: superfamily, containing a mixture of nucleophile class families, S: purely serine proteases. superfamily. Within each superfamily, protein family, families are designated by their catalytic nucl ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Geobacillus Stearothermophilus
''Geobacillus stearothermophilus'' (previously ''Bacillus stearothermophilus'') is a rod-shaped, Gram-positive bacterium and a member of the phylum Bacillota. The bacterium is a thermophile and is widely distributed in soil, hot springs, ocean sediment, and is a cause of spoilage in food products. It will grow within a temperature range of 30–75 °C. Some strains are capable of oxidizing carbon monoxide aerobically. It is commonly used as a challenge organism for sterilization validation studies and periodic check of sterilization cycles. The biological indicator contains spores of the organism on filter paper inside a vial. After sterilizing, the cap is closed, an ampule of growth medium inside of the vial is crushed and the whole vial is incubated. A color and/or turbidity change indicates the results of the sterilization process; no change indicates that the sterilization conditions were achieved, otherwise the growth of the spores indicates that the sterilizati ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Globular Protein
In biochemistry, globular proteins or spheroproteins are spherical ("globe-like") proteins and are one of the common protein types (the others being fibrous, disordered and membrane proteins). Globular proteins are somewhat water-soluble (forming colloids in water), unlike the fibrous or membrane proteins. There are multiple fold classes of globular proteins, since there are many different architectures that can fold into a roughly spherical shape. The term globin can refer more specifically to proteins including the globin fold. Globular structure and solubility The term globular protein is quite old (dating probably from the 19th century) and is now somewhat archaic given the hundreds of thousands of proteins and more elegant and descriptive structural motif vocabulary. The globular nature of these proteins can be determined without the means of modern techniques, but only by using ultracentrifuges or dynamic light scattering techniques. The spherical structure is induce ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
X-ray Crystallography
X-ray crystallography is the experimental science of determining the atomic and molecular structure of a crystal, in which the crystalline structure causes a beam of incident X-rays to Diffraction, diffract in specific directions. By measuring the angles and intensities of the X-ray diffraction, a crystallography, crystallographer can produce a three-dimensional picture of the density of electrons within the crystal and the positions of the atoms, as well as their chemical bonds, crystallographic disorder, and other information. X-ray crystallography has been fundamental in the development of many scientific fields. In its first decades of use, this method determined the size of atoms, the lengths and types of chemical bonds, and the atomic-scale differences between various materials, especially minerals and alloys. The method has also revealed the structure and function of many biological molecules, including vitamins, drugs, proteins and nucleic acids such as DNA. X-ray crystall ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Beta-sheet
The beta sheet (β-sheet, also β-pleated sheet) is a common structural motif, motif of the regular protein secondary structure. Beta sheets consist of beta strands (β-strands) connected laterally by at least two or three backbone chain, backbone hydrogen bonds, forming a generally twisted, pleated sheet. A β-strand is a stretch of peptide, polypeptide chain typically 3 to 10 amino acids long with backbone in an extended conformational isomerism, conformation. The supramolecular association of β-sheets has been implicated in the formation of the Amyloid fibril, fibrils and Amyloid plaques, protein aggregates observed in amyloidosis, Alzheimer's disease and other Proteinopathy, proteinopathies. History The first β-sheet structure was proposed by William Astbury in the 1930s. He proposed the idea of hydrogen bonding between the peptide bonds of parallel or antiparallel extended β-strands. However, Astbury did not have the necessary data on the bond geometry of the amino acids ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
