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Bacillus is a genus of Gram-positive, rod-shaped bacteria, a member of the phylum Bacillota, with 266 named species. The term is also used to describe the shape (rod) of other so-shaped bacteria; and the plural Bacilli is the name of the class of bacteria to which this genus belongs. Bacillus species can be either obligate aerobes which are dependent on oxygen, or facultative anaerobes which can survive in the absence of oxygen. Cultured Bacillus species test positive for the enzyme catalase if oxygen has been used or is present.
Bacillus cereus is a Gram-positive rod-shaped bacterium commonly found in soil, food, and marine sponges. The specific name, cereus, meaning "waxy" in Latin, refers to the appearance of colonies grown on blood agar. Some strains are harmful to humans and cause foodborne illness due to their spore-forming nature, while other strains can be beneficial as probiotics for animals, and even exhibit mutualism with certain plants. B. cereus bacteria may be anaerobes or facultative anaerobes, and like other members of the genus Bacillus, can produce protective endospores. They have a wide range of virulence factors, including phospholipase C, cereulide, sphingomyelinase, metalloproteases, and cytotoxin K, many of which are regulated via quorum sensing. B. cereus strains exhibit flagellar motility.
Autolysins are endogenous lytic enzymes that break down the peptidoglycan components of biological cells which enables the separation of daughter cells following cell division. They are involved in cell growth, cell wall metabolism, cell division and separation, as well as peptidoglycan turnover and have similar functions to lysozymes.
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.
Microbial collagenase is an enzyme. This enzyme catalyses the following chemical reaction
Subtilisin is a protease initially obtained from Bacillus subtilis.
Thermolysin is a thermostable neutral metalloproteinase enzyme produced by the Gram-positive bacteria Bacillus thermoproteolyticus. It requires one zinc ion for enzyme activity and four calcium ions for structural stability. Thermolysin specifically catalyzes the hydrolysis of peptide bonds containing hydrophobic amino acids. However thermolysin is also widely used for peptide bond formation through the reverse reaction of hydrolysis. Thermolysin is the most stable member of a family of metalloproteinases produced by various Bacillus species. These enzymes are also termed 'neutral' proteinases or thermolysin -like proteinases (TLPs).
Glycerol dehydrogenase (EC 1.1.1.6, also known as NAD+-linked glycerol dehydrogenase, glycerol: NAD+ 2-oxidoreductase, GDH, GlDH, GlyDH) is an enzyme in the oxidoreductase family that utilizes the NAD+ to catalyze the oxidation of glycerol to form glycerone (dihydroxyacetone).
In enzymology, an alanine racemase is an enzyme that catalyzes the chemical reaction
Rsa RNAs are non-coding RNAs found in the bacterium Staphylococcus aureus. The shared name comes from their discovery, and does not imply homology. Bioinformatics scans identified the 16 Rsa RNA families named RsaA-K and RsaOA-OG. Others, RsaOH-OX, were found thanks to an RNomic approach. Although the RNAs showed varying expression patterns, many of the newly discovered RNAs were shown to be Hfq-independent and most carried a C-rich motif (UCCC).
Acetoin dehydrogenase (EC 2.3.1.190, acetoin dehydrogenase complex, acetoin dehydrogenase enzyme system, AoDH ES) is an enzyme with systematic name acetyl-CoA:acetoin O-acetyltransferase. This enzyme catalyses the following chemical reaction
Streptogrisin B is an enzyme. This enzyme catalyses the following chemical reaction
SpoIVB peptidase is an enzyme. This enzyme catalyses the following chemical reaction
Scytalidocarboxyl peptidase B, also known as Scytalidoglutamic peptidase and Scytalidopepsin B is a proteolytic enzyme. It was previously thought to be an aspartic protease, but determination of its molecular structure showed it to belong a novel group of proteases, glutamic protease.
Serralysin is an enzyme. This enzyme catalyses the following chemical reaction
Vibriolysin is an enzyme. This enzyme catalyses the following chemical reaction
Pseudolysin is an enzyme. This enzyme catalyses the following chemical reaction
Beta-lytic metalloendopeptidase is an enzyme. This enzyme catalyses the following chemical reaction
2-hydroxymuconate tautomerase is an enzyme with systematic name (2Z,4E)-2-hydroxyhexa-2,4-dienedioate keto-enol isomerase. This enzyme catalyses the following chemical reaction
The Monovalent Cation (K+ or Na+):Proton Antiporter-3 (CPA3) Family (TC# 2.A.63) is a member of the Na+ transporting Mrp superfamily. The CPA3 family consists of bacterial multicomponent K+:H+ and Na+:H+ antiporters. The best characterized systems are the PhaABCDEFG system of Sinorhizobium meliloti (TC# 2.A.63.1.1) that functions in pH adaptation and as a K+ efflux system, and the MnhABCDEFG system of Staphylococcus aureus (TC# 2.A.63.1.3) that functions as a Na+ efflux Na+:H+ antiporter.
References
- ↑ Morihara K, Tsuzuki H, Oka T (March 1968). "Comparison of the specificities of various neutral proteinases from microorganisms". Archives of Biochemistry and Biophysics. 123 (3): 572–88. doi:10.1016/0003-9861(68)90179-3. PMID 4967801.
- ↑ Millet J, Acher R (July 1969). "[Specificity of megateriopeptidase: an amino-endopeptidase with hydrophobic characteristics]". European Journal of Biochemistry. 9 (4): 456–62. doi: 10.1111/j.1432-1033.1969.tb00631.x . PMID 4980359.
- ↑ Feder J, Keay L, Garrett LR, Cirulis N, Moseley MH, Wildi BS (October 1971). "Bacillus cereus neutral protease". Biochimica et Biophysica Acta (BBA) - Protein Structure. 251 (1): 74–8. doi:10.1016/0005-2795(71)90061-4. PMID 5002444.
- ↑ Holmquist B, Vallee BL (January 1976). "Esterase activity of zinc neutral proteases". Biochemistry. 15 (1): 101–7. doi:10.1021/bi00646a016. PMID 2276.
- ↑ Vasantha N, Thompson LD, Rhodes C, Banner C, Nagle J, Filpula D (September 1984). "Genes for alkaline protease and neutral protease from Bacillus amyloliquefaciens contain a large open reading frame between the regions coding for signal sequence and mature protein". Journal of Bacteriology. 159 (3): 811–9. doi:10.1128/JB.159.3.811-819.1984. PMC 215730 . PMID 6090391.
- ↑ Yang MY, Ferrari E, Henner DJ (October 1984). "Cloning of the neutral protease gene of Bacillus subtilis and the use of the cloned gene to create an in vitro-derived deletion mutation". Journal of Bacteriology. 160 (1): 15–21. doi:10.1128/JB.160.1.15-21.1984. PMC 214674 . PMID 6090407.
- ↑ Takagi M, Imanaka T, Aiba S (September 1985). "Nucleotide sequence and promoter region for the neutral protease gene from Bacillus stearothermophilus". Journal of Bacteriology. 163 (3): 824–31. doi:10.1128/JB.163.3.824-831.1985. PMC 219205 . PMID 2993245.
- ↑ Sidler W, Niederer E, Suter F, Zuber H (July 1986). "The primary structure of Bacillus cereus neutral proteinase and comparison with thermolysin and Bacillus subtilis neutral proteinase". Biological Chemistry Hoppe-Seyler. 367 (7): 643–57. doi:10.1515/bchm3.1986.367.2.643. PMID 3092843.
- ↑ Pauptit RA, Karlsson R, Picot D, Jenkins JA, Niklaus-Reimer AS, Jansonius JN (February 1988). "Crystal structure of neutral protease from Bacillus cereus refined at 3.0 A resolution and comparison with the homologous but more thermostable enzyme thermolysin". Journal of Molecular Biology. 199 (3): 525–37. doi:10.1016/0022-2836(88)90623-7. PMID 3127592.
- ↑ Stoeva S, Kleinschmidt T, Mesrob B, Braunitzer G (January 1990). "Primary structure of a zinc protease from Bacillus mesentericus strain 76". Biochemistry. 29 (2): 527–34. doi:10.1021/bi00454a029. PMID 2302386.
