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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.
Cellulase is any of several enzymes produced chiefly by fungi, bacteria, and protozoans that catalyze cellulolysis, the decomposition of cellulose and of some related polysaccharides:
Endo-1,4-β-xylanase is any of a class of enzymes that degrade the linear polysaccharide xylan into xylose, thus breaking down hemicellulose, one of the major components of plant cell walls:
β-Glucosidase is an enzyme that catalyses the following reaction:
Trichoderma reesei is a mesophilic and filamentous fungus. It is an anamorph of the fungus Hypocrea jecorina. T. reesei can secrete large amounts of cellulolytic enzymes. Microbial cellulases have industrial application in the conversion of cellulose, a major component of plant biomass, into glucose.
Trichoderma is a genus of fungi in the family Hypocreaceae that is present in all soils, where they are the most prevalent culturable fungi. Many species in this genus can be characterized as opportunistic avirulent plant symbionts. This refers to the ability of several Trichoderma species to form mutualistic endophytic relationships with several plant species. The genomes of several Trichoderma specieshave been sequenced and are publicly available from the JGI.
The enzyme mannosyl-glycoprotein endo-β-N-acetylglucosaminidase (endoglycosidase H) (EC 3.2.1.96) has systematic name glycopeptide-D-mannosyl-N4-(N-acetyl-D-glucosaminyl)2-asparagine 1,4-N-acetyl-β-glucosaminohydrolase. It is a highly specific endoglycosidase which cleaves asparagine-linked mannose rich oligosaccharides, but not highly processed complex oligosaccharides from glycoproteins. It is used for research purposes to deglycosylate glycoproteins and to monitor intracellular protein trafficking through the secretory pathway.
The enzyme acetylxylan esterase catalyzes the deacetylation of xylans and xylo-oligosaccharides.
In molecular biology, glycoside hydrolase family 6 is a family of glycoside hydrolases EC 3.2.1., which are a widespread group of enzymes that hydrolyse the glycosidic bond between two or more carbohydrates, or between a carbohydrate and a non-carbohydrate moiety. A classification system for glycoside hydrolases, based on sequence similarity, has led to the definition of >100 different families. This classification is available on the CAZy web site, and also discussed at CAZypedia, an online encyclopedia of carbohydrate active enzymes.
Glucanases are enzymes that break down large polysaccharides via hydrolysis. The product of the hydrolysis reaction is called a glucan, a linear polysaccharide made of up to 1200 glucose monomers, held together with glycosidic bonds. Glucans are abundant in the endosperm cell walls of cereals such as barley, rye, sorghum, rice, and wheat. Glucanases are also referred to as lichenases, hydrolases, glycosidases, glycosyl hydrolases, and/or laminarinases. Many types of glucanases share similar amino acid sequences but vastly different substrates. Of the known endo-glucanases, 1,3-1,4-β-glucanase is considered the most active.
Endo-1,3(4)-β-glucanase -β-D-glucan 3(4)-glucanohydrolase) is an enzyme with systematic name 3(or 4)-β-D-glucan 3(4)-glucanohydrolase. It catalyses the following chemical reaction
Inulinase is an enzyme with systematic name 1-β-D-fructan fructanohydrolase. It catalyses the reaction
Xylan 1,4-β-xylosidase is an enzyme with systematic name 4-β-D-xylan xylohydrolase. This enzyme catalyses the following chemical reaction
Cellulose 1,4-β-cellobiosidase is an enzyme of interest for its capability of converting cellulose to useful chemicals, particularly cellulosic ethanol.
Blood-group-substance endo-1,4-β-galactosidase is an enzyme with systematic name blood-group-substance 4-β-D-galactanohydrolase. It catalyses endohydrolysis of (1→4)-β-D-galactosidic linkages in blood group A and B substances.
Chitosanase is an enzyme with systematic name chitosan N-acetylglucosaminohydrolase. This enzyme catalyses the following chemical reaction
Galactan endo-1,6-beta-galactosidase is an enzyme with systematic name endo-beta-(1->6)-galactanase. This enzyme catalyses the following chemical reaction
The enzyme exo-(1→4)-α-D-glucan lyase (EC 4.2.2.13, α-(1→4)-glucan 1,5-anhydro-D-fructose eliminase, α-1,4-glucan exo-lyase, α-1,4-glucan lyase, GLase) is an enzyme with systematic name (1→4)-α-D-glucan exo-4-lyase (1,5-anhydro-D-fructose-forming). This enzyme catalyses the following chemical reaction
Penicillium decumbens is an anamorph species of the genus of Penicillium which occurs widespread in nature, mainly in subtropical and tropical soil but it also occur in food. Analysis have shown that Penicillium decumbens has antibiotic activity Penicillium decumbens produces the cyclopentenone cyclopenicillone
N-acetyl-β-d-glucosaminidase(EC 3.2.1.30; EC 3.2.1.52) is a mesophilic hydrolase that specifically hydrolyzes N-acetyl-glucosides. The enzyme is found across a wide variety of marine and terrestrial creatures with the primary function of breaking down oligosaccharides in the presence of water. One of the primary functions of the enzyme is to target and hydrolyze oligosaccharides containing chitin. In this chitinase function, the enzyme contributes to the ability of many organisms to break down chitin-containing molecules and subsequently digest or re-uptake environmental chitin, carbon, or nitrogen. The enzyme's crystal structure varies slightly across organisms, but is characterized by three or four domains with one active site. Across proteins, the active site entails an α-β barrel with either an arginine or tryptophan residues in the barrel pocket to bind incoming substrate.
References
- ↑ Nanjo F, Katsumi R, Sakai K (June 1990). "Purification and characterization of an exo-beta-D-glucosaminidase, a novel type of enzyme, from Nocardia orientalis". The Journal of Biological Chemistry. 265 (17): 10088–94. PMID 2351651.
- ↑ Nogawa M, Takahashi H, Kashiwagi A, Ohshima K, Okada H, Morikawa Y (March 1998). "Purification and Characterization of Exo-beta-d-Glucosaminidase from a Cellulolytic Fungus, Trichoderma reesei PC-3-7". Applied and Environmental Microbiology. 64 (3): 890–5. PMC 106342 . PMID 16349528.
- ↑ Fukamizo T, Fleury A, Côté N, Mitsutomi M, Brzezinski R (November 2006). "Exo-beta-D-glucosaminidase from Amycolatopsis orientalis: catalytic residues, sugar recognition specificity, kinetics, and synergism". Glycobiology. 16 (11): 1064–72. doi: 10.1093/glycob/cwl026 . PMID 16877749.
- ↑ Côté N, Fleury A, Dumont-Blanchette E, Fukamizo T, Mitsutomi M, Brzezinski R (March 2006). "Two exo-beta-D-glucosaminidases/exochitosanases from actinomycetes define a new subfamily within family 2 of glycoside hydrolases". The Biochemical Journal. 394 (Pt 3): 675–86. doi:10.1042/bj20051436. PMC 1383717 . PMID 16316314.
- ↑ Ike M, Isami K, Tanabe Y, Nogawa M, Ogasawara W, Okada H, Morikawa Y (October 2006). "Cloning and heterologous expression of the exo-beta-D-glucosaminidase-encoding gene (gls93) from a filamentous fungus, Trichoderma reesei PC-3-7". Applied Microbiology and Biotechnology. 72 (4): 687–95. doi:10.1007/s00253-006-0320-y. PMID 16636831.
