the thermostable laminarinase is composed of a GH family 16 catalytic domain flanked by two family 4 carbohydrate-binding modules (CBM4-1 and CBM4-2) at each terminus
the thermostable laminarinase is composed of a GH family 16 catalytic domain flanked by two family 4 carbohydrate-binding modules (CBM4-1 and CBM4-2) at each terminus
killer toxin produced by Debaryomyces hansenii strains TEM8 and TEM17 shows amino acid sequence homologies with enzyme DEHA2G18766p from Debaryomyces hansenii strain CBS 767, overview. The sequence homology between the killer toxins and beta-1,3-glucanase suggests this glucanase activity might be involved in the killing action of the toxins
killer toxin produced by Debaryomyces hansenii strains TEM8 and TEM17 shows amino acid sequence homologies with enzyme DEHA2G18766p from Debaryomyces hansenii strain CBS 767, overview. The sequence homology between the killer toxins and beta-1,3-glucanase suggests this glucanase activity might be involved in the killing action of the toxins
killer toxin produced by Debaryomyces hansenii strains TEM8 and TEM17 shows amino acid sequence homologies with enzyme DEHA2G18766p from Debaryomyces hansenii strain CBS 767, overview. The sequence homology between the killer toxins and beta-1,3-glucanase suggests this glucanase activity might be involved in the killing action of the toxins
killer toxin produced by Debaryomyces hansenii strains TEM8 and TEM17 shows amino acid sequence homologies with enzyme DEHA2G18766p from Debaryomyces hansenii strain CBS 767, overview. The sequence homology between the killer toxins and beta-1,3-glucanase suggests this glucanase activity might be involved in the killing action of the toxins
killer toxin produced by Debaryomyces hansenii strains TEM8 and TEM17 shows amino acid sequence homologies with enzyme DEHA2G18766p from Debaryomyces hansenii strain CBS 767, overview. The sequence homology between the killer toxins and beta-1,3-glucanase suggests this glucanase activity might be involved in the killing action of the toxins
killer toxin produced by Debaryomyces hansenii strains TEM8 and TEM17 shows amino acid sequence homologies with enzyme DEHA2G18766p from Debaryomyces hansenii strain CBS 767, overview. The sequence homology between the killer toxins and beta-1,3-glucanase suggests this glucanase activity might be involved in the killing action of the toxins
BglS27 has the ability to inhibit the growth of phytopathogenic fungi Rhizoctonic solani and Fusarium oxysporum and some mycotoxin-producing fungi Fusarium crookwellense and Paecilomyces variotii
PCEng2 plays a significant role in cell wall regulation, the glucan-rich cyst cell wall is essential for cel viability, and regulation of cyst cell wall beta-glucans is a fundamental process during completion of the Pneumocystis life cycle
When Schizosaccharomyces pombe diploid cells undergo meiosis, they differentiate into asci containing four haploid ascospores that are highly resistant to environmental stress. beta-Glucanase Eng2 and endo-alpha-1,3-glucanase Agn2 are required for ascus wall endolysis after sporulation in Schizosaccharomyces pombe
enzyme is involved in the autolytic cell wall degradation resulting from carbon starvation of the fungus. The deletion of either engA or chiB encoding an endochitinase, causes highly reduced production of hydrolases in general
fibrolytic enzyme which plays an important role in the hydrolysis of polysaccharide components. It hydrolyzes internal beta-1,3-glycosidic linkages in beta-1,3-glucans, which form the main component of the cell wall in yeasts and filamentous fungi and the major structural and storage polysaccharide in marine macroalgae such as Laminaria saccharina
plant endo-1,3-beta-glucanases are involved in important physiological processes such as defence mechanisms, cell division and flowering. Endo-1,3-beta-glucanases in plants are believed to function as part of a defence mechanism against fungi by hydrolyzing the fungal cell wall, which is built mostly of (1,3)-beta-D-glucans
a mutant lacking the activities of GH81 enzyme Eng1 and the activities of GH16 isoforms Eng2 to Eng5 shows conidial defects, with linear chains of conidia unable to separate while the germination rate is not affected. The mutant shows a about 51% decrease in the endo-beta-(1,3)-glucanase activity in in dormant conidia, about 74% in swollen morphotype and about 32% in germinating conidia
Coprinopsis cinerea fruiting bodies produce three glucanases. The endo-1,3-beta-glucanase hydrolyzes internal glycosidic bonds of laminarin to generate 1,3-beta-oligosaccharides of various lengths, the exo-1,3-beta-glucanase cleaves the longer-chain laminarioligosaccharides into short-chain disaccharides, laminaribiose and gentiobiose, and the 1,3-beta-glucosidase further hydrolyzes laminaribiose to glucose
the enzyme exhibits immune stimulating effects via significantly increasing the phagocytic activity of macrophages and inducing the release of nitric oxide, tumor necrosis factor alpha, and interleukin-6 in RAW264.7 cells, overview
Coprinopsis cinerea fruiting bodies produce three glucanases. The endo-1,3-beta-glucanase hydrolyzes internal glycosidic bonds of laminarin to generate 1,3-beta-oligosaccharides of various lengths, the exo-1,3-beta-glucanase cleaves the longer-chain laminarioligosaccharides into short-chain disaccharides, laminaribiose and gentiobiose, and the 1,3-beta-glucosidase further hydrolyzes laminaribiose to glucose
fibrolytic enzyme which plays an important role in the hydrolysis of polysaccharide components. It hydrolyzes internal beta-1,3-glycosidic linkages in beta-1,3-glucans, which form the main component of the cell wall in yeasts and filamentous fungi and the major structural and storage polysaccharide in marine macroalgae such as Laminaria saccharina
the enzyme monomer consists of an N-terminal beta-sandwich domain, a C-terminal (alpha/alpha)6 domain and an additional domain between them. Glu553 and Glu557 are proposed to serve as the proton donor and basic catalyst, respectively, in a single-displacement mechanism. In addition, Tyr386, Tyr482 and Ser554 possibly contribute to both the position or the ionization state of the basic catalyst Glu557, catalytic cleft and the active site structure, overview
the enzyme monomer consists of an N-terminal beta-sandwich domain, a C-terminal (alpha/alpha)6 domain and an additional domain between them. Glu553 and Glu557 are proposed to serve as the proton donor and basic catalyst, respectively, in a single-displacement mechanism. In addition, Tyr386, Tyr482 and Ser554 possibly contribute to both the position or the ionization state of the basic catalyst Glu557, catalytic cleft and the active site structure, overview
the geometry of the active site cleft clearly precludes any (1,4)-beta-glucan topology at the subsites from -3 to +4 and could possibly accommodate beta-1,6-branching only at subsites +1 and +2. The glucose units at subsites -1 and -2 interact with highly conserved protein residues. In contrast, subsites -3, +3 and +4 are variable, suggesting that the mode of glucose binding at these sites may vary between different plant endo-1,3-beta-glucanases. Low substrate affinity is observed at subsites +1 and +2, as manifested by disorder of the glycosyl units there. Structure-function analysis, overview
the geometry of the active site cleft clearly precludes any (1,4)-beta-glucan topology at the subsites from -3 to +4 and could possibly accommodate beta-1,6-branching only at subsites +1 and +2. The glucose units at subsites -1 and -2 interact with highly conserved protein residues. In contrast, subsites -3, +3 and +4 are variable, suggesting that the mode of glucose binding at these sites may vary between different plant endo-1,3-beta-glucanases. Low substrate affinity is observed at subsites +1 and +2, as manifested by disorder of the glycosyl units there. Structure-function analysis, overview
residue Glu119 acts as a nucleophile in the endo-1,3-beta-glucanase reaction and has an effect on the balance between hydrolysis and transglycosylation
the enzyme monomer consists of an N-terminal beta-sandwich domain, a C-terminal (alpha/alpha)6 domain and an additional domain between them. Glu553 and Glu557 are proposed to serve as the proton donor and basic catalyst, respectively, in a single-displacement mechanism. In addition, Tyr386, Tyr482 and Ser554 possibly contribute to both the position or the ionization state of the basic catalyst Glu557, catalytic cleft and the active site structure, overview
residue Glu119 acts as a nucleophile in the endo-1,3-beta-glucanase reaction and has an effect on the balance between hydrolysis and transglycosylation