1,3-β-Glucanase
1,3-β-Glucanase structure
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Common Name | 1,3-β-Glucanase | ||
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| CAS Number | 9044-93-3 | Molecular Weight | 282.294 | |
| Density | 1.3±0.1 g/cm3 | Boiling Point | 475.5±55.0 °C at 760 mmHg | |
| Molecular Formula | C16H14N2O3 | Melting Point | N/A | |
| MSDS | USA | Flash Point | 241.4±31.5 °C | |
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Contribution of the gas1 gene of the entomopathogenic fungus Beauveria bassiana, encoding a putative glycosylphosphatidylinositol-anchored beta-1,3-glucanosyltransferase, to conidial thermotolerance and virulence.
Appl. Environ. Microbiol. 77(8) , 2676-84, (2011) Beauveria bassiana is a mycoinsecticide alternative to chemicals for use in biological pest control. The fungus-insect interaction is also an emerging model system to examine unique aspects of the development, pathogenesis, and diversity of fungal lifestyles.... |
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Cofilin-mediated sorting and export of specific cargo from the Golgi apparatus in yeast.
Mol. Biol. Cell 23(12) , 2327-38, (2012) The mechanism of cargo sorting at the trans-Golgi network (TGN) for secretion is poorly understood. We previously reported the involvement of the actin-severing protein cofilin and the Ca(2+) ATPase secretory pathway calcium ATPase 1 (SPCA1) in the sorting of... |
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Mitotic exit and separation of mother and daughter cells.
Genetics 192(4) , 1165-202, (2012) Productive cell proliferation involves efficient and accurate splitting of the dividing cell into two separate entities. This orderly process reflects coordination of diverse cytological events by regulatory systems that drive the cell from mitosis into G1. I... |
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Activation of the yeast cell wall integrity MAPK pathway by zymolyase depends on protease and glucanase activities and requires the mucin-like protein Hkr1 but not Msb2
FEBS Lett. 587(22) , 3675-80, (2013) • The main cell-wall digesting enzymes of zymolyase were individually inhibited. • β-1,3-Glucanase and protease activities are required for CWI MAPK pathway activation. • Hkr1 mucin is essential for signaling cell-wall damage caused by zymolyase in yeast. |
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Surface stress induces a conserved cell wall stress response in the pathogenic fungus Candida albicans.
Eukaryotic Cell 12(2) , 254-64, (2013) The human fungal pathogen Candida albicans can grow at temperatures of up to 45°C. Here, we show that at 42°C substantially less biomass was formed than at 37°C. The cells also became more sensitive to wall-perturbing compounds, and the wall chitin levels inc... |
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Beta-D-1, 3 Glucanases in fungi.
Can. J. Microbiol. 5(2) , 173-85, (1959)
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A rice β-1,3-glucanase gene Osg1 is required for callose degradation in pollen development.
Planta 233(2) , 309-23, (2011) Plant β-1,3-glucanases are involved in plant defense and development. In rice (Oryza sativa), 14 genes encoding putative β-1,3-glucanases have been isolated and sequenced. However, only limited information is available on the function of these β-1,3-glucanase... |
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The RabGAP proteins Gyp5p and Gyl1p recruit the BAR domain protein Rvs167p for polarized exocytosis.
Traffic 12(8) , 1084-97, (2011) The Rab GTPase-activating proteins (GAP) Gyp5p and Gyl1p are involved in the control of polarized exocytosis at the small-bud stage in Saccharomyces cerevisiae. Both Gyp5p and Gyl1p interact with the N-Bin1/Amphiphysin/Rvs167 (BAR) domain protein Rvs167p, but... |
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The structure of a glycoside hydrolase family 81 endo-β-1,3-glucanase.
Acta Crystallogr. D Biol. Crystallogr. 69(Pt 10) , 2027-38, (2013) Endo-β-1,3-glucanases catalyze the hydrolysis of β-1,3-glycosidic linkages in glucans. They are also responsible for rather diverse physiological functions such as carbon utilization, cell-wall organization and pathogen defence. Glycoside hydrolase (GH) famil... |
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Presence of a large β(1-3)glucan linked to chitin at the Saccharomyces cerevisiae mother-bud neck suggests involvement in localized growth control.
Eukaryotic Cell 11(4) , 388-400, (2012) Previous results suggested that the chitin ring present at the yeast mother-bud neck, which is linked specifically to the nonreducing ends of β(1-3)glucan, may help to suppress cell wall growth at the neck by competing with β(1-6)glucan and thereby with manno... |