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evolution
the enzyme belongs to the CAZy glycosyltransferase family GT-62 that contains metal-dependent, retaining mannosyltransferases that are predicted to possess the GT-A fold and use GDP-Man as their donor substrate
evolution
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the enzyme belongs to the CAZy glycosyltransferase family GT-62 that contains metal-dependent, retaining mannosyltransferases that are predicted to possess the GT-A fold and use GDP-Man as their donor substrate
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malfunction
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the variant surface glycoprotein sVSG221 synthesized by the ALG12-/- parasites shows different glycosylation patterns to that synthesized by wild-type cells, changes in sVSG221 glycosylation induced by the deletion of the ALG12 gene, overview
malfunction
cells expressing catalytically inactive ScMnn9p show growth kinetics comparable with those measured for cells lacking the enzyme, phenotypes of inactive enzyme mutants, overview
malfunction
deletion of the mnn9 gene results in an increased sensitivity to calcofluor white, Congo red, or hygromycin B as well as in reduced cell wall components and abnormal polarity. Although there is no major effect on N-glycan synthesis, covalently-linked cell wall mannoprotein Mp1 is significantly reduced in the mutant
malfunction
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the deletion mutant DELTAVdOCH1 is impaired in certain characteristics such as fungal growth, conidia production, and microsclerotia formation. Also, DELTAVdOCH1 mutants are more sensitive to the cell wall perturbing reagents, such as SDS and Congo red, lose their penetration ability through cellophane membrane, and exhibit dramatically decreased pathogenicity to sunflower
malfunction
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cells expressing catalytically inactive ScMnn9p show growth kinetics comparable with those measured for cells lacking the enzyme, phenotypes of inactive enzyme mutants, overview
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malfunction
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deletion of the mnn9 gene results in an increased sensitivity to calcofluor white, Congo red, or hygromycin B as well as in reduced cell wall components and abnormal polarity. Although there is no major effect on N-glycan synthesis, covalently-linked cell wall mannoprotein Mp1 is significantly reduced in the mutant
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physiological function
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the TbALG12 gene encodes the alpha1-6-mannosyltransferase that converts Man7GlcNAc2-PP-Dol to Man8GlcNAc2-PP-Dol
physiological function
ScMnn9p catalytic activity is indispensable for mannoprotein synthesis in yeast. Yeast mannan biosynthesis is initiated by a Golgi-located complex (M-Pol I) of two GT-62 mannosyltransferases, Mnn9p and Van1p, that are conserved in fungal pathogens. Enzyme Mnn9 is both a priming glycosyltransferase and an allosteric activator of mannan biosynthesis, an allosteric activator for ScVan1 polymerase activity
physiological function
Mnn9 is required for mannan and mannoprotein biosynthesis. The enzyme is essential for cell wall integrity, morphogenesis, and proper localization of cell wall mannoprotein
physiological function
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the enzyme manipulates the biological characteristics, microsclerotia formation and pathogenic ability of Verticillium dahliae in sunflower
physiological function
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ScMnn9p catalytic activity is indispensable for mannoprotein synthesis in yeast. Yeast mannan biosynthesis is initiated by a Golgi-located complex (M-Pol I) of two GT-62 mannosyltransferases, Mnn9p and Van1p, that are conserved in fungal pathogens. Enzyme Mnn9 is both a priming glycosyltransferase and an allosteric activator of mannan biosynthesis, an allosteric activator for ScVan1 polymerase activity
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physiological function
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Mnn9 is required for mannan and mannoprotein biosynthesis. The enzyme is essential for cell wall integrity, morphogenesis, and proper localization of cell wall mannoprotein
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additional information
enzyme ScMnn9 possesses the GT-A fold and shows structural similarity to GT families 15 and 78. ScMnn9 possesses a unique extrusion that may act as a molecular ruler or multimerization domain
additional information
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enzyme ScMnn9 possesses the GT-A fold and shows structural similarity to GT families 15 and 78. ScMnn9 possesses a unique extrusion that may act as a molecular ruler or multimerization domain
additional information
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enzyme ScMnn9 possesses the GT-A fold and shows structural similarity to GT families 15 and 78. ScMnn9 possesses a unique extrusion that may act as a molecular ruler or multimerization domain
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