2.4.1.109	dolichyl beta-D-mannosyl phosphate + L-seryl-[protein]	-	
2.4.1.109	dolichyl beta-D-mannosyl phosphate + L-threonyl-[protein]	-	
2.4.1.109	dolichyl phosphate D-mannose + alpha-dystroglycan	in vitro asssay with both enzyme isoforms (RT and TW), 20 mM Tris, pH 8.0, mercaptoethanol, EDTA, n-octyl-beta-D-thioglucoside, sugar donor is tritium-labeled, alpha-dystroglycan isoform C contains mucin-type domain that is target of O-mannose modifications in mammals, high grade of O-mannosylation, A isoform without noticeable O-mannosylation, rabbit alpha-dystroglycan as positive control shows lower O-mannosylation	
2.4.1.109	dolichyl phosphate D-mannose + glucoamylase I	the AaPmtA protein is involved in the formation of the normal cell wall. AaPmtA protein is responsible for the transfer of mannose to glucoamylase I	
2.4.1.109	dolichyl phosphate D-mannose + protein	-	
2.4.1.109	dolichyl phosphate D-mannose + protein	acceptor substrate specificities of PMT1-4,6	
2.4.1.109	dolichyl phosphate D-mannose + protein	acceptor substrates: secretory proteins	
2.4.1.109	dolichyl phosphate D-mannose + protein	production of cell-wall mannoproteins	
2.4.1.109	dolichyl phosphate D-mannose + protein	catalyzes the initial step of O-mannosyl glycan biosynthesis	
2.4.1.109	dolichyl phosphate D-mannose + protein	central role for Pmt4-mediated protein O-mannosylation in growth, cell wall integrity, and virulence of Cryptococcus neoformans	
2.4.1.109	dolichyl phosphate D-mannose + protein	O-glycosylation initiated by Ogm proteins plays crucial physiological roles and can serve as a sorting determinant for protein transport of membrane glycoproteins. None of the ogm genes is found to be essential	
2.4.1.109	dolichyl phosphate D-mannose + protein	O-glycosylation initiated by Ogm proteins plays crucial physiological roles and can serve as a sorting determinant for protein transport of membrane glycoproteins. None of the ogm genes is found to be essential. ogm4D mutants differ morphologically from wild type and exhibit defects in sexual agglutination	
2.4.1.109	dolichyl phosphate D-mannose + protein	O-glycosylation initiated by Ogm proteins plays crucial physiological roles and can serve as a sorting determinant for protein transport of membrane glycoproteins. While none of the ogm genes is found to be essential, ogm1D mutants differ morphologically from wildtype and exhibit defects in sexual agglutination. O-glycosylation of chitinase from Saccharomyces cerevisiae is decreased in ogm1D cells	
2.4.1.109	dolichyl phosphate D-mannose + protein	protein O-mannosylation is crucial for cell wall integrity, septation and viability	
2.4.1.109	dolichyl phosphate D-mannose + protein	role of O-glycosylation in the control of folding of secretory proteins in the endoplasmic reticulum	
2.4.1.109	dolichyl phosphate D-mannose + protein Aga2	i.e. small-agglutinin	
2.4.1.109	dolichyl phosphate D-mannose + protein Aga2	activity is not affected by disruption mutations of PMT1-4	
2.4.1.109	dolichyl phosphate D-mannose + protein Aga2	protein is located at the cell surface	
2.4.1.109	dolichyl phosphate D-mannose + protein AN5660	the un-glycosylated 32 kDa protein is an ortholog of Wsc family proteins in Saccharomyces cerevisiae, these proteins serve as sensors of stress, such as high temperature and cell wall-perturbing chemicals	
2.4.1.109	dolichyl phosphate D-mannose + protein Bar1	PMT1 and PMT2, not PMT3 and PMT4	
2.4.1.109	dolichyl phosphate D-mannose + protein Bar1	protein is located in the medium	
2.4.1.109	dolichyl phosphate D-mannose + protein chitinase 1	PMT1	
2.4.1.109	dolichyl phosphate D-mannose + protein chitinase 1	PMT1, PMT4, PMT6 and especially PMT2, not PMT3	
2.4.1.109	dolichyl phosphate D-mannose + protein chitinase 1	protein is located in the cell wall and medium	
2.4.1.109	dolichyl phosphate D-mannose + protein Ggp1/Gas1	PMT4 and PMT6, not PMT1-3	
2.4.1.109	dolichyl phosphate D-mannose + protein Ggp1/Gas1	protein is located at the cell surface	
2.4.1.109	dolichyl phosphate D-mannose + protein Kex2	PMT4, not PMT1-3	
2.4.1.109	dolichyl phosphate D-mannose + protein Kex2	protein is located in the Golgi apparatus	
2.4.1.109	dolichyl phosphate D-mannose + protein Kre9	mainly PMT1 and PMT2, not PMT3 and PMT4	
2.4.1.109	dolichyl phosphate D-mannose + protein Kre9	protein is located in the Golgi apparatus	
2.4.1.109	dolichyl phosphate D-mannose + protein Pir2/hsp150	PMT1	
2.4.1.109	dolichyl phosphate D-mannose + protein Pir2/hsp150	PMT1, PMT2, and to some extent PMT4, not PMT3	
2.4.1.109	dolichyl phosphate D-mannose + protein Pir2/hsp150	protein is located in the medium	
2.4.1.109	dolichyl phosphate D-mannose + ribonuclease 2	C-mannosylation activity	
2.4.1.109	dolichyl phosphate D-mannose + ribonuclease 2	biosynthetic pathway	
2.4.1.109	additional information	defective mutants are used to investigate the substrate specificities of PMT1-4,6 in vivo	
2.4.1.109	additional information	PMT2 is essential for growth	
2.4.1.109	additional information	PMT4 is required for full virulence of Candida albicans	
2.4.1.109	additional information	PMT5 does not make a significant contribution to virulence	
2.4.1.109	additional information	protein mannosyltransferases (Pmt proteins Pmt1p, Pmt2p, Pmt4p, Pmt5p, and Pmt6p) initiate O mannosylation of secretory proteins. Virulence of the fungal pathogen Candida albicans requires the five isoforms of protein mannosyltransferases. The importance of individual Pmt isoforms may differ in specific host niches	
2.4.1.109	additional information	protein O-mannosyltransferase isoforms regulate biofilm formation in Candida albicans	
2.4.1.109	additional information	Afpmt1 acts as an O-mannosyltransferase. Characterization of the DELTAAfpmt1 mutant shows that a lack of AfPmt1p results in sensitivity to elevated temperature and defects in growth and cell wall integrity, thereby affecting cell morphology, conidium formation, and germination. In a mouse model, Afpmt1 is not required for the virulence of Aspergillus fumigatus	
2.4.1.109	additional information	although the improved secretion of the protein by suppression of O mannosylation might not be a general phenomenon, the suppression of O mannosylation could be beneficial for the production of proteins forming either homomeric or heteromeric complexes through their hydrophobic interaction in yeast	
2.4.1.109	additional information	disruption of the pmt1 gene decreased protein secretion but has no effect on glycosylation of secreted proteins. PMTI protein O-mannosyltranferase does not take part in glycosylation of these proteins	
2.4.1.109	additional information	O-mannosylation of specific secretory proteins of the bacterial pathogen Mycobacterium tuberculosis contributes significantly to virulence	
2.4.1.109	additional information	O-mannosylation of specific secretory proteins of the human fungal pathogen Candida albicans contributes significantly to virulence	
2.4.1.109	additional information	O-mannosylation of specific secretory proteins of the human fungal pathogen Candida albicans contributes significantly to virulence. PMT2 is essential for growth. Loss of a single PMT2 allele already sufficed to significantly retarded growth