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evolution
PfDPMS is a membrane enzymes of the GT2 family. All known bona fide DPMSs use GDP-Man as donor substrate. Proposed model of substrate binding and product release
evolution
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PfDPMS is a membrane enzymes of the GT2 family. All known bona fide DPMSs use GDP-Man as donor substrate. Proposed model of substrate binding and product release
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evolution
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PfDPMS is a membrane enzymes of the GT2 family. All known bona fide DPMSs use GDP-Man as donor substrate. Proposed model of substrate binding and product release
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evolution
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PfDPMS is a membrane enzymes of the GT2 family. All known bona fide DPMSs use GDP-Man as donor substrate. Proposed model of substrate binding and product release
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malfunction
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loss-of-function mutations and RNA interference-mediated reduction of DPMS1 expression in Arabidopsis causes a wrinkled seed coat phenotype and most remarkably enhanced hypersensitivity to ammonium that is manifested by extensive chlorosis and a strong reduction of root growth
malfunction
failure to produce or utilize dolichyl mannosyl phosphate compromises organism viability
malfunction
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failure to produce or utilize dolichyl mannosyl phosphate compromises organism viability
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malfunction
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failure to produce or utilize dolichyl mannosyl phosphate compromises organism viability
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malfunction
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failure to produce or utilize dolichyl mannosyl phosphate compromises organism viability
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metabolism
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dolichyl phosphate mannose synthase is a key enzyme in the O-glycosylation pathway
metabolism
the enzyme is involved in dolichylphosphate mannose biosynthesis
metabolism
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the enzyme is involved in dolichylphosphate mannose biosynthesis
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metabolism
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the enzyme is involved in dolichylphosphate mannose biosynthesis
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metabolism
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the enzyme is involved in dolichylphosphate mannose biosynthesis
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physiological function
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high level of expression of (GlcNAc-beta-(1,4)-GlcNAc) 1-4-beta-GlcNAc-NeuAc glycans on the external surface of the capillary endothelial cells overexpressing DPMS. Increased cellular proliferation and accelerated healing of the wound induced by mechanical stress of the DPMS-overexpressing clone unequivocally supports a role of DPMS in angiogenesis
physiological function
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overexpression of DPMS accelerates angiogenesis, a higher rate of cellular proliferation in DPMS overexpressing cells compared to the pEGFP-N1 vector and the parental cells
physiological function
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elevated activity of overexpressed Saccharomyces cerevisiae dolichyl phosphate mannose synthase enhances biocontrol abilities of Trichoderma atroviride
physiological function
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overexpression of DPMS1 in Arabidopsis thaliana results in disorganized stem morphology and vascular bundle arrangements, wrinkled seed coat, and constitutive ER stress response
physiological function
subunits Dpm1 and Dpm3 function as host dependency factors for Dengue virus and other related flaviviruses such as Zika virus. Mutation in the DXD motif of Dpm1, which is essential for its catalytic activity, abolishes DPMS-mediated Dengue virus infection. Genetic ablation of mannosyltransferase ALG3 renders cells poorly susceptible to Dengue virus. In cells deficient for DPMS activity, viral RNA amplification is hampered and truncated oligosaccharides are transferred to the viral precursor of the M protein and E glycoproteins, affecting their proper folding
physiological function
transient depletion of the Dpm genes, the resulting morphant embryos show early death, muscle disorganization, low dolichol-phosphate mannose synthase complex activity, and increased levels of apoptotic nuclei, together with hypoglycosylated alpha-dystroglycan in muscle fibers
physiological function
the membrane protein dolichylphosphate mannose synthase (DPMS) catalyzes the reaction whereby mannose is transferred from GDP-mannose to the dolichol carrier dolichyl phosphate (Dol-P), to yield dolichyl mannosyl phosphate (Dol-P-Man). Lipid binding couples to movements of interface helices, metal binding, and acceptor loop dynamics to control critical events leading to Dol-P-Man synthesis
physiological function
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the membrane protein dolichylphosphate mannose synthase (DPMS) catalyzes the reaction whereby mannose is transferred from GDP-mannose to the dolichol carrier dolichyl phosphate (Dol-P), to yield dolichyl mannosyl phosphate (Dol-P-Man). Lipid binding couples to movements of interface helices, metal binding, and acceptor loop dynamics to control critical events leading to Dol-P-Man synthesis
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physiological function
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the membrane protein dolichylphosphate mannose synthase (DPMS) catalyzes the reaction whereby mannose is transferred from GDP-mannose to the dolichol carrier dolichyl phosphate (Dol-P), to yield dolichyl mannosyl phosphate (Dol-P-Man). Lipid binding couples to movements of interface helices, metal binding, and acceptor loop dynamics to control critical events leading to Dol-P-Man synthesis
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physiological function
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the membrane protein dolichylphosphate mannose synthase (DPMS) catalyzes the reaction whereby mannose is transferred from GDP-mannose to the dolichol carrier dolichyl phosphate (Dol-P), to yield dolichyl mannosyl phosphate (Dol-P-Man). Lipid binding couples to movements of interface helices, metal binding, and acceptor loop dynamics to control critical events leading to Dol-P-Man synthesis
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additional information
structure-function analysis, and structural comparison with related enzymes, detailed overview. The IF helices IFH1 and IFH2 are important for activity
additional information
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structure-function analysis, and structural comparison with related enzymes, detailed overview. The IF helices IFH1 and IFH2 are important for activity
additional information
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structure-function analysis, and structural comparison with related enzymes, detailed overview. The IF helices IFH1 and IFH2 are important for activity
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additional information
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structure-function analysis, and structural comparison with related enzymes, detailed overview. The IF helices IFH1 and IFH2 are important for activity
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additional information
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structure-function analysis, and structural comparison with related enzymes, detailed overview. The IF helices IFH1 and IFH2 are important for activity
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