2.4.1.83: dolichyl-phosphate beta-D-mannosyltransferase
This is an abbreviated version!
For detailed information about dolichyl-phosphate beta-D-mannosyltransferase, go to the full flat file.
Word Map on EC 2.4.1.83
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2.4.1.83
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n-linked
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n-glycosylation
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glycosylphosphatidylinositol
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lipid-linked
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reesei
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dolichol-phosphate-mannose
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asparagine-linked
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amphomycin
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dolichol-linked
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glc3man9glcnac2-pp-dol
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mannoproteins
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c-mannosylation
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medicine
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drug development
- 2.4.1.83
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n-linked
-
n-glycosylation
- glycosylphosphatidylinositol
-
lipid-linked
- reesei
-
dolichol-phosphate-mannose
-
asparagine-linked
- amphomycin
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dolichol-linked
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glc3man9glcnac2-pp-dol
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mannoproteins
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c-mannosylation
- medicine
- drug development
Reaction
Synonyms
AglD, bDPM1, D-P-M, Dol-P Man synthase, Dol-P-Man synthase, Dol-P-Man synthase1, Dol-P-Man-synthase, Dol-P-Mansynthase, Dol-PMan synthase, dolichol phosphate mannose synthase, dolichol phosphoryl mannose synthase, dolichol-P-mannose synthase, dolicholphosphate mannose synthase, dolichyl mannosyl phosphate synthase, dolichyl phosphate mannosyltransferase, dolichyl-phosphate mannose synthase, dolichyl-phosphate mannosyltransferase, dolichyl-phospho-mannose synthase, dolichylphosphate mannose synthase, DPM, DPM synthase, DPM1, DPMS, DPMS1, GDP-Man:DolP mannosyltransferase, GDP-mannose-dolichol phosphate mannosyltransferase, GDPMan:DolP mannosyltransferase, GDPmannose-dolichylmonophosphate mannosyltransferase, GDPmannose:dolichyl-phosphate mannosyltransferase, mannosylphospho dolichol synthase, mannosylphosphodolichol synthase, mannosylphosphoryldolichol synthase, mannosyltransferase, guanosine diphosphomannose-dolichol phosphate, MPD synthase, PF0058, Pfdpm1, PfDPMS, PH0051
ECTree
2.4.1.83 dolichyl-phosphate beta-D-mannosyltransferaseAdvanced search results
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results (Engineering
Engineering on EC 2.4.1.83 - dolichyl-phosphate beta-D-mannosyltransferase
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PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
G10E
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Lec15.1 cell have a single point mutation within the coding region of DPM2 gene. The mutant DPM2 cDNA is expresses a drastically reduced amount of DPM2 protein
I253N
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higher value for the apparent Km-value for dolichyl phosphate when assayed in detergent solution, mutation has no effect on Km-value when the enzyme is reconstituted with phosphatidylethanolamine
S141A
functionally active mutant enzyme with more than 50% reduction in catalytic activity compared to wild-type enzyme
additional information
additional information
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cloned Pfdpm1 gene fails to complement a Saccharomyces cerevisiae mutant indicating that the parasite gene does not belong to the bakers yeast group. Furthermore, Pfdpm1 is unable to complement a mouse mutant deficient in DPM but efficiently complements the Schizosaccharomyces pombe fission yeast mutant, indicating a difference between fission yeast and mammalian DPM genes
additional information
generation of a PfDPMS truncation variant DELTA230-352 which includes only the catalytic domain
additional information
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generation of a PfDPMS truncation variant DELTA230-352 which includes only the catalytic domain
additional information
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generation of a PfDPMS truncation variant DELTA230-352 which includes only the catalytic domain
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additional information
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generation of a PfDPMS truncation variant DELTA230-352 which includes only the catalytic domain
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additional information
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generation of a PfDPMS truncation variant DELTA230-352 which includes only the catalytic domain
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additional information
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mutant enzymes containing successive deletions or mutations of the hydrophobic region exhibit decreased transferase activity in vitro compared to the wild type enzyme, but the sequence is not essential for growth or for protein glycosylation. Although deletion of the entire hydrophobic region results in a soluble protein, mutant proteins containing 3 or 8 hydrophobic residues are still membrane-associated
additional information
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DPM synthase mutants have an aberrant cell wall composition and ultrastructure. Mutant is oversensitive to Calcofluor white, an agent interacting with the cell wall chitin. Chemical analysis of the cell wall alkali-insoluble fraction indicates an increased amount of chitin and changes in the quantity of beta1,6- and beta1,3-glucan in dpm1-6 mutants. Cell wall defect is suppressed by an increased dolichol availability caused by the RER2 (cis-prenyl transferase-encoding) gene overexpression and subsequent upregulation of DolPPGlcNAc2 synthesis. This is concomitant with an increase in glycosylation and stability of the plasma membrane protein Gas1 and rearrangement of the cell wall components
additional information
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DPM synthase mutants have an aberrant cell wall composition and ultrastructure. Mutant is oversensitive to Calcofluor white, an agent interacting with the cell wall chitin. Chemical analysis of the cell wall alkali-insoluble fraction indicates an increased amount of chitin and changes in the quantity of beta1,6- and beta1,3-glucan in dpm1-6 mutants. Cell wall defect is suppressed by an increased dolichol availability caused by the RER2 (cis-prenyl transferase-encoding) gene overexpression and subsequent upregulation of DolPPGlcNAc2 synthesis. This is concomitant with an increase in glycosylation and stability of the plasma membrane protein Gas1 and rearrangement of the cell wall components
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