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Information on EC 2.4.1.83 - dolichyl-phosphate beta-D-mannosyltransferase and Organism(s) Saccharomyces cerevisiae and UniProt Accession P14020
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2.4.1.83 dolichyl-phosphate beta-D-mannosyltransferaseIUBMB Comments
Acts only on long-chain polyprenyl phosphates and alpha-dihydropolyprenyl phosphates that are larger than C35.
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Word Map
- 2.4.1.83
-
n-linked
-
n-glycosylation
- glycosylphosphatidylinositol
-
lipid-linked
- reesei
-
dolichol-phosphate-mannose
-
asparagine-linked
- amphomycin
-
dolichol-linked
-
glc3man9glcnac2-pp-dol
-
mannoproteins
-
c-mannosylation
- medicine
- drug development
The taxonomic range for the selected organisms is: Saccharomyces cerevisiae
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
Synonyms
dol-p-man synthase, dpm synthase, dolichol phosphate mannose synthase, mannosylphosphoryldolichol synthase, mpd synthase, d-p-m, dolichyl-phosphate mannosyltransferase, mannosylphospho dolichol synthase, dolichylphosphate mannose synthase, mannosylphosphodolichol synthase, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
Dol-P-Man-synthase
-
-
-
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Dol-P-Mansynthase
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-
-
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dolichol phosphate mannose synthase
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-
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dolichyl mannosyl phosphate synthase
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-
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dolichyl phosphate mannosyltransferase
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-
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dolichyl-phosphate mannose synthase
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-
-
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dolichyl-phospho-mannose synthase
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-
-
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DPMS
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-
-
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GDP-Man:DolP mannosyltransferase
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-
-
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GDP-mannose-dolichol phosphate mannosyltransferase
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-
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GDPMan:DolP mannosyltransferase
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-
-
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GDPmannose-dolichylmonophosphate mannosyltransferase
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GDPmannose:dolichyl-phosphate mannosyltransferase
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mannosylphosphodolichol synthase
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-
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mannosylphosphoryldolichol synthase
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-
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mannosyltransferase, guanosine diphosphomannose-dolichol phosphate
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-
-
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MPD synthase
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-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hexosyl group transfer
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-
-
-
PATHWAY SOURCE
PATHWAYS
-
-, -, -, -, -
SYSTEMATIC NAME
IUBMB Comments
GDP-mannose:dolichyl-phosphate beta-D-mannosyltransferase
Acts only on long-chain polyprenyl phosphates and alpha-dihydropolyprenyl phosphates that are larger than C35.
CAS REGISTRY NUMBER
COMMENTARY
62213-44-9
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
GDP-mannose + dolichyl phosphate
GDP + dolichyl D-mannosyl phosphate
-
-
-
?
(6Z,10E,14E,18E,22E)-3,7,15,19,23,27-hexamethyl-11-[(naphthalen-1-ylamino)methyl]octacosa-6,10,14,18,22,26-hexaen-1-yl dihydrogen phosphate + dolichyl phosphate
?
-
-
-
-
?
(6Z,10Z,14Z,18Z,22E,26E)-3,7,11,15,19,23,27-heptamethyl-30-(naphthalen-1-ylamino)triaconta-6,10,14,18,22,26-hexaen-1-yl dihydrogen phosphate + dolichyl phosphate
?
-
-
-
-
?
(6Z,10Z,14Z,18Z,22Z,26Z,30E,34E,38E)-3,7,11,15,19,23,27,31,35,39-decamethyl-42-(naphthalen-1-ylamino)dotetraconta-6,10,14,18,22,26,30,34,38-nonaen-1-yl dihydrogen phosphate + dolichyl phosphate
?
-
-
-
-
?
GDPmannose + (S)-3-methyloctadecanyl phosphate
GDP + (S)-3-methyloctadecanyl D-mannosyl phosphate
-
-
-
-
?
GDPmannose + C100 alpha-dihydropolyprenyl phosphate
GDP + C100 alpha-dihydropolyprenyl D-mannosyl phosphate
-
-
-
-
?
GDPmannose + C55 alpha-dihydropolyprenyl phosphate
GDP + C55 alpha-dihydropolyprenyl D-mannosyl phosphate
-
-
-
-
?
GDPmannose + C80 alpha-dihydropolyprenyl phosphate
GDP + C80 alpha-dihydropolyprenyl D-mannosyl phosphate
-
-
-
-
?
GDPmannose + phytanyl phosphate
GDP + phytanyl D-mannosyl phosphate
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at 60-70% of the activity with dolichyl phosphate
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-
?
GDP-mannose + dolichyl phosphate
GDP + dolichyl D-mannosyl phosphate
-
-
-
-
?
GDP-mannose + dolichyl phosphate
GDP + dolichyl D-mannosyl phosphate
-
the enzyme transfers mannose from the water soluble cytoplasmic donor GDP-Man, to the membrane bound, extremely hydrophobic, and long-chain polyisoprenoid acceptor, dolichyl-phosphate
-
-
?
GDP-mannose + dolichyl phosphate
GDP + dolichyl D-mannosyl phosphate
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or synthetic analogs of dolichyl phosphate
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-
?
GDPmannose + dolichyl phosphate
GDP + dolichyl D-mannosyl phosphate
-
-
-
?
GDPmannose + dolichyl phosphate
GDP + dolichyl D-mannosyl phosphate
-
-
-
?
GDPmannose + dolichyl phosphate
GDP + dolichyl D-mannosyl phosphate
-
-
-
?
GDPmannose + dolichyl phosphate
GDP + dolichyl D-mannosyl phosphate
-
-
-
?
GDPmannose + dolichyl phosphate
GDP + dolichyl D-mannosyl phosphate
-
-
-
?
GDPmannose + dolichyl phosphate
GDP + dolichyl D-mannosyl phosphate
-
-
-
?
GDPmannose + dolichyl phosphate
GDP + dolichyl D-mannosyl phosphate
-
-
-
?
GDPmannose + dolichyl phosphate
GDP + dolichyl D-mannosyl phosphate
-
-
-
?
GDPmannose + dolichyl phosphate
GDP + dolichyl D-mannosyl phosphate
-
-
-
?
GDPmannose + dolichyl phosphate
GDP + dolichyl D-mannosyl phosphate
-
the enzyme is involved in glycoconjugate biosynthesis
-
-
?
GDPmannose + dolichyl phosphate
GDP + dolichyl D-mannosyl phosphate
-
synthesis of dolichol-phosphate mannose, a key mannosyl donor for the biosynthesis of N-linked oligosaccharides as well as for O-linked oligosaccharides on yeast glycoproteins
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-
?
additional information
?
-
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activities of fluorescent labeled dolichyl-phosphate derivatives
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-
?
additional information
?
-
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branching of lipid phosphates is essential for substrates of the enzyme, transfer of mannose occurs even if only branching at C3 is present
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-
?
additional information
?
-
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increased availability of GDP-mannose corrects glycosylation defects in the endoplasmic reticulum, such as dolichyl D-mannosyl phosphate formation in dolichyl-phosphate beta-D-mannosyltransferase mutants of Saccharomyces cerevisiae
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-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
GDP-mannose + dolichyl phosphate
GDP + dolichyl D-mannosyl phosphate
-
the enzyme transfers mannose from the water soluble cytoplasmic donor GDP-Man, to the membrane bound, extremely hydrophobic, and long-chain polyisoprenoid acceptor, dolichyl-phosphate
-
-
?
additional information
?
-
-
increased availability of GDP-mannose corrects glycosylation defects in the endoplasmic reticulum, such as dolichyl D-mannosyl phosphate formation in dolichyl-phosphate beta-D-mannosyltransferase mutants of Saccharomyces cerevisiae
-
-
?
GDPmannose + dolichyl phosphate
GDP + dolichyl D-mannosyl phosphate
-
the enzyme is involved in glycoconjugate biosynthesis
-
-
?
GDPmannose + dolichyl phosphate
GDP + dolichyl D-mannosyl phosphate
-
synthesis of dolichol-phosphate mannose, a key mannosyl donor for the biosynthesis of N-linked oligosaccharides as well as for O-linked oligosaccharides on yeast glycoproteins
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mg2+
-
Mg2+ and Mn2+ up to a concentration of 5 mM result in the same activation
Mn2+
-
Mg2+ and Mn2+ up to a concentration of 5 mM result in the same activation
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
GDP, GTP, IDP or GMP provide protection against inactivation by thiol reagents
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0751
(6Z,10E,14E,18E,22E)-3,7,15,19,23,27-hexamethyl-11-[(naphthalen-1-ylamino)methyl]octacosa-6,10,14,18,22,26-hexaen-1-yl dihydrogen phosphate
-
pH 7.5
0.0246
(6Z,10Z,14Z,18Z,22E,26E)-3,7,11,15,19,23,27-heptamethyl-30-(naphthalen-1-ylamino)triaconta-6,10,14,18,22,26-hexaen-1-yl dihydrogen phosphate
-
pH 7.5
0.0248
(6Z,10Z,14Z,18Z,22Z,26Z,30E,34E,38E)-3,7,11,15,19,23,27,31,35,39-decamethyl-42-(naphthalen-1-ylamino)dotetraconta-6,10,14,18,22,26,30,34,38-nonaen-1-yl dihydrogen phosphate
-
pH 7.5
0.0025
dolichyl phosphate
-
wild-type enzyme reconstituted with phosphatidylethanolamine
0.0027
dolichyl phosphate
-
wild-type enzyme reconstituted with phosphatidylethanolamine
0.0106
dolichyl phosphate
-
wild-type enzyme assayed in solution of Nonidet P-40
0.0015
GDPmannose
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wild-type enzyme assayed in solution of Nonidet P-40
additional information
additional information
the KM-values for dolichyl phosphate do not differ between the invitro phosphorylated and the control enzyme
-
additional information
additional information
-
the KM-values for dolichyl phosphate do not differ between the invitro phosphorylated and the control enzyme
-
additional information
additional information
-
KM-values for synthetic dolichyl phosphate analogs
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
enzyme is closely associated with membranes of the endoplasmic reticulum
-
enzyme is anchored with both its N-termini and C-termini in the membrane, while the main part of the protein is oriented towards the lumen of the endoplasmic reticulum
-
enzyme is closely associated with membranes of the endoplasmic reticulum
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
metabolism
-
dolichyl phosphate mannose synthase is a key enzyme in the O-glycosylation pathway
physiological function
-
elevated activity of overexpressed Saccharomyces cerevisiae dolichyl phosphate mannose synthase enhances biocontrol abilities of Trichoderma atroviride
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
phosphoprotein
in vitro phosphorylation by cAMP-dependent protein kinase up-regulates recombinant Saccharomyces cerevisiae mannosylphosphodolichol synthase
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
S141A
functionally active mutant enzyme with more than 50% reduction in catalytic activity compared to wild-type enzyme
I253N
-
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
additional information
additional information
-
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
-
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
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
functionally active mutant enzyme S141A is expressed in Escherichia coli
gene can complement a lethal null mutation in Schizosaccharomyces pombe
-
glycoprotein hypersecretion alters the cell wall in Trichoderma reesei strains expressing the Saccharomyces cerevisiae dolichylphosphate mannose synthase gene
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Babczinski, P.; Haselbeck, A.; Tanner, W.
Yeast mannosyl transferases requiring dolichyl phosphate and dolichyl phosphate mannose as substrate. Partial purification and characterization of the solubilized enzyme
Eur. J. Biochem.
105
509-515
1980
Saccharomyces cerevisiae
Palamarczyk, G.; Lehle, L.; Mankowski, T.; Chojnacki, T.; Tanner, W.
Specificity of solubilized yeast glycosyl transferases for polyprenyl derivatives
Eur. J. Biochem.
105
517-523
1980
Saccharomyces cerevisiae
Haselbeck, A.
Purification of GDP mannose:dolichyl-phosphate O-beta-D-mannosyltransferase from Saccharomyces cerevisiae
Eur. J. Biochem.
181
663-668
1989
Saccharomyces cerevisiae
Wilson, I.B.H.; Taylor, J.P.; Webberley, M.C.; Turner, N.J.; Flitsch, S.L.
A novel mono-branched lipid phosphate acts as a substrate for dolichyl phosphate mannose synthetase
Biochem. J.
295
195-201
1993
Saccharomyces cerevisiae
-
Schutzbach, J.S.; Zimmerman, J.W.; Forsee, W.T.
The purification and characterization of recombinant yeast dolichyl-phosphate-mannose synthase. Site-directed mutagenesis of the putative dolichol recognition sequence
J. Biol. Chem.
268
24190-24196
1993
Saccharomyces cerevisiae
Colussi, P.A.; Taron, C.H.; Mack, J.C.; Orlean, P.
Human and Saccharomyces cerevisiae dolichol phosphate mannose synthases represent two classes of the enzyme, but both function in Schizosaccharomyces pombe
Proc. Natl. Acad. Sci. USA
94
7873-7878
1997
Homo sapiens (O60762), Homo sapiens, Saccharomyces cerevisiae
Xing, J.; Forsee, W.T.; Lamani, E.; Maltsev, S.D.; Danilov, L.L.; Shibaev, V.N.; Schutzbach, J.S.; Cheung, H.C.; Jedrzejas, M.J.
Investigations of the active site of Saccharomyces cerevisiae dolichyl-phosphate-mannose synthase using fluorescent labeled dolichyl-phosphate derivatives
Biochemistry
39
7886-7894
2000
Saccharomyces cerevisiae
Zimmerman, J.W.; Robbins, P.W.
The hydrophobic domain of dolichyl-phosphate-mannose synthase is not essential for enzyme activity or growth in Saccharomyces cerevisiae
J. Biol. Chem.
268
16746-16753
1993
Saccharomyces cerevisiae
Forsee, W.T.; McPherson, D.; Schutzbach, J.S.
Characterization of recombinant yeast dolichyl mannosyl phosphate synthase and site-directed mutagenesis of its cysteine residues
Eur. J. Biochem.
244
953-958
1997
Saccharomyces cerevisiae
Janik, A.; Sosnowska, M.; Kruszewska, J.; Krotkiewski, H.; Lehle, L.; Palamarczyk, G.
Overexpression of GDP-mannose pyrophosphorylase in Saccharomyces cerevisiae corrects defects in dolichol-linked saccharide formation and protein glycosylation
Biochim. Biophys. Acta
1621
22-30
2003
Saccharomyces cerevisiae
Banerjee, D.K.; Carrasquillo, E.A.; Hughey, P.; Schutzbach, J.S.; Martinez, J.A.; Baksi, K.
In vitro phosphorylation by cAMP-dependent protein kinase up-regulates recombinant Saccharomyces cerevisiae mannosylphosphodolichol synthase
J. Biol. Chem.
280
4174-4181
2005
Saccharomyces cerevisiae (P14020), Saccharomyces cerevisiae
Orlowski, J.; Machula, K.; Janik, A.; Zdebska, E.; Palamarczyk, G.
Dissecting the role of dolichol in cell wall assembly in the yeast mutants impaired in early glycosylation reactions
Yeast
24
239-252
2007
Saccharomyces cerevisiae
Perlinska-Lenart, U.; Orlowski, J.; Laudy, A.E.; Zdebska, E.; Palamarczyk, G.; Kruszewska, J.S.
Glycoprotein hypersecretion alters the cell wall in Trichoderma reesei strains expressing the Saccharomyces cerevisiae dolichylphosphate mannose synthase gene
Appl. Environ. Microbiol.
72
7778-7784
2006
Saccharomyces cerevisiae
Lamani, E.; Mewbourne, R.B.; Fletcher, D.S.; Maltsev, S.D.; Danilov, L.L.; Veselovsky, V.V.; Lozanova, A.V.; Grigorieva, N.Y.; Pinsker, O.A.; Xing, J.; Forsee, W.T.; Cheung, H.C.; Schutzbach, J.S.; Shibaev, V.N.; Jedrzejas, M.J.
Structural studies and mechanism of Saccharomyces cerevisiae dolichyl-phosphate-mannose synthase: insights into the initial step of synthesis of dolichyl-phosphate-linked oligosaccharide chains in membranes of endoplasmic reticulum
Glycobiology
16
666-678
2006
Saccharomyces cerevisiae
Zembek, P.; Perlinska-Lenart, U.; Brunner, K.; Reithner, B.; Palamarczyk, G.; Mach, R.L.; Kruszewska, J.S.
Elevated activity of dolichyl phosphate mannose synthase enhances biocontrol abilities of Trichoderma atroviride
Mol. Plant Microbe Interact.
24
1522-1529
2011
Saccharomyces cerevisiae
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