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Information on EC 2.4.1.117 - dolichyl-phosphate beta-glucosyltransferase for references in articles please use BRENDA:EC2.4.1.117
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EC Tree
IUBMB Comments Solanesyl phosphate and ficaprenyl phosphate can act as acceptors, but more slowly.
The enzyme appears in viruses and cellular organisms
Synonyms
glucosyltransferase, uridine diphosphoglucose-dolichol, polyprenyl phosphate:UDP-D-glucose glucosyltransferase, UDP-glucose dolichyl-phosphate glucosyltransferase, UDP-glucose:dolichol phosphate glucosyltransferase, UDP-glucose:dolicholphosphoryl glucosyltransferase, UDP-glucose:dolichyl monophosphate glucosyltransferase, UDP-glucose:dolichyl phosphate glucosyltransferase, UDP-glucose:dolichyl-phosphate glucosyltransferase, UDP-glucose:dolichylphosphate glucosyltransferase, wollknäuel,
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glucosyltransferase, uridine diphosphoglucose-dolichol
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polyprenyl phosphate:UDP-D-glucose glucosyltransferase
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UDP-glucose dolichyl-phosphate glucosyltransferase
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UDP-glucose:dolichol phosphate glucosyltransferase
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UDP-glucose:dolicholphosphoryl glucosyltransferase
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UDP-glucose:dolichyl monophosphate glucosyltransferase
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UDP-glucose:dolichyl phosphate glucosyltransferase
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UDP-glucose:dolichyl-phosphate glucosyltransferase
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UDP-glucose:dolichylphosphate glucosyltransferase
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UDP-alpha-D-glucose + dolichyl phosphate = UDP + dolichyl beta-D-glucosyl phosphate
UDP-alpha-D-glucose + dolichyl phosphate = UDP + dolichyl beta-D-glucosyl phosphate
sequential mechanism
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UDP-alpha-D-glucose + dolichyl phosphate = UDP + dolichyl beta-D-glucosyl phosphate
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hexosyl group transfer
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UDP-glucose:dolichyl-phosphate beta-D-glucosyltransferase
Solanesyl phosphate and ficaprenyl phosphate can act as acceptors, but more slowly.
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UDP-glucose + dolichyl phosphate
UDP + dolichyl beta-D-glucosyl phosphate
UDP-glucose + ficaprenyl phosphate
UDP + ficaprenyl beta-D-glucosyl phosphate
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r
UDP-glucose + solanesyl phosphate
UDP + solanesyl beta-D-glucosyl phosphate
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r
additional information
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UDP-glucose + dolichyl phosphate
UDP + dolichyl beta-D-glucosyl phosphate
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r
UDP-glucose + dolichyl phosphate
UDP + dolichyl beta-D-glucosyl phosphate
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UDP-glucose + dolichyl phosphate
UDP + dolichyl beta-D-glucosyl phosphate
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UDP-glucose + dolichyl phosphate
UDP + dolichyl beta-D-glucosyl phosphate
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r
UDP-glucose + dolichyl phosphate
UDP + dolichyl beta-D-glucosyl phosphate
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UDP-glucose + dolichyl phosphate
UDP + dolichyl beta-D-glucosyl phosphate
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UDP-glucose + dolichyl phosphate
UDP + dolichyl beta-D-glucosyl phosphate
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UDP-glucose + dolichyl phosphate
UDP + dolichyl beta-D-glucosyl phosphate
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UDP-glucose + dolichyl phosphate
UDP + dolichyl beta-D-glucosyl phosphate
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UDP-glucose + dolichyl phosphate
UDP + dolichyl beta-D-glucosyl phosphate
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additional information
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no substrate: GDP-D-glucose, UDP-D-glucuronic acid, UDP-N-acetyl-D-glucosamine, UDP-D-xylose
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additional information
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synthesis of dolichyl D-glucosyl phosphate, a glucosyl donor in the formation of lipid-linked core oligosaccharides
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additional information
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mutations in wollknäuel, a UDPglucose:dolichyl-phosphate glucosyltransferase involved in N-linked protein glycosylation, disrupts Drosophila embryo development by affecting the expression of a few key gene regulators. Reduced glycosylation efficiency in wol mutant embryos triggers the unfolded protein response. As a result, phosphorylation of eIF2a is increased
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additional information
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enzyme is involved in the biosynthesis of the lipid-linked oligosaccharides that are precursors of N-linked glycoproteins
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UDP-glucose + dolichyl phosphate
UDP + dolichyl beta-D-glucosyl phosphate
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r
additional information
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additional information
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synthesis of dolichyl D-glucosyl phosphate, a glucosyl donor in the formation of lipid-linked core oligosaccharides
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additional information
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mutations in wollknäuel, a UDPglucose:dolichyl-phosphate glucosyltransferase involved in N-linked protein glycosylation, disrupts Drosophila embryo development by affecting the expression of a few key gene regulators. Reduced glycosylation efficiency in wol mutant embryos triggers the unfolded protein response. As a result, phosphorylation of eIF2a is increased
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additional information
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enzyme is involved in the biosynthesis of the lipid-linked oligosaccharides that are precursors of N-linked glycoproteins
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Zn2+
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divalent cation required, efficiency of activiation in descending order: Mg2+, Mn2+, Ca2+, Co2+, Zn2+
Ca2+
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no stimulation
Ca2+
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divalent cation required, maximum stimulation in presence of Ca2+. Co2+, Mg2+ or Mn2+ can replace Ca2+
Ca2+
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CaCl2 cannot replace MgCl2 or MnCl2
Ca2+
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divalent cation required, efficiency of activiation in descending order: Mg2+, Mn2+, Ca2+, Co2+, Zn2+
Co2+
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divalent cation required, maximum stimulation in presence of Ca2+. Co2+, Mg2+ or Mn2+ can replace Ca2+
Co2+
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divalent cation required, efficiency of activiation in descending order: Mg2+, Mn2+, Ca2+, Co2+, Zn2+
Mg2+
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divalent cation required, either Mg2+ or Mn2+, Mn2+ stimulates the enzyme to a greater extent than Mg2+ at low concentrations, Mg2+ stimulates to a greater extent than Mn2+ at high concentration, but each is maximally effective at a concentration around 8 mM
Mg2+
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Mg2+ required, not Mn2+, Ca2+
Mg2+
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divalent cation required, maximum stimulation in presence of Ca2+. Co2+, Mg2+ or Mn2+ can replace Ca2+
Mg2+
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divalent cation required, efficiency of activiation in descending order: Mg2+, Mn2+, Ca2+, Co2+, Zn2+; Km: 0.7 mM
Mn2+
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divalent cation required, either Mg2+ or Mn2+, Mn2+ stimulates the enzyme to a greater extent than Mg2+ at low concentrations, Mg2+ stimulates to a greater extent than Mn2+ at high concentration, but each is maximally effective at a concentration around 8 mM
Mn2+
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divalent cation required, maximum stimulation in presence of Ca2+. Co2+, Mg2+ or Mn2+ can replace Ca2+
Mn2+
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MnCl2 stimulates at 1 mM, inhibits at higher concentration
Mn2+
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divalent cation required, efficiency of activiation in descending order: Mg2+, Mn2+, Ca2+, Co2+, Zn2+
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Amphomycin
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IC50 0.04 mM
MnCl2
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stimulates at 1 mM, inhibits at higher concentration
EDTA
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inhibition reversed by MgCl2
tunicamycin
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tunicamycin
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50% inhibition at 0.04 mg per ml
UDP
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competitive
UMP
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reversible
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detergent
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required for maximum activity, optimum for Triton X-100: 0.015%
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Phospholipid
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required, phosphatidylethanolamine most effective
Reducing agent
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required
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Triton X-100
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required for optimal activity, 0.01-0.015%
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Plasmacytoma
Partial purification and properties of a murine plasmacytoma glucosyltransferase.
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0.0012 - 0.0045
dolichyl phosphate
0.00015 - 0.104
UDP-glucose
additional information
additional information
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0.0012
dolichyl phosphate
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0.002
dolichyl phosphate
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0.0045
dolichyl phosphate
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0.00015
UDP-glucose
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pH 7.2
0.00033
UDP-glucose
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pH 5.3
additional information
additional information
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additional information
additional information
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0.0076
UDP-glucuronic acid
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0.1
UDP
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at pH 7.2
0.1
UMP
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0.04
Amphomycin
Candida albicans
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IC50 0.04 mM
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additional information
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additional information
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5.3
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second optimum at pH 7.2
7.2
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second optimum at pH 5.3
7.5
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Tris/HCl buffer
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5.6 - 8.8
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pH 5.6: 25% of maximum activity, pH 8.8: about 40% of maximum activity
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brenda
calf
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mung bean
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L. inbred A 636
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strain ATCC 26555
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rat
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culture
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active centres are cytoplasmically oriented, activation by detergent may be conformation-dependent
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membrane
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36000
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x * 36000, SDS-PAGE
38000
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x * 38000, deduced from gene sequence
39000
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x * 39000, SDS-PAGE after photoaffinity labeling, catalytic subunit
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?
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x * 36000, SDS-PAGE
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x * 38000, deduced from gene sequence
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x * 39000, SDS-PAGE after photoaffinity labeling, catalytic subunit
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30
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2 h, 50% loss of activity
52
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10 min, complete loss of activity
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uridine or UDPglucuronic acid, 5 mM, protects solubilized enzyme against rapid inactivation
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-20°C, indefinitely stable below
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4°C, stable for several days
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partial
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5 mM uridine or UDPglucuronic acid reconstitutes inactivated enzyme
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Villemez, C.L.; Carlo, P.L.
Properties of a soluble polyprenyl phosphate: UDP-D-glucose glucosyltransferase
J. Biol. Chem.
254
4814-4819
1979
Acanthamoeba castellanii
brenda
Herscovics, A.; Bugge, B.; Jeanloz, R.W.
Glucosyltransferase activity in calf pancreas microsomes. Formation of dolichyl D[14C]glucosyl phosphate and 14C-labeled lipid-linked oligosaccharides from UDP-D-[14C]glucose
J. Biol. Chem.
252
2271-2277
1977
Bos taurus
brenda
Behrens, N.H.; Leloir, L.F.
Dolichol monophosphate glucose: an intermediate in glucose transfer in liver
Proc. Natl. Acad. Sci. USA
66
153-159
1970
Rattus norvegicus
brenda
Riedell, W.E.; Miernyk, J.A.
Glycoprotein synthesis in maize endosperm cells. The nucleoside diphosphate-sugar:dolichol-phosphate glycosyltransferase
Plant Physiol.
87
420-426
1988
Zea mays
brenda
Matern, H.; Bolz, R.; Matern, S.
Isolation and characterization of UDP-glucose dolichyl-phosphate glucosyltransferase from human liver
Eur. J. Biochem.
190
99-105
1990
Homo sapiens
brenda
Matern, H.; Matern, S.
Control of dolichyl phosphoglucose formation in human liver microsomes. Kinetic and inhibition studies of nucleosides, nucleotides and analogues of UDPglucose
Biochim. Biophys. Acta
1004
67-72
1989
Homo sapiens
brenda
Drake, R.R.; Kaushal, G.P.; Pastuszak, I.; Elbein, A.D.
Partial purificaton, photoaffinity labeling, and properties of mung bean UDP-glucose:dolicholphosphate glucosyltransferase
Plant Physiol.
97
396-401
1991
Vigna radiata var. radiata
brenda
Miernyk, J.A.; Riedell, W.E.
Characterization of maize endosperm UDP-glucose:dolicholphosphate glucosyltransferase
Phytochemistry
30
2865-2867
1991
Zea mays
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brenda
Arroyo-Flores, B.L.; Rodriguez-Bonilla, J.; Villagomez-Castro, J.C.; Calvo-Mendez, C.; Flores-Carreon, A.; Lopez-Romero, E.
Biosynthesis of glycoproteins in Candida albicans: Activity of mannosyl and glucosyl transferases
Fungal Genet. Biol.
30
127-133
2000
Candida albicans
brenda
Gartung, C.; Matern, S.; Matern, H.
The submicrosomal localization of uridine 5'-diphosphate-glucose dolichyl-phosphate glucosyltransferase and bile acid glucosyltransferase in the human liver
J. Hepatol.
20
32-40
1994
Homo sapiens
brenda
Bossuyt, X.; Blanckaert, N.
Topology of nucleotide-sugar:dolichyl phosphate glycosyltransferases involved in the dolichol pathway for protein glycosylation in native rat liver microsomes
Biochem. J.
296
627-632
1993
Rattus norvegicus
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brenda
Heesen, S.; Lehle, L.; Weissmann, A.; Aebi, M.
Isolation of the ALG5 locus encoding the UDP-glucose:dolichyl-phosphate glucosyltransferase from Saccharomyces cerevisiae
Eur. J. Biochem.
224
71-79
1994
Saccharomyces cerevisiae
brenda
Rodriguez-Bonilla, J.; Vargas-Rodriguez, L.; Calvo-Mendez, C.; Flores-Carreon, A.; Lopez-Romero, E.
Biosynthesis of glycoproteins in Candida albicans: Biochemical characterization of dolichol phosphate glucose synthase
Antonie van Leeuwenhoek
73
373-380
1998
Candida albicans
brenda
Lopez-Romero, E.; Flores-Carreon, A.; Arroyo-Flores, B.L.; Torre-Bouscoulet, M.E.; Bravo-Torres, J.C.; Villagomez-Castro, J.C.; Balcazar-Orozco, R.
Glycosyl transferases and glycosidases of glycoprotein biosynthesis with emphasis on Candida albicans and Entamoeba histolytica
Recent Res. Dev. Microbiol.
4
667-681
2000
Candida albicans
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brenda
Haecker, A.; Bergman, M.; Neupert, C.; Moussian, B.; Luschnig, S.; Aebi, M.; Mannervik, M.
Wollknauel is required for embryo patterning and encodes the Drosophila ALG5 UDP-glucose:dolichyl-phosphate glucosyltransferase
Development
135
1745-1749
2008
Drosophila sp. (in: Insecta)
brenda
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2.4.1.117 dolichyl-phosphate beta-glucosyltransferase
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