Any feedback?
No. of entries
Information on EC 2.4.1.117 - dolichyl-phosphate beta-glucosyltransferase
for references in articles please use BRENDA:EC2.4.1.117
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree 2 Transferases
2.4 Glycosyltransferases
2.4.1 Hexosyltransferases
2.4.1.117 dolichyl-phosphate beta-glucosyltransferase
IUBMB Comments
Solanesyl phosphate and ficaprenyl phosphate can act as acceptors, but more slowly.
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
- 2.4.1.117
-
n-linked
- glycosyltransferases
- detergent
-
lipid-linked
- aureus
-
photolabeled
-
photolysis
-
photoaffinity
- oligosaccharide
-
photoinsertion
-
mannosyltransferase
Reaction Schemes
showSynonyms
udp-glucose:dolichyl-phosphate glucosyltransferase, udp-glucose:dolichylphosphate glucosyltransferase, dolichyl-phosphate beta-glucosyltransferase, udp-glucose dolichyl-phosphate glucosyltransferase, udp-glucose:dolichol phosphate glucosyltransferase, udp-glucose:dolichyl phosphate glucosyltransferase, more
topPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
Alg5E
dolichyl-phosphate beta-glucosyltransferase E
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:dolichylphosphate glucosyltransferase
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
UDP-alpha-D-glucose + dolichyl phosphate = UDP + dolichyl beta-D-glucosyl phosphate
sequential mechanism
-
UDP-alpha-D-glucose + dolichyl phosphate = UDP + dolichyl beta-D-glucosyl phosphate
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hexosyl group transfer
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PATHWAY SOURCE
PATHWAYS
MetaCyc
protein N-glycosylation initial phase (eukaryotic)
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SYSTEMATIC NAME
IUBMB Comments
UDP-glucose:dolichyl-phosphate beta-D-glucosyltransferase
Solanesyl phosphate and ficaprenyl phosphate can act as acceptors, but more slowly.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CAS REGISTRY NUMBER
COMMENTARY
71061-42-2
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
UDP-glucose + ficaprenyl phosphate
UDP + ficaprenyl beta-D-glucosyl phosphate
-
Substrates: -
Products: -
Products: -
r
UDP-glucose + solanesyl phosphate
UDP + solanesyl beta-D-glucosyl phosphate
-
Substrates: -
Products: -
Products: -
r
UDP-alpha-D-glucose + dolichyl phosphate
UDP + dolichyl beta-D-glucosyl phosphate
Substrates: the catalytic reaction is faster with longer carbon chains in the substrate. Alg5E shows a preference for branched chain methyl groups in the lipid structure
Products: -
Products: -
?
UDP-alpha-D-glucose + dolichyl phosphate
UDP + dolichyl beta-D-glucosyl phosphate
Substrates: the catalytic reaction is faster with longer carbon chains in the substrate. Alg5E shows a preference for branched chain methyl groups in the lipid structure
Products: -
Products: -
?
UDP-glucose + dolichyl phosphate
UDP + dolichyl beta-D-glucosyl phosphate
-
Substrates: -
Products: -
Products: -
r
UDP-glucose + dolichyl phosphate
UDP + dolichyl beta-D-glucosyl phosphate
-
Substrates: -
Products: -
Products: -
?
UDP-glucose + dolichyl phosphate
UDP + dolichyl beta-D-glucosyl phosphate
-
Substrates: -
Products: -
Products: -
r
UDP-glucose + dolichyl phosphate
UDP + dolichyl beta-D-glucosyl phosphate
-
Substrates: -
Products: -
Products: -
?
UDP-glucose + dolichyl phosphate
UDP + dolichyl beta-D-glucosyl phosphate
-
Substrates: -
Products: -
Products: -
?
UDP-glucose + dolichyl phosphate
UDP + dolichyl beta-D-glucosyl phosphate
-
Substrates: -
Products: -
Products: -
?
UDP-glucose + dolichyl phosphate
UDP + dolichyl beta-D-glucosyl phosphate
-
Substrates: -
Products: -
Products: -
?
UDP-glucose + dolichyl phosphate
UDP + dolichyl beta-D-glucosyl phosphate
-
Substrates: -
Products: -
Products: -
?
UDP-glucose + dolichyl phosphate
UDP + dolichyl beta-D-glucosyl phosphate
-
Substrates: -
Products: -
Products: -
?
additional information
?
-
-
Substrates: no substrate: GDP-D-glucose, UDP-D-glucuronic acid, UDP-N-acetyl-D-glucosamine, UDP-D-xylose
Products: -
Products: -
?
additional information
?
-
-
Substrates: synthesis of dolichyl D-glucosyl phosphate, a glucosyl donor in the formation of lipid-linked core oligosaccharides
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: enzyme is involved in the biosynthesis of the lipid-linked oligosaccharides that are precursors of N-linked glycoproteins
Products: -
Products: -
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
UDP-glucose + dolichyl phosphate
UDP + dolichyl beta-D-glucosyl phosphate
-
Substrates: -
Products: -
Products: -
r
additional information
?
-
-
Substrates: synthesis of dolichyl D-glucosyl phosphate, a glucosyl donor in the formation of lipid-linked core oligosaccharides
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: enzyme is involved in the biosynthesis of the lipid-linked oligosaccharides that are precursors of N-linked glycoproteins
Products: -
Products: -
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
Co2+
Mg2+
Mn2+
Zn2+
-
divalent cation required, efficiency of activiation in descending order: Mg2+, Mn2+, Ca2+, Co2+, Zn2+
Ca2+
-
divalent cation required, maximum stimulation in presence of Ca2+. Co2+, Mg2+ or Mn2+ can replace Ca2+
Ca2+
-
divalent cation required, efficiency of activiation in descending order: Mg2+, Mn2+, Ca2+, Co2+, Zn2+
Co2+
-
divalent cation required, maximum stimulation in presence of Ca2+. Co2+, Mg2+ or Mn2+ can replace Ca2+
Co2+
-
divalent cation required, efficiency of activiation in descending order: Mg2+, Mn2+, Ca2+, Co2+, Zn2+
Mg2+
-
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+
-
divalent cation required, maximum stimulation in presence of Ca2+. Co2+, Mg2+ or Mn2+ can replace Ca2+
Mg2+
-
divalent cation required, efficiency of activiation in descending order: Mg2+, Mn2+, Ca2+, Co2+, Zn2+
Mn2+
-
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+
-
divalent cation required, maximum stimulation in presence of Ca2+. Co2+, Mg2+ or Mn2+ can replace Ca2+
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
detergent
-
required for maximum activity, optimum for Triton X-100: 0.015%
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Plasmacytoma
Partial purification and properties of a murine plasmacytoma glucosyltransferase.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.5
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5.6 - 8.8
-
pH 5.6: 25% of maximum activity, pH 8.8: about 40% of maximum activity
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
active centres are cytoplasmically oriented, activation by detergent may be conformation-dependent
-
brenda
Highest Expressing Human Cell Lines
Cell Line Links Show AA Sequence and Transmembrane Helices (6581 entries)
Longer loading times are possible. Please use the AA Sequence and Transmembrane Helices Search for a specific query.
Longer loading times are possible. Please use the AA Sequence and Transmembrane Helices Search for a specific query.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
39000
-
x * 39000, SDS-PAGE after photoaffinity labeling, catalytic subunit
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
?
-
x * 39000, SDS-PAGE after photoaffinity labeling, catalytic subunit
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
uridine or UDPglucuronic acid, 5 mM, protects solubilized enzyme against rapid inactivation
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
partial
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
-
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
-
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
-
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: flies)
brenda
Li, R.; Hu, Y.; Shang, E.; Gao, X.; Wang, N.
Analysis of enzyme activity and substrate specificity of dolichyl-phosphate beta-glucosyltransferase
Chin. J. Biotechnol.
40
1833-1844
2024
Trichomonas vaginalis (A2DSR8), Trichomonas vaginalis ATCC PRA-98 (A2DSR8)
-
brenda
EXTERNAL LINKS (specific for EC-Number 2.4.1.117)
html completed
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2026.1 (March 2026)
About BRENDA
Social media
Help
Survey
Download
Contribution
Legal
Curated at
Member of
![DSMZ Digital Diversity]()
![Global Core Biodata Resource]()
![ELIXIR Core Data Resource]()
![German Network for Bioinformatics Infrastructure]()
