Information on EC 2.4.1.117 - dolichyl-phosphate beta-glucosyltransferase

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The enzyme appears in viruses and cellular organisms

top print hide
EC NUMBER
COMMENTARY hide
2.4.1.117
-
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RECOMMENDED NAME
GeneOntology No.
dolichyl-phosphate beta-glucosyltransferase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
UDP-glucose + dolichyl phosphate = UDP + dolichyl beta-D-glucosyl phosphate
show the reaction diagram
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hexosyl group transfer
-
-
-
-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
protein N-glycosylation initial phase (eukaryotic)
-
-
dolichyl-diphosphooligosaccharide biosynthesis
-
-
N-Glycan biosynthesis
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-
Metabolic pathways
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-
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SYSTEMATIC NAME
IUBMB Comments
UDP-glucose:dolichyl-phosphate beta-D-glucosyltransferase
Solanesyl phosphate and ficaprenyl phosphate can act as acceptors, but more slowly.
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CAS REGISTRY NUMBER
COMMENTARY hide
71061-42-2
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
calf
-
-
Manually annotated by BRENDA team
mung bean
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-
Manually annotated by BRENDA team
L. inbred A 636
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-
Manually annotated by BRENDA team
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
UDP-glucose + dolichyl phosphate
UDP + dolichyl beta-D-glucosyl phosphate
show the reaction diagram
UDP-glucose + ficaprenyl phosphate
UDP + ficaprenyl beta-D-glucosyl phosphate
show the reaction diagram
-
-
-
-
r
UDP-glucose + solanesyl phosphate
UDP + solanesyl beta-D-glucosyl phosphate
show the reaction diagram
-
-
-
-
r
additional information
?
-
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
UDP-glucose + dolichyl phosphate
UDP + dolichyl beta-D-glucosyl phosphate
show the reaction diagram
-
-
-
-
r
additional information
?
-
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Zn2+
-
divalent cation required, efficiency of activiation in descending order: Mg2+, Mn2+, Ca2+, Co2+, Zn2+
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Amphomycin
-
IC50 0.04 mM
Ca2+
-
slight inhibition
Mn2+
-
slight inhibition
MnCl2
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stimulates at 1 mM, inhibits at higher concentration
tunicamycin
UDP-glucuronic acid
-
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
detergent
-
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
-
required
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Triton X-100
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required for optimal activity, 0.01-0.015%
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0012 - 0.0045
dolichyl phosphate
0.00015 - 0.104
UDP-glucose
additional information
additional information
-
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.1 - 0.17
UDP
0.0076
UDP-glucuronic acid
-
-
0.1 - 0.66
UMP
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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.04
Amphomycin
Candida albicans
-
IC50 0.04 mM
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.3
-
second optimum at pH 7.2
6.5
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-
7.2
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second optimum at pH 5.3
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
top print hide
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
36000
-
x * 36000, SDS-PAGE
38000
-
x * 38000, deduced from gene sequence
39000
-
x * 39000, SDS-PAGE after photoaffinity labeling, catalytic subunit
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30
-
2 h, 50% loss of activity
52
-
10 min, complete loss of activity
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
uridine or UDPglucuronic acid, 5 mM, protects solubilized enzyme against rapid inactivation
-
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, indefinitely stable below
-
-70°C, up to 4 weeks
-
4°C, stable for several days
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
partial
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
top print hide
Renatured/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
5 mM uridine or UDPglucuronic acid reconstitutes inactivated enzyme
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Show AA Sequence (122 entries)
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LINKS TO OTHER DATABASES (specific for EC-Number 2.4.1.117)
ExplorEnz
ExPASy
KEGG
MetaCyc
SABIO-RK
NCBI: PubMed, Protein, Nucleotide, Structure, Genome, OMIM
IUBMB Enzyme Nomenclature
PROSITE Database of protein families and domains
InterPro (database of protein families, domains and functional sites)