Any feedback?
Information on EC 2.4.1.80 - ceramide glucosyltransferase and Organism(s) Rattus norvegicus and UniProt Accession Q9R0E0
for references in articles please use BRENDA:EC2.4.1.80Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
2.4.1.80 ceramide glucosyltransferaseIUBMB Comments
Sphingosine and dihydrosphingosine can also act as acceptors; CDP-glucose can act as donor.
Specify your search results
Word Map
- 2.4.1.80
- glucosylceramide
- glycosphingolipids
- sphingolipids
- gangliosides
- gm3
-
sphingoid
- galactosylceramide
- d-threo-1-phenyl-2-decanoylamino-3-morpholino-1-propanol
- gaucher
-
d-pdmp
- n-butyldeoxynojirimycin
-
nb-dnj
- 1-phenyl-2-decanoylamino-3-morpholino-1-propanol
-
galcers
- medicine
-
udp-galactose:ceramide
- glucocerebroside
- cgalt
-
laccer
-
conduritol
- pharmacology
- molecular biology
- drug development
The taxonomic range for the selected organisms is: Rattus norvegicus
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Reaction Schemes
Synonyms
glccer synthase, ceramide glucosyltransferase, glct-1, glccers, udp-glucose ceramide glucosyltransferase, udp-glucose:ceramide glucosyltransferase, cgt-3, cgt-1, udp-glucose ceramide glycosyltransferase, udp-glc:ceramide glucosyltransferase, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
ceramide:UDP-glucose glucosyltransferase
-
-
-
-
ceramide:UDPGlc glucosyltransferase
-
-
-
-
glucosylceramide synthase
glucosyltransferase, uridine diphosphoglucose-ceramide
-
-
-
-
UDP glucose-ceramide glucosyltransferase
-
-
-
-
UDP-glucose:ceramide glucosyltransferase
-
-
-
-
uridine diphosphoglucose-ceramide glucosyltransferase
-
-
-
-
glucosylceramide synthase
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
UDP-alpha-D-glucose + an N-acylsphingosine = UDP + a beta-D-glucosyl-N-acylsphingosine
UDP-glucose and inhibitor D-PDMP binding region overlap and contain His193
UDP-alpha-D-glucose + an N-acylsphingosine = UDP + a beta-D-glucosyl-N-acylsphingosine
enzyme DNA sequence contains conserved D1,D2,D3,QXXRW motif found also in other progressive beta-glycosyltransferases, putative active site, Cys207 and His193 involved
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hexosyl group transfer
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
UDP-glucose:N-acylsphingosine D-glucosyltransferase
Sphingosine and dihydrosphingosine can also act as acceptors; CDP-glucose can act as donor.
CAS REGISTRY NUMBER
COMMENTARY
37237-44-8
-
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
UDP-glucose + N-[7-(4-nitrobenzo-2-oxa-1,3-diazole)]-6-aminocaproyl-D-erythro-sphingosine
UDP + D-glucosyl-N-[7-(4-nitrobenzo-2-oxa-1,3-diazole)]-6-aminocaproyl-D-erythro-sphingosine
CDP-glucose + N-acylsphingosine
CDP + D-glucosyl-N-acylsphingosine
-
i.e. ceramide
i.e. glucosylceramide
?
TDP-glucose + N-acylsphingosine
TDP + D-glucosyl-N-acylsphingosine
-
i.e. ceramide
i.e. glucosylceramide
?
UDP-glucose + dihydrosphingosine
UDP + D-glucosyl-dihydrosphingosine
-
dihydrosphingosine is no substrate
-
-
?
UDP-glucose + N-acylsphinganine
UDP + D-glucosyl-N-acylsphingosine
-
stereospecific and dependent on nature and chain length of N-acylsphinganine substrate
-
?
UDP-glucose + N-[7-(4-nitrobenzo-2-oxa-1,3-diazole)]-6-aminocaproyl-D-erythro-sphingosine
UDP + D-glucosyl-N-[7-(4-nitrobenzo-2-oxa-1,3-diazole)]-6-aminocaproyl-D-erythro-sphingosine
UDP-glucose + N-acylsphingosine
UDP + D-glucosyl-N-acylsphingosine
i.e. ceramide
i.e. glucosylceramide
?
UDP-glucose + N-acylsphingosine
UDP + D-glucosyl-N-acylsphingosine
i.e. ceramide
i.e. glucosylceramide
?
UDP-glucose + N-acylsphingosine
UDP + D-glucosyl-N-acylsphingosine
i.e. ceramide
i.e. glucosylceramide
?
UDP-glucose + N-[7-(4-nitrobenzo-2-oxa-1,3-diazole)]-6-aminocaproyl-D-erythro-sphingosine
UDP + D-glucosyl-N-[7-(4-nitrobenzo-2-oxa-1,3-diazole)]-6-aminocaproyl-D-erythro-sphingosine
synthetic fluorescent ceramide substrate analogue for fluorescence enzyme assay
-
-
?
UDP-glucose + N-[7-(4-nitrobenzo-2-oxa-1,3-diazole)]-6-aminocaproyl-D-erythro-sphingosine
UDP + D-glucosyl-N-[7-(4-nitrobenzo-2-oxa-1,3-diazole)]-6-aminocaproyl-D-erythro-sphingosine
synthetic fluorescent ceramide substrate analogue for fluorescence enzyme assay
-
-
?
UDP-glucose + N-acylsphingosine
UDP + D-glucosyl-N-acylsphingosine
-
i.e. glucosylceramide
?
UDP-glucose + N-acylsphingosine
UDP + D-glucosyl-N-acylsphingosine
-
acceptor substrate specificity, overview
i.e. glucosylceramide
?
UDP-glucose + N-acylsphingosine
UDP + D-glucosyl-N-acylsphingosine
-
i.e. ceramide
i.e. glucosylceramide
?
UDP-glucose + N-acylsphingosine
UDP + D-glucosyl-N-acylsphingosine
-
i.e. ceramide
i.e. glucosylceramide
?
UDP-glucose + N-acylsphingosine
UDP + D-glucosyl-N-acylsphingosine
-
i.e. ceramide
i.e. glucosylceramide
?
UDP-glucose + N-acylsphingosine
UDP + D-glucosyl-N-acylsphingosine
-
i.e. ceramide
i.e. glucosylceramide
?
UDP-glucose + N-acylsphingosine
UDP + D-glucosyl-N-acylsphingosine
-
i.e. ceramide
i.e. glucosylceramide
?
UDP-glucose + N-acylsphingosine
UDP + D-glucosyl-N-acylsphingosine
-
i.e. ceramide
i.e. glucosylceramide
?
UDP-glucose + N-acylsphingosine
UDP + D-glucosyl-N-acylsphingosine
i.e. ceramide
i.e. glucosylceramide
?
UDP-glucose + N-acylsphingosine
UDP + D-glucosyl-N-acylsphingosine
-
stereospecific and dependent on nature and chain length of N-acylsphingosine substrate
i.e. glucosylceramide
?
UDP-glucose + N-acylsphingosine
UDP + D-glucosyl-N-acylsphingosine
-
UDP-glucose is the preferred donor substrate
i.e. glucosylceramide
?
UDP-glucose + N-acylsphingosine
UDP + D-glucosyl-N-acylsphingosine
-
ceramide plays an important role in signal transduction, regulation, and cell homeostasis, thus its glycosylation may play a role in regulation of the cellular level of the bioactive lipid
i.e. glucosylceramide
?
UDP-glucose + N-acylsphingosine
UDP + D-glucosyl-N-acylsphingosine
-
catalyzes the first step during the sequential addition of carbohydrate moieties for ganglioside biosynthesis
-
-
?
UDP-glucose + N-acylsphingosine
UDP + D-glucosyl-N-acylsphingosine
-
initial key enzyme in glycosphingolipid biosynthesis
-
-
?
UDP-glucose + N-acylsphingosine
UDP + D-glucosyl-N-acylsphingosine
-
initial key enzyme in glycosphingolipid biosynthesis
i.e. glucosylceramide
?
UDP-glucose + N-acylsphingosine
UDP + D-glucosyl-N-acylsphingosine
-
initial key enzyme in glycosphingolipid biosynthesis
i.e. glucosylceramide
?
UDP-glucose + N-acylsphingosine
UDP + D-glucosyl-N-acylsphingosine
-
enzyme activity is regulated developmentally
i.e. glucosylceramide
?
UDP-glucose + N-acylsphingosine
UDP + D-glucosyl-N-acylsphingosine
-
first step in synthesis of gangliosides
-
-
?
UDP-glucose + N-[7-(4-nitrobenzo-2-oxa-1,3-diazole)]-6-aminocaproyl-D-erythro-sphingosine
UDP + D-glucosyl-N-[7-(4-nitrobenzo-2-oxa-1,3-diazole)]-6-aminocaproyl-D-erythro-sphingosine
-
synthetic fluorescent ceramide substrate analogue for fluorescence enzyme assay
-
-
?
UDP-glucose + N-[7-(4-nitrobenzo-2-oxa-1,3-diazole)]-6-aminocaproyl-D-erythro-sphingosine
UDP + D-glucosyl-N-[7-(4-nitrobenzo-2-oxa-1,3-diazole)]-6-aminocaproyl-D-erythro-sphingosine
synthetic fluorescent ceramide substrate analogue for fluorescence enzyme assay
-
-
?
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
UDP-glucose + N-acylsphingosine
UDP + D-glucosyl-N-acylsphingosine
-
i.e. glucosylceramide
?
UDP-glucose + N-acylsphingosine
UDP + D-glucosyl-N-acylsphingosine
-
ceramide plays an important role in signal transduction, regulation, and cell homeostasis, thus its glycosylation may play a role in regulation of the cellular level of the bioactive lipid
i.e. glucosylceramide
?
UDP-glucose + N-acylsphingosine
UDP + D-glucosyl-N-acylsphingosine
-
catalyzes the first step during the sequential addition of carbohydrate moieties for ganglioside biosynthesis
-
-
?
UDP-glucose + N-acylsphingosine
UDP + D-glucosyl-N-acylsphingosine
-
initial key enzyme in glycosphingolipid biosynthesis
-
-
?
UDP-glucose + N-acylsphingosine
UDP + D-glucosyl-N-acylsphingosine
-
initial key enzyme in glycosphingolipid biosynthesis
i.e. glucosylceramide
?
UDP-glucose + N-acylsphingosine
UDP + D-glucosyl-N-acylsphingosine
-
initial key enzyme in glycosphingolipid biosynthesis
i.e. glucosylceramide
?
UDP-glucose + N-acylsphingosine
UDP + D-glucosyl-N-acylsphingosine
-
enzyme activity is regulated developmentally
i.e. glucosylceramide
?
UDP-glucose + N-acylsphingosine
UDP + D-glucosyl-N-acylsphingosine
-
first step in synthesis of gangliosides
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mg2+
Mn2+
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Phospholipase A
-
treatment of microsomes results in loss of enzyme activity
-
Phospholipase C
-
treatment of microsomes results in loss of enzyme activity
-
D-threo-1-phenyl-2-(decanoylamino)-3-morpholino-1-propanol-HCl
i.e. PDMP
D-threo-1-phenyl-2-(decanoylamino)-3-morpholino-1-propanol-HCl
His193 mutants are not inhibited
diethyl dicarbonate
reversible by hydroxylamine, UDP-glucose protects, inhibitor acts on histidine residues, including His193, within or near UDP-glucose binding site
Detergents
-
inhibition of enzyme due to permeabilization of microsomal membrane
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
dioleoyl phosphatidylcholine
-
or other exogenous phospholipid, required for activity
L-threo-1-phenyl-2-decanoylamino-3-morpholino-1-propanol
-
L-PDMP treatment induces a 2.4 increase in glucosylceramide
detergent
-
activity is reduced by most of the detergents tested, only CHAPS and CHAPSO at concentration of 1% w/v stimulate
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.4
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
cerebellar granule cells are treated with GCS inhibitor D-threo-2-palmitoylamino-3-pyrrolidino-1-propanol which induces an increase in log-chain ceramides, loss of viability and dramatic changes in neuron/neurite morphology
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
additional information
-
associated with membranes, structural integrity of the microsomal membranes is essential for activity
-
additional information
-
enzyme is not associated with synaptosomes and myelin
-
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). CEGT_RAT
394
3
44823
Swiss-Prot
Secretory Pathway (Reliability: 1)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
amino acid sequence of conserved D1,D2,D3,QXXRW motif
additional information
-
type III membrane protein structure with N-terminal signal-anchor sequence and a long cytoplasmic tail
additional information
-
enzyme forms dimeric or oligomeric complexes with another protein in the Golgi membrane vivo, topology
additional information
-
enzyme forms dimeric or oligomeric complexes with another protein in the Golgi membrane vivo, topology
additional information
enzyme forms dimeric or oligomeric complexes with another protein in the Golgi membrane vivo, topology
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
C143A
site-directed mutagenesis, increased activity, reduced expression level compared to wild-type
C207A
site-directed mutagenesis, reduced activity, reduced inhibitory effect of N-ethylmaleimide, reduced expression level compared to wild-type
C213A
site-directed mutagenesis, reduced activity, reduced expression level compared to wild-type
C232A
site-directed mutagenesis, reduced expresssion level compared to wild-type
C290A
site-directed mutagenesis, reduced expression level compared to wild-type
C296A
site-directed mutagenesis, reduced activity, reduced expression level compared to wild-type
C343A
site-directed mutagenesis, enhanced activity, slightly reduced expression level compared to wild-type
C86A
site-directed mutagenesis, reduced activity, reduced expression level compared to wild-type
C98A
site-directed mutagenesis, reduced activity, reduced expression level compared to wild-type
H169A
26.4% activity compared to wild-type, reduced inhibition by diethyldicarbonate and increased protection by UDP-glucose
H193A
33.0% activity compared to wild-type, reduced inhibition by diethyldicarbonate and reduced protection by UDP-glucose
H193N
23.0% activity compared to wild-type, reduced inhibition by diethyldicarbonate and reduced protection by UDP-glucose
H26R
118.5% activity compared to wild-type, slightly enhanced inhibition by diethyldicarbonate and slightly reduced protection by UDP-glucose
H308A
35.2% activity compared to wild-type, slightly reduced inhibition by diethyldicarbonate and slightly reduced protection by UDP-glucose
H322N
49.8% activity compared to wild-type, slightly enhanced inhibition by diethyldicarbonate and slightly reduced protection by UDP-glucose
H36A
103.2% activity compared to wild-type, slightly enhanced inhibition by diethyldicarbonate and slightly reduced protection by UDP-glucose
additional information
-
deletion mutants, lacking the first 10 or the last 8 amino acid residues, show only 4% of the wild-type activity
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
partial from Golgi membranes
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
cloning from rat brain genetic library and expression in Escherichia coli BL21(DE3)
cloning from rat brain genetic library and expression in Escherichia coli BL21(DE3)
cloning from rat brain genetic library and expression in Escherichia coli BL21(DE3)
RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
reconstitution of solubilized enzyme in detergent-free lipid vesicles
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
medicine
enzyme inhibition is a possible target for chemotherapeutic agents for a number of diseases, including cancer
medicine
enzyme inhibition is a possible target for chemotherapeutic agents for a number of diseases, including cancer
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Basu, S.; Kaufman, B.; Roseman, S.
Enzymatic synthesis of glucocerebroside by a glucosyltransferase from embryonic chicken brain
J. Biol. Chem.
248
1388-1394
1973
Cavia porcellus, Gallus gallus, Ovis aries, Homo sapiens, Rattus norvegicus, Sus scrofa
Shah, S.N.
UDP-glucose: ceramide glucosyltransferase of rat brain: an association with smooth microsomes and requirement of an intact membrane for enzyme activity
Arch. Biochem. Biophys.
159
143-150
1973
Rattus norvegicus, Rattus norvegicus Sprague-Dawley
Matsuo, N.; Nomura, T.; Imokawa, G.
A rapid and simple assay method for UDP-glucose:ceramide glucosyltransferase
Biochim. Biophys. Acta
1116
97-103
1992
Rattus norvegicus
Paul, P.; Kamisaka, Y.; Marks, D.L.; Pagano, R.E.
Purification and characterization of UDP-glucose:ceramide glucosyltransferase from rat liver Golgi membranes
J. Biol. Chem.
271
2287-2293
1996
Rattus norvegicus
Ichikawa, S.; Hirabayashi, Y.
Glucosylceramide synthase and glycosphingolipid synthesis
Trends Cell Biol.
8
198-202
1998
Caenorhabditis elegans, Mus musculus, Rattus norvegicus, Homo sapiens (Q16739)
Marks, D.L.; Wu, K.; Paul, P.; Kamisaka, Y.; Watanabe, R.; Pagano, R.E.
Oligomerization and topology of the Golgi membrane protein glucosylceramide synthase
J. Biol. Chem.
274
451-456
1999
Homo sapiens, Rattus norvegicus
Wu, K.; Marks, D.L.; Watanabe, R.; Paul, P.; Rajan, N.; Pagano, R.E.
Histidine-193 of rat glucosylceramide synthase resides in a UDP-glucose-and inhibitor (D-threo-1-phenyl-2-decanoylamino-3-morpholinopropan-1-ol)-binding region: a biochemical and mutational study
Biochem. J.
341
395-400
1999
Homo sapiens (Q16739), Rattus norvegicus (Q9R0E0)
-
Marks, D.L.; Paul, P.; Kamisaka, Y.; Pagano, R.E.
Methods for studying glucosylceramide synthase
Methods Enzymol.
311
50-59
2000
Gallus gallus, Homo sapiens, Homo sapiens (Q16739), Mus musculus, Rattus norvegicus, Rattus norvegicus (Q9R0E0), Rattus norvegicus Sprague-Dawley, Sus scrofa
Marks, D.L.; Dominguez, M.; Wu, K.; Pagano, R.E.
Identification of active site residues in glucosylceramide synthase. A nucleotide-binding/catalytic motif conserved with processive beta-glycosyltransferases
J. Biol. Chem.
276
26492-26498
2001
Rattus norvegicus (Q9R0E0)
Marks, N.; Berg, M.J.; Saito, M.; Saito, M.
Glucosylceramide synthase decrease in frontal cortex of Alzheimer brain correlates with abnormal increase in endogenous ceramides: consequences to morphology and viability on enzyme suppression in cultured primary neurons
Brain Res.
1191
136-147
2008
Homo sapiens, Rattus norvegicus
EXTERNAL LINKS (specific for EC-Number 2.4.1.80)
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
Legal
Curated at
Member of
