Information on EC 2.4.1.45 - 2-hydroxyacylsphingosine 1-beta-galactosyltransferase

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The expected taxonomic range for this enzyme is: Amniota

EC NUMBER
COMMENTARY
2.4.1.45
-
RECOMMENDED NAME
GeneOntology No.
2-hydroxyacylsphingosine 1-beta-galactosyltransferase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
UDP-alpha-D-galactose + a 2-(2-hydroxyacyl)sphingosine = UDP + a 1-(beta-D-galactosyl)-2-(2-hydroxyacyl)sphingosine
show the reaction diagram
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
hexosyl group transfer
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
UDP-galactose:2-(2-hydroxyacyl)sphingosine 1-beta-D-galactosyl-transferase
Highly specific.
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
cerebroside synthase
-
-
-
-
CGalT
-
-
-
-
CGT
-
-
-
-
galactosyltransferase, uridine diphosphogalactose-2-hydroxyacylsphingosine
-
-
-
-
UDPgalactose-2-hydroxyacylsphingosine galactosyltransferase
-
-
-
-
UDPgalactose:2-2-hydroxyacylsphingosine galactosyltransferase
-
-
-
-
UDPgalactose:ceramide galactosyltransferase
-
-
-
-
uridine diphosphogalactose-2-hydroxyacylsphingosine galactosyltransferase
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY
37277-54-6
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
3 days old
-
-
Manually annotated by BRENDA team
19-20 days old embryos
-
-
Manually annotated by BRENDA team
15-19 days old
-
-
Manually annotated by BRENDA team
1 month old
-
-
Manually annotated by BRENDA team
15-16 days old
-
-
Manually annotated by BRENDA team
15-20 days old
-
-
Manually annotated by BRENDA team
20 days old; Wistar rats
-
-
Manually annotated by BRENDA team
7, 14 and 21 days old; Wistar rats
-
-
Manually annotated by BRENDA team
isoform GalT-1, expression in CHOlec8 cells
-
-
Manually annotated by BRENDA team
overexpression in transgenic Mus musculus
-
-
Manually annotated by BRENDA team
Sprague-Dawley rats, 18-25 days old
-
-
Manually annotated by BRENDA team
fetus
-
-
Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
UDPgalactose + 2-(2-hydroxyacyl)sphingosine
1-(beta-D-galactosyl)-2-(2-hydroxyacyl)sphingosine + UDP
show the reaction diagram
-
-
-
?
UDPgalactose + 2-(2-hydroxyacyl)sphingosine
1-(beta-D-galactosyl)-2-(2-hydroxyacyl)sphingosine + UDP
show the reaction diagram
-
-
-
?
UDPgalactose + 2-(2-hydroxyacyl)sphingosine
1-(beta-D-galactosyl)-2-(2-hydroxyacyl)sphingosine + UDP
show the reaction diagram
-
-
-
?
UDPgalactose + 2-(2-hydroxyacyl)sphingosine
1-(beta-D-galactosyl)-2-(2-hydroxyacyl)sphingosine + UDP
show the reaction diagram
-
-
-
?
UDPgalactose + 2-(2-hydroxyacyl)sphingosine
1-(beta-D-galactosyl)-2-(2-hydroxyacyl)sphingosine + UDP
show the reaction diagram
-
-
-
?
UDPgalactose + 2-(2-hydroxyacyl)sphingosine
1-(beta-D-galactosyl)-2-(2-hydroxyacyl)sphingosine + UDP
show the reaction diagram
-
-
-
?
UDPgalactose + 2-(2-hydroxyacyl)sphingosine
1-(beta-D-galactosyl)-2-(2-hydroxyacyl)sphingosine + UDP
show the reaction diagram
-
-
cerebroside
?
UDPgalactose + 2-(2-hydroxyacyl)sphingosine
1-(beta-D-galactosyl)-2-(2-hydroxyacyl)sphingosine + UDP
show the reaction diagram
-
-
galactoceramide
?
UDPgalactose + 2-(2-hydroxyacyl)sphingosine
1-(beta-D-galactosyl)-2-(2-hydroxyacyl)sphingosine + UDP
show the reaction diagram
-
-
i.e. 2-hydroxy fatty acid galactosylceramide
?
UDPgalactose + 2-(2-hydroxyacyl)sphingosine
1-(beta-D-galactosyl)-2-(2-hydroxyacyl)sphingosine + UDP
show the reaction diagram
-
highly specific
2-hydroxy fatty acid cerebroside
?
UDPgalactose + 2-(2-hydroxyacyl)sphingosine
1-(beta-D-galactosyl)-2-(2-hydroxyacyl)sphingosine + UDP
show the reaction diagram
-
highly specific
product: galactocerebroside containing 2-hydroxy fatty acids linked to the amino group of the sphingosine moiety
?
UDPgalactose + 2-(2-hydroxyacyl)sphingosine
1-(beta-D-galactosyl)-2-(2-hydroxyacyl)sphingosine + UDP
show the reaction diagram
-
highly specific
i.e. 2-hydroxy fatty acid galactosylceramide
?
UDPgalactose + 2-(2-hydroxyacyl)sphingosine
1-(beta-D-galactosyl)-2-(2-hydroxyacyl)sphingosine + UDP
show the reaction diagram
-
ceramide containing 2-hydroxystearic acid as the predominant fatty acid
product: galactocerebroside containing 2-hydroxy fatty acids linked to the amino group of the sphingosine moiety
?
UDPgalactose + 2-(2-hydroxyacyl)sphingosine
1-(beta-D-galactosyl)-2-(2-hydroxyacyl)sphingosine + UDP
show the reaction diagram
-
i.e. 2-hydroxy fatty acid ceramide
cerebroside
?
UDPgalactose + 2-(2-hydroxyacyl)sphingosine
1-(beta-D-galactosyl)-2-(2-hydroxyacyl)sphingosine + UDP
show the reaction diagram
-
i.e. 2-hydroxy fatty acid ceramide
cerebroside
?
UDPgalactose + 2-(2-hydroxyacyl)sphingosine
1-(beta-D-galactosyl)-2-(2-hydroxyacyl)sphingosine + UDP
show the reaction diagram
-
i.e. 2-hydroxy fatty acid ceramide
2-hydroxy fatty acid cerebroside
?
UDPgalactose + 2-(2-hydroxyacyl)sphingosine
1-(beta-D-galactosyl)-2-(2-hydroxyacyl)sphingosine + UDP
show the reaction diagram
-
i.e. 2-hydroxy fatty acid ceramide
2-hydroxy fatty acid cerebroside
?
UDPgalactose + 2-(2-hydroxyacyl)sphingosine
1-(beta-D-galactosyl)-2-(2-hydroxyacyl)sphingosine + UDP
show the reaction diagram
-
i.e. 2-hydroxy fatty acid ceramide
i.e. 2-hydroxy fatty acid galactosylceramide
?
UDPgalactose + 2-(2-hydroxyacyl)sphingosine
1-(beta-D-galactosyl)-2-(2-hydroxyacyl)sphingosine + UDP
show the reaction diagram
-
i.e. 2-hydroxy fatty acid ceramide
i.e. 2-hydroxy fatty acid galactosylceramide
?
UDPgalactose + 2-(2-hydroxyacyl)sphingosine
1-(beta-D-galactosyl)-2-(2-hydroxyacyl)sphingosine + UDP
show the reaction diagram
-
i.e. 2-hydroxy fatty acid ceramide
i.e. 2-hydroxy fatty acid galactosylceramide
?
UDPgalactose + 2-(2-hydroxyacyl)sphingosine
1-(beta-D-galactosyl)-2-(2-hydroxyacyl)sphingosine + UDP
show the reaction diagram
-
i.e. 2-hydroxy fatty acid ceramide, synthesis of cerebroside
-
?
UDPgalactose + 2-(2-hydroxyacyl)sphingosine
1-(beta-D-galactosyl)-2-(2-hydroxyacyl)sphingosine + UDP
show the reaction diagram
-
i.e. 2-hydroxy fatty acid ceramide, synthesis of cerebroside
-
?
UDPgalactose + 2-(2-hydroxyacyl)sphingosine
1-(beta-D-galactosyl)-2-(2-hydroxyacyl)sphingosine + UDP
show the reaction diagram
-
enzyme may play an important role in the synthesis of at least one type of myelin
-
?
UDPgalactose + 2-(2-hydroxyacyl)sphingosine
1-(beta-D-galactosyl)-2-(2-hydroxyacyl)sphingosine + UDP
show the reaction diagram
-
key enzymatic step in the biosynthesis of the galactocerebrosides, cell-specific and highly time-regulated expression of the CGT gene in the terminal differentiated oligodendrocytes of CNS and in Schwann cells of PNS
galactocerebroside
?
UDPgalactose + 2-(2-hydroxyacyl)sphingosine
1-(beta-D-galactosyl)-2-(2-hydroxyacyl)sphingosine + UDP
show the reaction diagram
-
key enzyme in the biosynthesis of galactocerebroside, the most abundant glycosphingolipid in the myelin sheath
galactocerebroside
?
UDPgalactose + 2-(2-hydroxyacyl)sphingosine
1-(beta-D-galactosyl)-2-(2-hydroxyacyl)sphingosine + UDP
show the reaction diagram
Rattus norvegicus Wistar
-
-
cerebroside
?
UDPglucose + 2-(2-hydroxyacyl)sphingosine
glucocerebroside + UDP
show the reaction diagram
-
at 7-10% of the activity with UDP-galactose
-
?
additional information
?
-
-
-
-
-
-
additional information
?
-
-
-
-
-
-
additional information
?
-
-
not: galactose, galactose-1-phosphat, ADP-galactose
-
-
-
additional information
?
-
-
not: glucosylceramide, lactosylceramide, asialo GM2ganglioside
-
-
-
additional information
?
-
-
not: ceramide containing nonhydroxy fatty acids
-
-
-
additional information
?
-
-
not: ceramide containing nonhydroxy fatty acids
-
-
-
additional information
?
-
-
final step of galactosylceramide synthesis, which plays a role in myelin formation, signal transduction and oligodendrocyte development
-
-
-
additional information
?
-
-
key enzyme in the biosynthesis of cerebrosides and sulfatides, cell-specific and highly time-regulated expression of the CGT gene is thought to play an important role in oligodendrocyte and Schwann cell differentiation
-
-
-
additional information
?
-
-
oligodendrocyte-specific enzyme is involved in the biosynthesis of the oligodendrocyte- and myelin-specific cerebrosides, time-regulated CGT expression with a peak around postnatal days 15-25
-
-
-
additional information
?
-
-
last step in biosynthesis of cerebrosides
-
-
-
additional information
?
-
-
enzyme ensures a supply of UDP-galactose in the endoplasmic reticulum lumen by retaining UDP-galactose transporter in a molecular complex
-
-
-
additional information
?
-
Rattus norvegicus Wistar
-
oligodendrocyte-specific enzyme is involved in the biosynthesis of the oligodendrocyte- and myelin-specific cerebrosides, time-regulated CGT expression with a peak around postnatal days 15-25
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
UDPgalactose + 2-(2-hydroxyacyl)sphingosine
1-(beta-D-galactosyl)-2-(2-hydroxyacyl)sphingosine + UDP
show the reaction diagram
-
i.e. 2-hydroxy fatty acid ceramide, synthesis of cerebroside
-
?
UDPgalactose + 2-(2-hydroxyacyl)sphingosine
1-(beta-D-galactosyl)-2-(2-hydroxyacyl)sphingosine + UDP
show the reaction diagram
-
i.e. 2-hydroxy fatty acid ceramide, synthesis of cerebroside
-
?
UDPgalactose + 2-(2-hydroxyacyl)sphingosine
1-(beta-D-galactosyl)-2-(2-hydroxyacyl)sphingosine + UDP
show the reaction diagram
-
enzyme may play an important role in the synthesis of at least one type of myelin
-
?
UDPgalactose + 2-(2-hydroxyacyl)sphingosine
1-(beta-D-galactosyl)-2-(2-hydroxyacyl)sphingosine + UDP
show the reaction diagram
-
key enzymatic step in the biosynthesis of the galactocerebrosides, cell-specific and highly time-regulated expression of the CGT gene in the terminal differentiated oligodendrocytes of CNS and in Schwann cells of PNS
galactocerebroside
?
UDPgalactose + 2-(2-hydroxyacyl)sphingosine
1-(beta-D-galactosyl)-2-(2-hydroxyacyl)sphingosine + UDP
show the reaction diagram
-
key enzyme in the biosynthesis of galactocerebroside, the most abundant glycosphingolipid in the myelin sheath
galactocerebroside
?
additional information
?
-
-
-
-
-
-
additional information
?
-
-
final step of galactosylceramide synthesis, which plays a role in myelin formation, signal transduction and oligodendrocyte development
-
-
-
additional information
?
-
-
key enzyme in the biosynthesis of cerebrosides and sulfatides, cell-specific and highly time-regulated expression of the CGT gene is thought to play an important role in oligodendrocyte and Schwann cell differentiation
-
-
-
additional information
?
-
-
oligodendrocyte-specific enzyme is involved in the biosynthesis of the oligodendrocyte- and myelin-specific cerebrosides, time-regulated CGT expression with a peak around postnatal days 15-25
-
-
-
additional information
?
-
-
last step in biosynthesis of cerebrosides
-
-
-
additional information
?
-
-
enzyme ensures a supply of UDP-galactose in the endoplasmic reticulum lumen by retaining UDP-galactose transporter in a molecular complex
-
-
-
additional information
?
-
Rattus norvegicus Wistar
-
oligodendrocyte-specific enzyme is involved in the biosynthesis of the oligodendrocyte- and myelin-specific cerebrosides, time-regulated CGT expression with a peak around postnatal days 15-25
-
-
-
METALS and IONS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
Ca2+
-
stimulates at 10 mM, dialyzed enzyme has requirement for divalent cations
Mg2+
-
dialyzed enzyme has requirement for divalent cations, optimal stimulation at 5 mM; stimulates
Mg2+
-
stimulates
Mg2+
-
Mg2+ required rather than Mn2+; stimulates
Mn2+
-
at 10 mM, dialyzed enzyme has requirement for divalent cations; stimulates
Mn2+
-
stimulates
Mn2+
-
Mg2+ required rather than Mn2+; stimulates
additional information
-
not activated by Cu2+, Fe2+, Co2+, Ni2+, Zn2+, Cd2+
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
Detergents
-
inhibition by excess detergent
DL-sphingosine
-
at higher concentrations
Octanoyl-D-threo-p-nitro-1-phenyl-2-amino-1,3-propanediol
-
-
-
Phospholipase A
-
almost complete inactivation
-
Phospholipase C
-
56% loss of activity
-
Protein inhibitor
-
from brain, kidney, spleen and liver of rat and other animals
-
Sodium deoxycholate
-
strong inhibition
sodium taurocholate
-
strong inhibition
sodium taurodeoxycholate
-
strong inhibition
additional information
-
nutritional inadequacy during the active growth phase of the brain causes significantly diminished enzyme activity
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
phosphatidylcholine
-
stimulates
phosphatidylcholine
-
optimum phospholipid requirement of phosphatidylethanolamine: phosphatidylcholine of 5:1 with 2.5fold stimulation, Na cholate prevents stimulation
phosphatidylethanolamine
-
stimulates
phosphatidylethanolamine
-
optimum phospholipid requirement of phosphatidylethanolamine: phosphatidylcholine of 5:1 with 2.5fold stimulation, Na cholate prevents stimulation
Phospholipids
-
addition to incubation mixture containing Triton X-100 increases activity
Phospholipids
-
optimum phospholipid requirement of phosphatidylethanolamine: phosphatidylcholine of 5:1 with 2.5fold stimulation, Na cholate prevents stimulation
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.018
-
2-(2-hydroxyacyl)sphingosine
-
Km value for ceramide is influenced by its dispersion state, in presence of 2 mM Triton S-100 biphasic kinetics are observed with increasing ceramide concentration, yielding two apparent Km values of 0.018 and 0.15 mM
0.11
-
2-(2-hydroxyacyl)sphingosine
-
-
0.15
-
2-(2-hydroxyacyl)sphingosine
-
Km value for ceramide is influenced by its dispersion state, in presence of 2 mM Triton S-100 biphasic kinetics are observed with increasing ceramide concentration, yielding two apparent Km values of 0.018 and 0.15 mM
0.027
0.034
UDPgalactose
-
-
0.04
-
UDPgalactose
-
-
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
0.001455
-
-
-
0.002733
-
-
-
additional information
-
-
more, specific activity is maximal at about 21 days and then gradually declines
additional information
-
-
-
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
7.7
-
-
in bicine buffer
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
27
-
-
assay at
37
-
-
assay at
SOURCE TISSUE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
SOURCE
-
cerebrum, cerebellum and brain stem of 14 and 21 days old rats, whole brain of 7 days old rats
Manually annotated by BRENDA team
Rattus norvegicus Wistar
-
-
-
Manually annotated by BRENDA team
-
cerebrum, cerebellum and brain stem of 14 and 21 days old rats
Manually annotated by BRENDA team
-
cerebrum, cerebellum and brain stem of 14 and 21 days old rats
Manually annotated by BRENDA team
-
cerebrum, cerebellum and brain stem of 14 and 21 days old rats
Manually annotated by BRENDA team
-
maximal activity in 19-20 day-old embryos
Manually annotated by BRENDA team
-
human fetal glioma cell line; N-370 FG cells
Manually annotated by BRENDA team
-
N-370 FG cells
Manually annotated by BRENDA team
-
only weakly expressed in
Manually annotated by BRENDA team
Rattus norvegicus Wistar
-
only weakly expressed in
-
Manually annotated by BRENDA team
-
neuroblastoma cell line
Manually annotated by BRENDA team
-
oligodendrocyte-specific enzyme
Manually annotated by BRENDA team
-
overexpression of enzyme results in 4fold increase in activity and concomitant decrease in alpha-hydroxylated galactosylceramide and significant up-regulation of the myelin and lymphocyte protein
Manually annotated by BRENDA team
Rattus norvegicus Wistar
-
oligodendrocyte-specific enzyme
-
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
translation product with N-terminal 20 amino acids signal sequence, C-terminal 23 amino acids transmembrane domain and KKVK endoplasmic reticulum retention signal
Manually annotated by BRENDA team
-
with endoplasmic reticulum retention signal
Manually annotated by BRENDA team
-
integrated into ER membrane, enzymatically active part of CGT may be oriented toward the lumen of the ER
Manually annotated by BRENDA team
-
with C-terminal 23 amino acids transmembrane domain
Manually annotated by BRENDA team
-
with transmembrane helical domain, hydrophobic sequence of 20 amino acids in the C-terminal domain
Manually annotated by BRENDA team
Rattus norvegicus Wistar
-
-
-
-
Manually annotated by BRENDA team
-
smooth endoplasmic reticulum, with C-terminal endoplasmic reticulum membrane retention signal, C-terminal 20 residue transmembrane domain as anchor of enzyme in the membrane of the ER
Manually annotated by BRENDA team
Rattus norvegicus Wistar
-
smooth endoplasmic reticulum, with C-terminal endoplasmic reticulum membrane retention signal, C-terminal 20 residue transmembrane domain as anchor of enzyme in the membrane of the ER
-
Manually annotated by BRENDA team
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
400000
500000
-
lipoprotein complex
400000
500000
-
enzyme-phospholipid-detergent complex, gel filtration
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
?
-
x * 53000, SDS-PAGE
?
-
x * 64000
?
-
x * 64000, glycosylated protein, x * 59000, deglycosylated protein with glycopeptidase F, SDS-PAGE
?
-
x * 54000, SDS-PAGE
?
Rattus norvegicus Wistar
-
x * 64000, glycosylated protein, x * 59000, deglycosylated protein with glycopeptidase F, SDS-PAGE
-
additional information
-
enzyme forms a complex with UDP-galactose transporter in the endoplasmic reticulum
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
glycoprotein
-
high mannose glycoprotein; translation product with 3 putative N-glycosylation sites
glycoprotein
-
3 putative glycosylation sites at Asn-78, Asn-333 and Asn-442, but only Asn-78 and Asn-333 are glycosylated, deglycosylated 59 kDa core protein is still enzymatically active; high mannose glycoprotein
lipoprotein
-
-
phospholipoprotein
-
intact phospholipids required for full activity, high phospholipid content
glycoprotein
Rattus norvegicus Wistar
-
3 putative glycosylation sites at Asn-78, Asn-333 and Asn-442, but only Asn-78 and Asn-333 are glycosylated, deglycosylated 59 kDa core protein is still enzymatically active; high mannose glycoprotein
-
glycoprotein
-
-
additional information
-
with 3 N-linked glycosylation sites
GENERAL STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
freezing causes 80-85% loss of activity, 2-mercaptoethanol protects against inactivation by freezing
-
glycerol stabilizes
-
in presence of glycerol the enzyme can be frozen and rethawed several times without appreciable loss of stability
-
rapidly inactivated by repeated freezing and thawing
-
stable in membrane-bound form, activity resisted destruction by pronase treatment at 4C
-
STORAGE STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
4C, dialyzed enzyme, 0.1% 2-mercaptoethanol, 0.32 M sucrose, 7 days, stable
-
-20C, 50% w/v glycerol, 1 month, about 30% loss of activity
-
0C, 1 day, 50% loss of activity
-
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
copurified with the L-glutamate/aspartate neurotransmitter transporter GLAST-1 of the central nervous system
-
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
CGT cDNA is cloned, single-copy gene
-
cell-specific and highly time-regulated expression of the CGT gene in the terminal differentiated oligodendrocyte of CNS and in Schwann cells of PNS; cloning and characterization of the CGT gene, chromosomal localization as a single-copy gene to 4q26; nucleotide sequence of the cDNA, single-copy gene
-
cloning and characterization of the CGT gene, chromosomal localization as a single-copy gene to 4q26
-
isolation of the complete copy of CGT cDNA, which is cloned into a pCR 3.1 expression vector, transfection of polyoma virus LT antigen-expressing CHO cells and expression; nucleotide sequence of the cDNA, single-copy gene
-
transcriptional regulation of the CGT gene, 2.3 kb CGT promoter
-
CGT gene is cloned, sequenced and characterized, cell-specific and highly time-regulated expression of the gene
-
cloning of the full-length CGT cDNA, open reading frame of 1623 bp encodes a 541 amino acids core protein
-
cloning of the full-length CGT cDNA, open reading frame of 1623 bp encodes a 541 amino acids core protein; time-regulated CGT expression
-
ENGINEERING
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
additional information
-
overexpression of enzyme results in 4fold increase in activity and concomitant decrease in alpha-hydroxylated galactosylceramide and significant up-regulation of the myelin and lymphocyte protein. Animals developed a progressive hindlimb paralysis and demyelination in the central nervous system
additional information
-
cotransfection of enzyme and UDP-galactose transporter retains UDP-galactose transporter in the endoplasmic reticulum, where it forms a complex with enzyme
APPLICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
medicine
-
study of CGT expression and polymorphism may provide a clue for the understanding of neuropathological diseases involving myelin and myelination