Information on EC 2.4.1.47 - N-acylsphingosine galactosyltransferase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
2.4.1.47
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RECOMMENDED NAME
GeneOntology No.
N-acylsphingosine galactosyltransferase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
UDP-alpha-D-galactose + a ceramide = UDP + a D-galactosylceramide
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
Ether lipid metabolism
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gala-series glycosphingolipids biosynthesis
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Metabolic pathways
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Sphingolipid metabolism
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SYSTEMATIC NAME
IUBMB Comments
UDP-galactose:N-acylsphingosine D-galactosyltransferase
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CAS REGISTRY NUMBER
COMMENTARY hide
37277-54-6
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37277-56-8
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
3 days old
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-
Manually annotated by BRENDA team
fetus
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-
Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
UDP-galactose + ceramide
UDP + D-galactosylceramide
show the reaction diagram
UDPgalactose + 2-(2-hydroxyacyl)sphingosine
1-(beta-D-galactosyl)-2-(2-hydroxyacyl)sphingosine + UDP
show the reaction diagram
UDPglucose + 2-(2-hydroxyacyl)sphingosine
glucocerebroside + UDP
show the reaction diagram
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at 7-10% of the activity with UDP-galactose
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?
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-galactose + ceramide
UDP + D-galactosylceramide
show the reaction diagram
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-
-
?
UDPgalactose + 2-(2-hydroxyacyl)sphingosine
1-(beta-D-galactosyl)-2-(2-hydroxyacyl)sphingosine + UDP
show the reaction diagram
additional information
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Ca2+
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stimulates at 10 mM, dialyzed enzyme has requirement for divalent cations
additional information
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not activated by Cu2+, Fe2+, Co2+, Ni2+, Zn2+, Cd2+
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Detergents
DL-sphingosine
Octanoyl-D-threo-p-nitro-1-phenyl-2-amino-1,3-propanediol
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Phospholipase A
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almost complete inactivation
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Phospholipase C
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56% loss of activity
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Protein inhibitor
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from brain, kidney, spleen and liver of rat and other animals
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Sodium deoxycholate
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strong inhibition
sodium taurocholate
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strong inhibition
sodium taurodeoxycholate
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strong inhibition
additional information
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nutritional inadequacy during the active growth phase of the brain causes significantly diminished enzyme activity
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
HSP70
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dog heat shock protein 70 increases production of lactosylceramide to 156%
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phosphatidylcholine
phosphatidylethanolamine
Phospholipids
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.018 - 0.15
2-(2-hydroxyacyl)sphingosine
0.027 - 0.04
UDPgalactose
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.001455
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0.002733
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additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.7
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in bicine buffer
7.8 - 8.2
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7.8
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assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
27
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assay at
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
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cerebrum, cerebellum and brain stem of 14 and 21 days old rats
Manually annotated by BRENDA team
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cerebrum, cerebellum and brain stem of 14 and 21 days old rats
Manually annotated by BRENDA team
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cerebrum, cerebellum and brain stem of 14 and 21 days old rats
Manually annotated by BRENDA team
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maximal activity in 19-20 day-old embryos
Manually annotated by BRENDA team
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neuroblastoma cell line
Manually annotated by BRENDA team
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HOG cell line
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
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integrated into ER membrane, enzymatically active part of CGT may be oriented toward the lumen of the ER
Manually annotated by BRENDA team
additional information
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activity can also be found to a minor degree in mitochondrial fraction
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Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
53000
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x * 53000, SDS-PAGE
54000
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x * 54000, SDS-PAGE
59000
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x * 64000, glycosylated protein, x * 59000, deglycosylated protein with glycopeptidase F, SDS-PAGE
400000 - 500000
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
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enzyme forms a complex with UDP-galactose transporter in the endoplasmic reticulum
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
glycoprotein
lipoprotein
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phospholipoprotein
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intact phospholipids required for full activity, high phospholipid content
additional information
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with 3 N-linked glycosylation sites
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
freezing causes 80-85% loss of activity, 2-mercaptoethanol protects against inactivation by freezing
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glycerol stabilizes
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in presence of glycerol the enzyme can be frozen and rethawed several times without appreciable loss of stability
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rapidly inactivated by repeated freezing and thawing
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stable in membrane-bound form, activity resisted destruction by pronase treatment at 4°C
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, 50% w/v glycerol, 1 month, about 30% loss of activity
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0°C, 1 day, 50% loss of activity
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4°C, dialyzed enzyme, 0.1% 2-mercaptoethanol, 0.32 M sucrose, 7 days, stable
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
copurified with the L-glutamate/aspartate neurotransmitter transporter GLAST-1 of the central nervous system
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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
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CGT cDNA is cloned, single-copy gene
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CGT gene is cloned, sequenced and characterized, cell-specific and highly time-regulated expression of the gene
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cloning and characterization of the CGT gene, chromosomal localization as a single-copy gene to 4q26
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cloning of the full-length CGT cDNA, open reading frame of 1623 bp encodes a 541 amino acids core protein
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cloning of the full-length CGT cDNA, open reading frame of 1623 bp encodes a 541 amino acids core protein; time-regulated CGT expression
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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
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transcriptional regulation of the CGT gene, 2.3 kb CGT promoter
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
after 17 h under a 42°C heat stress, GalT mRNA increased to 133%
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after 24 h under a 42°C heat stress, GalT mRNA significantly increased to 221%
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine
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study of CGT expression and polymorphism may provide a clue for the understanding of neuropathological diseases involving myelin and myelination