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 hide
2.4.1.45
-
RECOMMENDED NAME
GeneOntology No.
2-hydroxyacylsphingosine 1-beta-galactosyltransferase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
UDP-alpha-D-galactose + a 2-(2-hydroxyacyl)sphingosine = UDP + a 1-(beta-D-galactosyl)-2-(2-hydroxyacyl)sphingosine
show the reaction diagram
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-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hexosyl group transfer
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-
-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Ether lipid metabolism
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Metabolic pathways
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Sphingolipid metabolism
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SYSTEMATIC NAME
IUBMB Comments
UDP-galactose:2-(2-hydroxyacyl)sphingosine 1-beta-D-galactosyl-transferase
Highly specific.
CAS REGISTRY NUMBER
COMMENTARY hide
37277-54-6
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
3 days old
-
-
Manually annotated by BRENDA team
fetus
-
-
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
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
UDPgalactose + 2-(2-hydroxyacyl)sphingosine
1-(beta-D-galactosyl)-2-(2-hydroxyacyl)sphingosine + UDP
show the reaction diagram
additional information
?
-
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
-
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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-
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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
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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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
-
integrated into ER membrane, enzymatically active part of CGT may be oriented toward the lumen of the ER
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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 4C
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20C, 50% w/v glycerol, 1 month, about 30% loss of activity
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0C, 1 day, 50% loss of activity
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4C, 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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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