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Information on EC 2.4.1.47 - N-acylsphingosine galactosyltransferase and Organism(s) Homo sapiens and UniProt Accession Q16880

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EC Tree
     2 Transferases
         2.4 Glycosyltransferases
             2.4.1 Hexosyltransferases
                2.4.1.47 N-acylsphingosine galactosyltransferase
IUBMB Comments
This membrane-bound, endoplasmic reticulum-located enzyme catalyses the last step in the synthesis of galactocerebrosides, which are abundant sphingolipids of the myelin membrane of the central nervous system and peripheral nervous system. It has a strong preference for ceramides that contain hydroxylated fatty acids.
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Homo sapiens
UNIPROT: Q16880
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The taxonomic range for the selected organisms is: Homo sapiens
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Synonyms
ceramide galactosyltransferase, cgalt, cerebroside synthase, udpgalactose:ceramide galactosyltransferase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
cerebroside synthase
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CGalT
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CGT
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galactosyltransferase, uridine diphosphogalactose-2-hydroxyacylsphingosine
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galactosyltransferase, uridine diphosphogalactose-acylsphingosine
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UDP galactose-N-acylsphingosine galactosyltransferase
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UDPgalactose-2-hydroxyacylsphingosine galactosyltransferase
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UDPgalactose:2-2-hydroxyacylsphingosine galactosyltransferase
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UDPgalactose:ceramide galactosyltransferase
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uridine diphosphogalactose-2-hydroxyacylsphingosine galactosyltransferase
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uridine diphosphogalactose-acylsphingosine galactosyltransferase
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hexosyl group transfer
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PATHWAY SOURCE
PATHWAYS
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SYSTEMATIC NAME
IUBMB Comments
UDP-galactose:N-acylsphingosine D-galactosyltransferase
This membrane-bound, endoplasmic reticulum-located enzyme catalyses the last step in the synthesis of galactocerebrosides, which are abundant sphingolipids of the myelin membrane of the central nervous system and peripheral nervous system. It has a strong preference for ceramides that contain hydroxylated fatty acids.
CAS REGISTRY NUMBER
COMMENTARY hide
37277-54-6
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37277-56-8
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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
UDPgalactose + 2-(2-hydroxyacyl)sphingosine
1-(beta-D-galactosyl)-2-(2-hydroxyacyl)sphingosine + UDP
show the reaction diagram
additional information
?
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NATURAL SUBSTRATE
NATURAL 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
additional information
?
-
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
zoledronate
optimal inhibitor of human ceramide galactosyltransferase, showing a favorable steric hindrance factor in contrast to other inhibitors or UDP-gal. It exhibits binding sites distributed homogeneously that can bind simultaneously
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37
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assay at
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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UniProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
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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
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
CGT_HUMAN
541
2
61438
Swiss-Prot
Secretory Pathway (Reliability: 1)
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
glycoprotein
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additional information
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with 3 N-linked glycosylation sites
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
molecular modeling of structure and docking of UDP-Gal, inhibitor zoledronate and inhibitor derivatives. substrate UDP-Gal interacts with amino acids A295, G296, R322, Q343, H358, N362, S363, F380, H383
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
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cloning and characterization of the CGT gene, chromosomal localization as a single-copy gene to 4q26
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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
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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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APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine
study on UGT8 expression in tissue specimens of primary and corresponding metastatic lung tumors in 19 non-small cell lung carcinoma patients undergoing surgery. The majority of both lung primary and metastatic tumor tissues are positive in UGT8 signals. The cytoplasmic expression of UGT8 is found in 68.4% of cases of primary tumors and 82.2% of metastases, with a positive correlation between the UGT8 expression in both tumor tissues. The normal tissue adjacent to tumors shows no positive UGT8 staining. There is no appreciable difference in UGT8 expression depending on the clinical stage of non-small cell lung carcinoma or lymph node involvement found nor is there any association between UGT8 expression in tumor tissues and patients' survival time. UGT8, although enhanced in non-small cell lung carcinoma tissues, does not meet the criteria of a lung tumor marker
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
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Bosio, A.; Binczek, E.; Stoffel, W.
Molecular cloning and characterization of the mouse CGT gene encoding UDP-galactose ceramide-galactosyltransferase (cerebroside synthetase)
Genomics
35
223-226
1996
Homo sapiens, Mus musculus, Rattus norvegicus
Manually annotated by BRENDA team
Kapitonov, D.; Yu, R.K.
Cloning, characterization, and expression of human ceramide galactosyltransferase cDNA
Biochem. Biophys. Res. Commun.
232
449-453
1997
Gallus gallus, Homo sapiens
Manually annotated by BRENDA team
Bosio, A.; Binczek, E.; Le Beau, M.M.; Fernald, A.A.; Stoffel, W.
The human gene CGT encoding the UDP-galactose ceramide galactosyl transferase (cerebroside synthase): Cloning, characterization, and assignment to human chromosome 4, band q26
Genomics
34
69-75
1996
Homo sapiens
Manually annotated by BRENDA team
Tencomnao, T.; Yu, R.K.; Kapitonov, D.
Characterization of the human UDP-galactose:ceramide galactosyltransferase gene promoter
Biochim. Biophys. Acta
1517
416-423
2001
Homo sapiens
Manually annotated by BRENDA team
Rzechonek, A.; Cygan, M.; Blasiak, P.; Muszczynska-Bernhard, B.; Bobek, V.; Lubicz, M.; Adamiak, J.
Expression of ceramide calactosyltransferase (UGT8) in primary and metastatic lung tissues of non-small-cell lung cancer
Adv. Exp. Med. Biol.
952
51-58
2016
Homo sapiens (Q16880), Homo sapiens
Manually annotated by BRENDA team
Pannuzzo, G.; Graziano, A.C.; Pannuzzo, M.; Masman, M.F.; Avola, R.; Cardile, V.
Zoledronate derivatives as potential inhibitors of uridine diphosphate-galactose ceramide galactosyltransferase 8 A combined molecular docking and dynamic study
J. Neurosci. Res.
94
1318-1326
2016
Homo sapiens (Q16880), Homo sapiens
Manually annotated by BRENDA team