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Information on EC 2.4.1.92 - (N-acetylneuraminyl)-galactosylglucosylceramide N-acetylgalactosaminyltransferase and Organism(s) Mus musculus and UniProt Accession Q09200
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2.4.1.92 (N-acetylneuraminyl)-galactosylglucosylceramide N-acetylgalactosaminyltransferaseIUBMB Comments
This enzyme catalyses the formation of the gangliosides (i.e. sialic-acid-containing glycosphingolipids) GM2, GD2 and SM2 from GM3, GD3 and SM3, respectively. Asialo-GM3 and lactosylceramide are also substrates, but glycoproteins and oligosaccharides are not substrates.
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Word Map
- 2.4.1.92
- glycosphingolipids
- gd3
-
sialic
- lactosylceramide
- glycosyltransferases
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sialyltransferase
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laccer
- udp-galnac
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a-series
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hst3gal
-
anti-gm3
-
infantile-onset
- synthesis
- medicine
The taxonomic range for the selected organisms is: Mus musculus
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Reaction Schemes
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Synonyms
gm3 synthase, gm2/gd2 synthase, gm2 synthase, gd2 synthase, gd2/gm2 synthase, beta1,4-n-acetylgalactosaminyltransferase, beta4galnacta, n-acetylgalactosaminyltransferase i, galgt1, st3gal v, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
acetylgalactosaminyltransferase
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acetylgalactosaminyltransferase, uridine diphosphoacetylgalactosamine-ganglioside GM3
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GalNAcT
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ganglioside GM2 synthase
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ganglioside GM3 acetylgalactosaminyltransferase
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GM2 synthase
GM2/GD2-synthase
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UDP acetylgalactosamine-(N-acetylneuraminyl)-D-galactosyl-D-glucosylceramide
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UDP-N-acetylgalactosamine GM3 N-acetylgalactosaminyltransferase
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UDP-N-acetylgalactosaminyltransferase I
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uridine diphosphoacetylgalactosamine-acetylneuraminylgalactosylglucosylceramide
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uridine diphosphoacetylgalactosamine-ganglioside GM3 acetylgalactosaminyltransferase
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uridine diphosphoacetylgalactosamine-hematoside acetylgalactosaminyltransferase
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GM2 synthase
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hexosyl group transfer
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SYSTEMATIC NAME
IUBMB Comments
UDP-N-acetyl-D-galactosamine:1-O-[O-(N-acetyl-alpha-neuraminosyl)-(2->3)-O-beta-D-galactopyranosyl-(1->4)-beta-D-glucopyranosyl]-ceramide 4-beta-N-acetyl-D-galactosaminyltransferase
This enzyme catalyses the formation of the gangliosides (i.e. sialic-acid-containing glycosphingolipids) GM2, GD2 and SM2 from GM3, GD3 and SM3, respectively. Asialo-GM3 [3] and lactosylceramide [2] are also substrates, but glycoproteins and oligosaccharides are not substrates.
CAS REGISTRY NUMBER
COMMENTARY
67338-98-1
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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-GalNAc + n-octyl-beta-D-glucopyranoside
UDP + GalNAcbeta(1-4)-glc-n-octyl
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?
UDP-N-acetyl-alpha-D-galactosamine + GD3(N-acetylneuraminic acid)-ganglioside
UDP + GD2(N-acetylneuraminic acid)-ganglioside
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-
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?
UDP-N-acetyl-alpha-D-galactosamine + GD3(N-glycolylneuraminic acid)-ganglioside
UDP + GD2(N-glycolylneuraminic acid)-ganglioside
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-
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?
UDP-N-acetyl-D-galactosamine + (N-acetylneuraminyl)-D-galactosyl-D-glucosylceramide
UDP + N-acetyl-D-galactosaminyl-(N-acetylneuraminyl)-D-galactosyl-D-glucosylceramide
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73%-78% as effective as GM3(N-glycolylneuraminic acid)
i.e. GM2(N-acetylneuraminic acid)-ganglioside
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UDP-N-acetyl-D-galactosamine + GD3-ganglioside
UDP + GD2-ganglioside
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GD3(N-glycolylneuraminic acid): 66% as effective as GM3(N-glycolylneuraminic acid), GD3(N-acetylneuraminic acid): 76% as effective as GM3(N-glycolylneuraminic acid)
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?
UDP-N-acetyl-D-galactosamine + GM3(N-acetylneuraminic acid)-ganglioside
UDP + GM2(N-acetylneuraminic acid)-ganglioside
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?
UDP-N-acetyl-D-galactosamine + GM3(N-glycolylneuraminic acid)-ganglioside
UDP + GM2(N-glycolylneuraminic acid)-ganglioside
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best substrate
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additional information
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no substrate: lactosylceramide, sialylparagloboside, GM1b(N-glycolylneuraminic acid), GD1a(N-acetylneuraminic acid), GT1b(N-acetylneuraminic acid), GQ1b(N-acetylneuraminic acid), GM1a(N-acetylneuraminic acid), GD1b(N-acetylneuraminic acid), globoside
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?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
alpha-L-iduronidase (IDUA) knockout mutant variant, gene B4GALNT1
SwissProt
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
additional information
ganglioside profile analyses in brain tissues, overview. Tissue dependent ganglioside alteration in IDUA KO mice with a total ganglioside increase in cortex and cerebellum, and a selective presence of GM3, GM2 and GD3 gangliosides in the hippocampus and hypothalamus. Evaluation of gene expression of ganglioside synthesis (GM3, GD3 and GM2/GD2 synthases) and degradation of (neuraminidase1) enzymes in the cerebellum and hippocampus by RT-sq-PCR. Percentage distribution of gangliosides in wild-type and IDUA knockout mice, overview
additional information
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ganglioside profile analyses in brain tissues, overview. Tissue dependent ganglioside alteration in IDUA KO mice with a total ganglioside increase in cortex and cerebellum, and a selective presence of GM3, GM2 and GD3 gangliosides in the hippocampus and hypothalamus. Evaluation of gene expression of ganglioside synthesis (GM3, GD3 and GM2/GD2 synthases) and degradation of (neuraminidase1) enzymes in the cerebellum and hippocampus by RT-sq-PCR. Percentage distribution of gangliosides in wild-type and IDUA knockout mice, overview
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
alpha-L-iduronidase knockout mutant, IDUA KO, mice show reduced expression of GD3 and GM2/GD2 synthases and neuraminidase1 in cerebellum, and a decrease in GM2/GD2 synthase and neuraminidase 1 in the hippocampus. The observed ganglioside changes result from a combined effect of glycosaminoglycans on ganglioside biosynthesis and degradation. C57Bl/6 knockout mice deficient for alpha-L-iduronidase (IDUA-KO) represent a murine model for human mucopolysaccharidosis type I, MPS I, an autosomal recessive disease caused by a genetic defect that codifies a lysosomal hydrolase, alpha-L-iduronidase, IDUA, EC. 3.2.1.76
metabolism
the enzyme is responsible for the biosynthesis of GM2 and GD2 gangliosides, biosynthesis and degradation pathways of a- and b-series gangliosides, overview
malfunction
malfunction
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genes of complement components (C1qalpha, C1qbeta, C1qgamma, C4 and C3aR) are up-regulated in the cerebellum of mice with combined knockout of GM2/GD2 synthase and GD3 synthase
malfunction
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in animals lacking either GM2/GD2 or GM3 synthase, tissue cholesterol concentrations and synthesis rates are normal in nearly all organs, and whole-animal sterol pools and turnover also are not different from control animals. Mice lacking both synthases, however, have small elevations in cholesterol concentrations in several organs, and the whole-animal cholesterol pool is marginally elevated. When either the GM2/GD2 or GM3 synthase activity is deleted in mice lacking Niemann-Pick type C function, the clinical phenotype is not changed, but lifespan is shortened.
malfunction
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GM3 synthase/GM2 synthase double knock out cells evidence significantly impaired tumor growth in syngeneic immunocompetent mice
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). B4GN1_MOUSE
533
1
59212
Swiss-Prot
Secretory Pathway (Reliability: 2)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
palmitoylation
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beta4GalNAcT-I is S-acylated at conserved cysteine residues located close to the cytoplasmic border of the trans-membrane domains, and palmitoylation takes place in the endoplasmic reticulum. Cysteine residues that are the target of S-acylation on beta4GalNAcT-I are involved in the formation of homodimers through disulfide bonds
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
overexpression of gene leads to shift of ganglioside components from b-series to a-series
additional information
comparisons of relative expressions of ganglioside metabolism genes in wild-type and IDUA knockout mice, overview
additional information
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comparisons of relative expressions of ganglioside metabolism genes in wild-type and IDUA knockout mice, overview
additional information
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fusion protein with green, red or yellow fluorescent protein, localization to ER and Golgi, probably forms complex with sialyl-transferase II
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
4°C, purified enzyme, at least 6 days in 20% v/v glycerol, 1% w/v heptylthioglucoside, 1 M sucrose, 0.2 M NaCl and 1 mM EDTA in 0.03 M cacodylate buffer, pH 6.9
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene B4GALNT1, semi-quantitative PCR enzyme expression analysis in brain tissues in wild-type and IDUA knockout mice
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
synthesis
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expression of enzyme both as complete membrane-bound enzyme and as a soluble form in the baculovirus insect cell expression system
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Hashimoto, Y.; Sekine, M.; Iwasaki, K.; Suzuki, A.
Purification and characterization of UDP-N-acetylgalactosamine GM3/GD3 N-acetylgalactosaminyltransferase from mouse liver
J. Biol. Chem.
268
25857-25864
1993
Mus musculus
Bieberich, E.; MacKinnon, S.; Silva, J.; Li, D.D.; Tencomnao, T.; Irwin, L.; Kapitonov, D.; Yu, R.K.
Regulation of ganglioside biosynthesis by enzyme complex formation of glycosyltransferases
Biochemistry
41
11479-11487
2002
Mus musculus
Furukawa, K.; Takamiya, K.; Furukawa, K.
beta1,4-N-acetylgalactosaminyltransferase-GM2/GD2 synthase: a key enzyme to control the synthesis of brain-enriched complex gangliosides
Biochim. Biophys. Acta
1573
356-362
2002
Homo sapiens (Q00973), Mus musculus (Q09200)
Wendeler, M.; Reilaender, H.; Hoernschemeyer, J.; Schwarzmann, G.; Kolter, T.; Sandhoff, K.
Recombinant ganglioside GM2 synthase-expression in insect cells and enzyme assay
Methods Enzymol.
363
476-489
2003
Mus musculus
Furukawa, K.; Aixinjueluo, W.; Kasama, T.; Ohkawa, Y.; Yoshihara, M.; Ohmi, Y.; Tajima, O.; Suzumura, A.; Kittaka, D.; Furukawa, K.
Disruption of GM2/GD2 synthase gene resulted in overt expression of 9-O-acetyl GD3 irrespective of Tis21
J. Neurochem.
105
1057-1066
2008
Mus musculus (Q09200), Mus musculus
Li, H.; Turley, S.D.; Liu, B.; Repa, J.J.; Dietschy, J.M.
GM2/GD2 and GM3 gangliosides have no effect on cellular cholesterol pools or turnover in normal or NPC1 mice
J. Lipid Res.
49
1816-1828
2008
Mus musculus
Ohmi, Y.; Tajima, O.; Ohkawa, Y.; Mori, A.; Sugiura, Y.; Furukawa, K.; Furukawa, K.
Gangliosides play pivotal roles in the regulation of complement systems and in the maintenance of integrity in nerve tissues
Proc. Natl. Acad. Sci. USA
106
22405-22410
2009
Mus musculus
Suzuki, Y.; Yanagisawa, M.; Ariga, T.; Yu, R.K.
Histone acetylation-mediated glycosyltransferase gene regulation in mouse brain during development
J. Neurochem.
116
874-880
2011
Mus musculus
Liu, Y.; Yan, S.; Wondimu, A.; Bob, D.; Weiss, M.; Sliwinski, K.; Villar, J.; Notario, V.; Sutherland, M.; Colberg-Poley, A.M.; Ladisch, S.
Ganglioside synthase knockout in oncogene-transformed fibroblasts depletes gangliosides and impairs tumor growth
Oncogene
29
3297-3306
2010
Mus musculus
Kreutz, F.; dos Santos Petry, F.; Camassola, M.; Schein, V.; Guma, F.C.; Nardi, N.B.; Trindade, V.M.
Alterations of membrane lipids and in gene expression of ganglioside metabolism in different brain structures in a mouse model of mucopolysaccharidosis type I (MPS I)
Gene
527
109-114
2013
Mus musculus (Q09200), Mus musculus, Mus musculus C57BL/6 (Q09200)
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