Information on EC 2.4.1.79 - globotriaosylceramide 3-beta-N-acetylgalactosaminyltransferase

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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria

EC NUMBER
COMMENTARY hide
2.4.1.79
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RECOMMENDED NAME
GeneOntology No.
globotriaosylceramide 3-beta-N-acetylgalactosaminyltransferase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
UDP-N-acetyl-alpha-D-galactosamine + alpha-D-galactosyl-(1->4)-beta-D-galactosyl-(1->4)-beta-D-glucosyl-(1<->1)-ceramide = UDP + N-acetyl-beta-D-galactosaminyl-(1->3)-alpha-D-galactosyl-(1->4)-beta-D-galactosyl-(1->4)-beta-D-glucosyl-(1<->1)-ceramide
show the reaction diagram
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-
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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
Glycosphingolipid biosynthesis - globo series
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Metabolic pathways
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SYSTEMATIC NAME
IUBMB Comments
UDP-N-acetyl-D-galactosamine:alpha-D-galactosyl-(1->4)-beta-D-galactosyl-(1->4)-beta-D-glucosyl-(1<->1)-ceramide III3-beta-N-acetyl-D-galactosaminyltransferase
Globoside is a neutral glycosphingolipid in human erythrocytes and has blood-group-P-antigen activity [4]. The enzyme requires a divalent cation for activity, with Mn2+ required for maximal activity [3]. UDP-GalNAc is the only sugar donor that is used efficiently by the enzyme: UDP-Gal and UDP-GlcNAc result in very low enzyme activity [3]. Lactosylceramide, globoside and gangliosides GM3 and GD3 are not substrates [4]. For explanation of the superscripted '3' in the systematic name, see {iupac/misc/glylp#5.3::GL-5.3.4}.
CAS REGISTRY NUMBER
COMMENTARY hide
62213-46-1
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83215-90-1
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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-
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Manually annotated by BRENDA team
strain Rd
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-
Manually annotated by BRENDA team
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SwissProt
Manually annotated by BRENDA team
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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-N-acetyl-D-galactosamine + D-galactosyl-1,4-D-galactosyl-1,4-D-glucosylceramide
UDP + N-acetyl-D-galactosaminyl-1,3-D-galactosyl-1,4-D-galactosyl-1,4-D-glucosylceramide
show the reaction diagram
UDP-N-acetyl-D-galactosamine + disialoganglioside GD3
UDP + ?
show the reaction diagram
-
-
-
-
?
UDP-N-acetyl-D-galactosamine + Galalpha1,3Galbeta1,4Glc
UDP + GalNAcbeta1,3-D-Galalpha1,3Galbeta1,4Glc
show the reaction diagram
-
-
-
-
?
UDP-N-acetyl-D-galactosamine + Galalpha1,3Galbeta1,4Glc-NHAc
UDP + GalNAcbeta1,3-D-Galalpha1,3Galbeta1,4Glc-NHAc
show the reaction diagram
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-
-
-
?
UDP-N-acetyl-D-galactosamine + Galalpha1,3Galbeta1,4Glc-OBn
UDP + GalNAcbeta1,3-D-Galalpha1,3Galbeta1,4Glc-OBn
show the reaction diagram
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-
-
-
?
UDP-N-acetyl-D-galactosamine + Galalpha1,3Galbeta1,4Glc-OMe
UDP + GalNAcbeta1,3-D-Galalpha1,3Galbeta1,4Glc-OMe
show the reaction diagram
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-
-
-
?
UDP-N-acetyl-D-galactosamine + Galalpha1,3Galbeta1,4Glc-SPh
UDP + GalNAcbeta1,3-D-Galalpha1,3Galbeta1,4Glc-SPh
show the reaction diagram
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-
-
-
?
UDP-N-acetyl-D-galactosamine + Galalpha1,3Galbeta1,4GlcNAc
UDP + GalNAcbeta1,3-D-Galalpha1,3Galbeta1,4GlcNAc
show the reaction diagram
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-
-
-
?
UDP-N-acetyl-D-galactosamine + Galalpha1,4Galbeta1,4Glc
UDP + GalNAcbeta1,3-D-Galalpha1,4Galbeta1,4Glc
show the reaction diagram
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-
-
-
?
UDP-N-acetyl-D-galactosamine + Galalpha1,4Galbeta1,4Glc-N3
UDP + GalNAcbeta1,3-D-Galalpha1,4Galbeta1,4Glc-N3
show the reaction diagram
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-
-
-
?
UDP-N-acetyl-D-galactosamine + Galalpha1,4Galbeta1,4Glc-OBn
UDP + GalNAcbeta1,3-D-Galalpha1,4Galbeta1,4Glc-OBn
show the reaction diagram
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-
-
-
?
UDP-N-acetyl-D-galactosamine + Galalpha1,4Galbeta1,4Glc-OMe
UDP + GalNAcbeta1,3-D-Galalpha1,4Galbeta1,4Glc-OMe
show the reaction diagram
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-
-
-
?
UDP-N-acetyl-D-galactosamine + Galalpha1,4Galbeta1,4Glc-SPh
UDP + GalNAcbeta1,3-D-Galalpha1,4Galbeta1,4Glc-SPh
show the reaction diagram
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-
-
-
?
UDP-N-acetyl-D-galactosamine + Galalpha1,4Galbeta1,4GlcNAc
UDP + GalNAcbeta1,3-D-Galalpha1,4Galbeta1,4GlcNAc
show the reaction diagram
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-
-
-
?
UDP-N-acetyl-D-galactosamine + globotriosylceramide
UDP + globotetraosylceramide
show the reaction diagram
UDP-N-acetyl-D-galactosamine + hematoside GM3
UDP + ?
show the reaction diagram
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equine erythrocyte hematoside
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?
additional information
?
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the enzyme catalyzes the conversion of human blood group Pk antigen into P antigen
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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-N-acetyl-D-galactosamine + D-galactosyl-1,4-D-galactosyl-1,4-D-glucosylceramide
UDP + N-acetyl-D-galactosaminyl-1,3-D-galactosyl-1,4-D-galactosyl-1,4-D-glucosylceramide
show the reaction diagram
UDP-N-acetyl-D-galactosamine + globotriosylceramide
UDP + globotetraosylceramide
show the reaction diagram
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glycosphingolipid metabolism
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-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Fe2+
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19% of the activation with Mn2+
Li+
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11% of the activation with Mn2+
Mg2+
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18% as effective as Mn2+ in activation
additional information
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Mg2+ cannot replace Mn2+
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
4-hydroxymercuribenzoate
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0.5 mM, complete inhibition
Globotetraosylceramide
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GSH
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2 mM, 17% inhibition
II3-alpha-N-Acetylneuraminyl-lactosylceramide
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iodoacetamide
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1 mM, 65% inhibition
iodoacetic acid
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1 mM, 91% inhibition
NaN3
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2 mM, 38% inhibition
NEM
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1 mM, 67% inhibition
Sodium deoxycholate
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UDP
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competitive to UDP-N-acetylgalactosamine, non-competitive to globotriaosylceramide
additional information
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no effect: lactosylceramide
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Detergents
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dithiothreitol
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10 mM, stimulation to 120% of the original activity
Myrj 59
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activation is half as effective as with taurocholate
Nonionic detergents
sodium taurocholate
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required for optimal activity
sodium taurodeoxycholate
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greatest activation, 1 mg/ml
Triton CF-54
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activates
Triton X100
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activates
Tween 20
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activation is half as effective as with taurocholate
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0025 - 1.7
D-galactosyl-1,4-D-galactosyl-1,4-D-glucosylceramide
0.42
globotriosylceramide
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0.14
UDP-N-acetyl-D-galactosamine
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0.2 - 0.23
UDP-N-acetylgalactosamine
0.014
UDP-N-acetylglucosamine
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4.5 - 8
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maximal activity in 2-(N-morpholino)ethanesulfonic acid
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.5 - 8
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about 50% of maximal activity at pH 5.5 and 8.0
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
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cultured hamster cells, NIL-8
Manually annotated by BRENDA team
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strong gene expression
Manually annotated by BRENDA team
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strong gene expression
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
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MW of the bifunctional beta(1,3)-N-acetylgalactosaminyltransferase/UDP-N-acetylglucosamine C4 epimerase fusion protein is 70000 Da
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
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the enzyme contains five potential N-linked glycosylation sites
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
diluted enzyme solutions, below 0.1 mg protein/ml, unstable
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Stable to repeated freeze-thawing
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-80°C, above 0.1 mg protein/ml in 25 mM sodium cacodylate buffer, pH 6.9, 1% Triton X-100 and 20% glycerol, stable for at least 3 months
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
one-step purification of the bifunctional beta(1->3) N-acetylgalactosaminyltransferase/UDP-N-acetylglucosamine C4 epimerase fusion protein
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
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preparation of a bifunctional beta(1->3) N-acetylgalactosaminyltransferase/UDP-N-acetylglucosamine C4 epimerase fusion protein by in-frame linking of the Plesiomonas shigelloides wbgU gene downstream to the Haemophilus influenzae lgtD gene through a five-residue peptide linker (Thr-Gly-Gly-Gly-Gly). The enzyme is expressed in Escherichia coli BL21 at a relatively high level
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
synthesis