Information on EC 2.4.99.2 - beta-D-galactosyl-(1->3)-N-acetyl-beta-D-galactosaminide alpha-2,3-sialyltransferase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
2.4.99.2
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RECOMMENDED NAME
GeneOntology No.
beta-D-galactosyl-(1->3)-N-acetyl-beta-D-galactosaminide alpha-2,3-sialyltransferase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
CMP-N-acetyl-beta-neuraminate + a beta-D-galactosyl-(1->3)-N-acetyl-beta-D-galactosaminyl-R = CMP + an N-acetyl-alpha-neuraminyl-(2->3)-beta-D-galactosyl-(1->3)-N-acetyl-beta-D-galactosaminyl-R
show the reaction diagram
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
glycosyl group transfer
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
ABH and Lewis epitopes biosynthesis from type 1 precursor disaccharide
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ganglio-series glycosphingolipids biosynthesis
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SYSTEMATIC NAME
IUBMB Comments
CMP-N-acetyl-beta-neuraminate:a beta-D-galactosyl-(1->3)-N-acetyl-beta-D-galactosaminyl-R alpha-(2->3)-N-acetylneuraminyltransferase (configuration-inverting)
The enzyme recognizes the sequence beta-D-galactosyl-(1->3)-N-acetyl-D-galactosaminyl (known as type 1 histo-blood group precursor disaccharide) in non-reducing termini of glycan moieties in glycoproteins and glycolipids [1]. When acting on gangloside GM1a, it forms gangloside GD1a [2].
CAS REGISTRY NUMBER
COMMENTARY hide
60202-12-2
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
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UniProt
Manually annotated by BRENDA team
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SwissProt
Manually annotated by BRENDA team
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Manually annotated by BRENDA team
Sprague-Dawley strain
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Manually annotated by BRENDA team
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UniProt
Manually annotated by BRENDA team
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A8R0Y0
UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
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scenario of the evolutionary relationships of st3gal genes coupled to a conceptual framework of the evolution of ST3Gal functions; scenario of the evolutionary relationships of st3gal genes coupled to a conceptual framework of the evolution of ST3Gal functions; scenario of the evolutionary relationships of st3gal genes coupled to a conceptual framework of the evolution of ST3Gal functions; scenario of the evolutionary relationships of st3gal genes coupled to a conceptual framework of the evolution of ST3Gal functions
metabolism
physiological function
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the enzyme is involved in pancreatic tumor progression processes
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
CMP-N-acetyl-beta-neuraminate + 2-azidoethyl beta-D-Gal-(1->3)-beta-D-GalNAc
CMP + 2-azidoethyl alpha-Neu5Ac-(2->3)-beta-D-Gal-(1->3)-beta-D-GalNAc
show the reaction diagram
CMP-N-acetyl-beta-neuraminate + 3-O-[beta-D-Gal-(1->3)-beta-D-GalNAc]-N-acetyl-L-tyrosine methyl ester
CMP + 3-O-[alpha-Neu5Ac-(2->3)-beta-D-Gal-(1->3)-beta-D-GalNAc]-N-acetyl-L-tyrosine methyl ester
show the reaction diagram
CMP-N-acetyl-beta-neuraminate + allyl beta-D-Gal-(1->3)-beta-D-GalNAc
CMP + allyl alpha-Neu5Ac-(2->3)-beta-D-Gal-(1->3)-beta-D-GalNAc
show the reaction diagram
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24.1% of the activity compared to allylbeta-D-Gal-(1->4)-beta-D-GlcNAc, alpha2,3(N) sialyltransferase. 112% of the activity compared to benzyl beta-D-(3-O-Me)Gal-(1->4)-beta-D-GlcNAc-(1->6)-[beta-D-Gal-(1->3)]-alpha-D-GalNAc, alpha2,3(O) sialyltransferase
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?
CMP-N-acetyl-beta-neuraminate + allylbeta-D-Gal-(1->3)-beta-D-GlcNAc
CMP + allyl alpha-Neu5Ac-(2->3)-beta-D-Gal-(1->3)-beta-D-GlcNAc
show the reaction diagram
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123.1% of the activity compared to allylbeta-D-Gal-(1->4)-beta-D-GlcNAc, alpha2,3(N) sialyltransferase. 42.1% of the activity compared to benzyl beta-D-(3-O-Me)Gal-(1->4)-beta-D-GlcNAc-(1->6)-[beta-D-Gal-(1->3)]-alpha-D-GalNAc, alpha2,3(O) sialyltransferase
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?
CMP-N-acetyl-beta-neuraminate + benzyl beta-D-Gal-(1->3)-beta-D-GalNAc
CMP + benzyl alpha-Neu5Ac-(2->3)-beta-D-Gal-(1->3)-beta-D-GalNAc
show the reaction diagram
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?
CMP-N-acetyl-beta-neuraminate + beta-D-(2-O-Me)Gal-(1->3)-beta-D-GlcNAc
CMP + alpha-Neu5Ac-(2->3)-beta-D-(2-O-Me)Gal-(1->3)-beta-D-GlcNAc
show the reaction diagram
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115.3% of the activity compared to allylbeta-D-Gal-(1->4)-beta-D-GlcNAc, alpha2,3(N) sialyltransferase. 2.9% of the activity compared to benzyl beta-D-(3-O-Me)Gal-(1->4)-beta-D-GlcNAc-(1->6)-[beta-D-Gal-(1->3)]-alpha-D-GalNAc, alpha2,3(O) sialyltransferase
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?
CMP-N-acetyl-beta-neuraminate + beta-D-Gal-(1->3)-beta-D-GalNAc
CMP + alpha-Neu5Ac-(2->3)-beta-D-Gal-(1->3)-beta-D-GalNAc
show the reaction diagram
CMP-N-acetyl-beta-neuraminate + beta-D-Gal-(1->3)-beta-D-GlcNAc
CMP + alpha-Neu5Ac-(2->3)-beta-D-Gal-(1->3)-beta-D-GlcNAc
show the reaction diagram
CMP-N-acetyl-beta-neuraminate + beta-D-Gal-(1->3)-beta-D-GlcNAc
CMP + alpha-Neu5Ac-(2->3)-beta-D-Glc-(1->3)-beta-D-GalNAc
show the reaction diagram
relative Vmax is 2:5:1 for beta-D-Gal-(1->3)-beta-D-GlcNAc, beta-D-Gal-(1->4)-beta-D-GlcNAc and beta-D-Gal-(1->3)-beta-D-GalNAc, respectively
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?
CMP-N-acetyl-beta-neuraminate + beta-Gal-(1->4)-beta-GlcNAc-R
CMP + alphaNeuAc-(2->3)-beta-Gal-(1->4)-beta-GlcNA-R
show the reaction diagram
ST3Gal IV overexpressed in the gastric MKN45 cell line, shows exclusive enzymatic activity towards glycoproteins containing terminal beta-Gal-(1->4)-beta-GlcNAc structure
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?
CMP-N-acetyl-beta-neuraminate + ganglioside GA1
CMP + ganglioside GM1b
show the reaction diagram
CMP-N-acetyl-beta-neuraminate + ganglioside Gb5
CMP + ganglioside MSGb5
show the reaction diagram
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i.e. beta-D-Gal-(1_>3)-beta-D-GalNAc-(1-3)-alpha-D-Gal-(1->4)-beta-D-Gal-(1->4)-beta-D-Glc
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?
CMP-N-acetyl-beta-neuraminate + ganglioside GD1b
CMP + ganglioside GT1b
show the reaction diagram
CMP-N-acetyl-beta-neuraminate + ganglioside GM1a
CMP + ganglioside GD1a
show the reaction diagram
CMP-N-acetyl-beta-neuraminate + methyl beta-D-(3-O-sulfo)Gal-(1->3)-beta-D-GalNAc-(1->3)-alpha-D-Gal
CMP + methyl alpha-Neu5Ac-(2->3)-beta-D-(3-O-sulfo)Gal-(1->3)-beta-D-GalNAc-(1->3)-alpha-D-Gal
show the reaction diagram
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?
CMP-N-acetyl-beta-neuraminate + methyl beta-D-Gal-(1->3)-beta-D-GalNAc-(1->3)-alpha-D-Gal
CMP + methyl alpha-Neu5Ac-(2->3)-beta-D-Gal-(1->3)-beta-D-GalNAc-(1->3)-alpha-D-Gal
show the reaction diagram
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106.8% of the activity compared to allylbeta-D-Gal-(1->4)-beta-D-GlcNAc, alpha2,3(N) sialyltransferase. 120.8% of the activity compared to benzyl beta-D-(3-O-Me)Gal-(1->4)-beta-D-GlcNAc-(1->6)-[beta-D-Gal-(1->3)]-alpha-D-GalNAc, alpha2,3(O) sialyltransferase
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?
CMP-N-acetyl-beta-neuraminate + [asialofetuin]-(O-3-(beta-D-Gal-(1->3)-beta-D-GalNAc-(1->)))-L-serine
CMP + [protein]-(O-3-(alpha-Neu5Ac-(2->3)-beta-D-Gal-(1->3)-beta-D-GalNAc-(1->)))-L-serine
show the reaction diagram
CMP-N-acetyl-beta-neuraminate + [asialofetuin]-(O-3-(beta-D-Gal-(1->3)-beta-D-GalNAc-(1->)))-L-threonine
CMP + [protein]-(O-3-(alpha-Neu5Ac-(2->3)-beta-D-Gal-(1->3)-beta-D-GalNAc-(1->)))-L-threonine
show the reaction diagram
CMP-N-acetylneuraminate + beta-D-Gal-(1->3)-beta-D-GalNAc-R
CMP + alpha-Neu5Ac-(2->3)-beta-D-Gal-(1->3)-beta-D-GalNAc-R
show the reaction diagram
broad substrate specificity, the viral enzyme utilizes disaccharides type I-III and also fucosylated Lewis a and Lewis x
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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
CMP-N-acetyl-beta-neuraminate + ganglioside GM1a
CMP + ganglioside GD1a
show the reaction diagram
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?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
NaCl
A8R0Y0;
in presence of 500-700 mM NaCl 2fold increase in activity
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Ba2+
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10 mM BaCl2, 12% inhibition
beta-D-Gal-(1->3)-beta-D-GalNAc
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the enzyme exhibits competitive inhibition between all kinds of acceptors; the enzyme exhibits noncompetitive inhibition between ganglioside GA1 and beta-D-Gal-(1->3)-beta-D-GalNAc or between ganglioside GA1 and [asialofeuin]-(O-3-(alpha-Neu5Ac-(2->3)-beta-D-Gal-(1->3)-alpha-D-GalNAc-(1->)))-L-serine
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Ca2+
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10 mM CaCl2, 39% inhibition
Cd2+
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10 mM CdCl2, 85% inhibition
CMP-N-acetylneuraminate
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above 0.2 M
Co2+
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10 mM CoCl2, 44% inhibition
Cu2+
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10 mM CuCl2, complete inhibition
ganglioside GA1
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the enzyme exhibits competitive inhibition between all kinds of acceptors; the enzyme exhibits noncompetitive inhibition between ganglioside GA1 and beta-D-Gal-(1->3)-beta-D-GalNAc or between ganglioside GA1 and [asialofeuin]-(O-3-(alpha-Neu5Ac-(2->3)-beta-D-Gal-(1->3)-alpha-D-GalNAc-(1->)))-L-serine
ganglioside GM3
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in the presence of Triton CF-54
lactosylceramide
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inhibits reaction with GM1a
Ni2+
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10 mM NiCl2, 75% inhibition
Zn2+
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10 mM ZnCl2, 10% inhibition
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Triton CF-54
Triton X-100
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.018 - 3
beta-D-Gal-(1->3)-beta-D-GalNAc
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0.75 - 3.2
beta-D-Gal-(1->3)-beta-D-GlcNAc
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0.0137 - 0.5
CMP-N-acetyl-beta-neuraminate
0.065
CMP-N-acetylneuraminate
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pH 6.5, 37°C
0.46 - 1.25
ganglioside GA1
0.000196 - 0.15
ganglioside GD1b
0.000538 - 1.5
ganglioside GM1a
1.25
methyl beta-D-(3-O-sulfo)Gal-(1->3)-beta-D-GalNAc-(1->3)-alpha-D-Gal
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pH 6.0, 37°C, alpha2,3(O) sialyltransferase
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0.12
methyl beta-D-Gal-(1->3)-beta-D-GalNAc-(1->3)-alpha-D-Gal
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pH 6.0, 37°C, alpha2,3(O) sialyltransferase
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75
naphthoquinol
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pH 6.5, 37°C
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
additional information
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.00000186
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0.0000033
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.5
A8R0Y0;
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5 - 9
A8R0Y0;
pH 5: about 40% of maximal activity, pH 9: about 60% of maximal actzivity
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
20
A8R0Y0;
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30
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assay
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
10 - 30
A8R0Y0;
10°C: 65% of maximal activity, 30°C: 80% of maximal activity
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
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type 2 mRNA isoform, type 1 mRNA isoform is not detected
Manually annotated by BRENDA team
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high expression
Manually annotated by BRENDA team
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type 2 mRNA isoform, type 1 mRNA isoform is not detected
Manually annotated by BRENDA team
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granule cell layers; high expression; high expression
Manually annotated by BRENDA team
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type 2 mRNA isoform, type 1 mRNA isoform is not detected
Manually annotated by BRENDA team
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high expression
Manually annotated by BRENDA team
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ST3Gal IV overexpressing pancreatic adenocarcinoma cell lines
Manually annotated by BRENDA team
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gastric carcinoma cell line; gastric carcinoma cell line
Manually annotated by BRENDA team
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granule cell layers; high expression; high expression
Manually annotated by BRENDA team
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type 1 and type 2 mRNA isoform (differ in 5'-untranslated region)
Manually annotated by BRENDA team
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type 1 and type 2 mRNA isoform (differ in 5'-untranslated region)
Manually annotated by BRENDA team
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type 1 and type 2 mRNA isoform (differ in 5'-untranslated region)
Manually annotated by BRENDA team
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type 1 and type 2 mRNA isoform (differ in 5'-untranslated region)
Manually annotated by BRENDA team
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high expression
Manually annotated by BRENDA team
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type 1 and type 2 mRNA isoform (differ in 5'-untranslated region)
Manually annotated by BRENDA team
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constitutive expression level of ST3Gal II in prostate cancer cells and normal prostate epithelium; constitutive expression level of ST3Gal I in prostate cancer cells and normal prostate epithelium
Manually annotated by BRENDA team
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a high level of ST3Gal II mRNA was detected in all human RCC cell lines except SMKT-R2
Manually annotated by BRENDA team
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strong expression; weakly expressed
Manually annotated by BRENDA team
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CD4, absent in native cells, rapidly up-regulated upon activation
Manually annotated by BRENDA team
additional information
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not expressed in brain and kidney
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
43921
A8R0Y0;
MALDI-TOF of truncated enzyme with N-terminal Lys2 to Cys22 deletion
44000
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x * 44000, SDS-PAGE
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
glycoprotein
phosphoprotein
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
56
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t1/2: 60 s
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, 3 months, retains full activity
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
recombinant enzyme
recombinant truncated enzyme
A8R0Y0;
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
a soluble form of hST3Gal II is expressed in COS-7 cells; expressed in COS-7 cells
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expressed in 293FT cells; expressed in 293FT cells; expressed in 293FT cells
expressed in COS-7 cells as a recombinant enzyme fused with protein A; expressed in COS-7 cells as a recombinant enzyme fused with protein A; expressed in COS-7 cells as a recombinant enzyme fused with protein A; expressed in COS-7 cells as a recombinant enzyme fused with protein A
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expressed in HEK-293 cells
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expression in CHO-K1 cells of truncated protein-A-His-tagged enzyme
expression in COS cells
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expression in COS-7 cell line of various constructs deleted in the N-terminal portion of the protein sequence. The souble forms of the protein consisting of amino acids 26-340, hST3-DELTA25, and amino acids 57-340, hST3-DELTA56, are efficiently secreted and active. Further deletion of the N-terminal region gives also rise to various polypeptides that are not active within the transfected cells and not secreted in the culture medium
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expression in Escherichia coli, N-terminally truncated form
A8R0Y0;
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
among the five mammalian homologs of the NF-jB family, RelB RNAi most effectively inhibits the expression of ST3Gal I; among the five mammalian homologs of the NF-jB family, RelB RNAi most effectively inhibits the expression of ST3Gal II
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expression of ST3Gal II is mildly induced by phorbol-12-myristate-13-acetate. The expression of both ST3Gal II reaches to the peak within 12 h. phorbol-12-myristate-13-acetate-induced ST3Gal II expression is inhibited by NF-kappaB decoy oligodeoxynucleotides but not by AP-1 decoy oligodeoxynucleotides; expression of ST3Gal I is mildly induced by phorbol-12-myristate-13-acetate. The expression of both ST3Gal I reaches to the peak within 12 h. phorbol-12-myristate-13-acetate-induced ST3Gal I expression is inhibited by NF-kappaB decoy oligodeoxynucleotides but not by AP-1 decoy oligodeoxynucleotides
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highly expressed in most pancreatic adenocarcinoma tissues
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induction of COX-2 in the MDAMB-231 breast cancer cell line results in the increased expression of ST3Gal-I, leading to increased sialylation of the substrate of ST3Gal-I; PGE2, one of the final products of the cyclooxygenase-2 (COX-2) pathway, can induce the mRNA expression of the sialyltransferase ST3Gal-I, resulting in increased sialyltransferase activity
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its increased expression level is closely related to renal carcinogenesis
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the number of ST3Gal IV-expressing neurons in the anterior thalamic nuclei increases from 2% to 21% in a time-dependent manner during epileptogenesis
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tumour necrosis factor induces the expression of the sialyltransferase ST3Gal IV in human bronchial mucosa via MSK1/2 protein kinases
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