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Enzyme Nomenclature
Information on EC 2.4.99.4 - beta-galactoside alpha-2,3-sialyltransferase
for references in articles please use BRENDA:EC2.4.99.4
Word Map on EC 2.4.99.4
- 2.4.99.4
-
sialylation
- st6gal
-
o-glycans
- alpha-2,6-sialyltransferase
-
st6galnac
-
st8sia
-
2.4.99.1
- alpha-1,3-fucosyltransferase
-
cmp-n-acetylneuraminic
- synthesis
- drug development
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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
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EC NUMBER 
COMMENTARY 
2.4.99.4
-
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RECOMMENDED NAME
GeneOntology No.
beta-galactoside alpha-2,3-sialyltransferase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
CMP-N-acetylneuraminate + beta-D-galactosyl-(1->3)-N-acetyl-alpha-D-galactosaminyl-R = CMP + alpha-N-acetylneuraminyl-(2->3)-beta-D-galactosyl-(1->3)-N-acetyl-alpha-D-galactosaminyl-R
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
glycosyl group transfer
-
-
-
-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
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SYSTEMATIC NAME
IUBMB Comments
CMP-N-acetylneuraminate:beta-D-galactoside alpha-(2->3)-N-acetylneuraminyl-transferase
The acceptor is Galbeta1,3GalNAc-R, where R is H, a threonine or serine residue in a glycoprotein, or a glycolipid. Lactose can also act as acceptor. May be identical with EC 2.4.99.2 monosialoganglioside sialyltransferase.
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CAS REGISTRY NUMBER
COMMENTARY
71124-51-1
-
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
metabolism
physiological function
metabolism
-
the enzyme is involved in biosynthesis of O-linked oligosaccharide chains of glycoproteins
metabolism
-
the enzyme specifically modifies glycoproteins and glycolipids which contain the sequence beta-D-Gal-(1->3)-beta-D-GalNAc to form the sequence alpha-Neu5Ac-(2->3)-beta-D-Gal-(1->3)-beta-D-GalNAc
physiological function
-
ST3Gal III overexpression inhibits Taxol-triggered caspase-8 activation. ST3Gal III upregulation produces cellular resistance to taxol and hence reduces the efficacy of taxol therapy
physiological function
-
the enzyme modulates pancreatic cancer cell motility and adhesion in vitro and enhances its metastatic potential in vivo. Isoform ST3Gal III increases de novo expression of SLex by enzymatic competition, enhances pancreatic adenocarcinoma cells adhesion to rh-E-selectin, and increases tumour cell adhesion to HSE cells
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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
CMP + 3-O-[alpha-Neu5Ac-(2->3)-beta-D-Gal-(1->3)-alpha-D-GalNAc]-L-tyrosyl-[protein]
CMP-N-acetyl-beta-neuraminate + 3-O-[beta-D-Gal-(1->3)-alpha-D-GalNAc]-L-tyrosyl-[protein]
the enzyme synthesizes CMP-NeuAc by transferring NeuAc from the alpha-Neu5Ac-(2->3)-beta-D-Gal-(1->3)-alpha-D-GalNAc-unit of O-glycans
-
-
r
CMP-N-acetyl-beta-neuraminate + benzyl beta-D-Gal-(1->3)-alpha-D-GalNAc
CMP + benzyl alpha-Neu5Ac-(2->3)-beta-D-Gal-(1->3)-alpha-D-GalNAc
-
-
-
-
?
CMP-N-acetyl-beta-neuraminate + octyl beta-D-Gal-(1->3)-alpha-D-GalNAc
CMP + octyl alpha-Neu5Ac-(2->3)-beta-D-Gal-(1->3)-alpha-D-GalNAc
-
-
-
-
?
CMP-N-acetyl-beta-neuraminate + [antifreeze glycoprotein]-(O-3-(beta-D-Gal-(1->3)-alpha-D-GalNAc-(1->)))-L-serine
CMP + [antifreeze glycoprotein]-(O-3-(alpha-Neu5Ac-(2->3)-beta-D-Gal-(1->3)-alpha-D-GalNAc-(1->)))-L-serine
-
the enzyme specifically modifies glycoproteins and glycolipids which contain the sequence beta-D-Gal-(1->3)-beta-D-GalNAc to form the sequence alpha-Neu5Ac-(2->3)-beta-D-Gal-(1->3)-beta-D-GalNAc
-
-
?
CMP-N-acetyl-beta-neuraminate + [antifreeze glycoprotein]-(O-3-(beta-D-Gal-(1->3)-alpha-D-GalNAc-(1->)))-L-threonine
CMP + [antifreeze glycoprotein]-(O-3-(alpha-Neu5Ac-(2->3)-beta-D-Gal-(1->3)-alpha-D-GalNAc-(1->)))-L-threonine
CMP-N-acetyl-beta-neuraminate + [asialoglycoprotein]-(O-3-(beta-D-Gal-(1->3)-alpha-D-GalNAc-(1->)))-L-serine
CMP + [asialoglycoprotein]-(O-3-(alpha-Neu5Ac-(2->3)-beta-D-Gal-(1->3)-alpha-D-GalNAc-(1->)))-L-serine
-
-
-
-
?
CMP-N-acetyl-beta-neuraminate + [asialoglycoprotein]-(O-3-(beta-D-Gal-(1->3)-alpha-D-GalNAc-(1->)))-L-threonine
CMP + [asialoglycoprotein]-(O-3-(alpha-Neu5Ac-(2->3)-beta-D-Gal-(1->3)-alpha-D-GalNAc-(1->)))-L-threonine
-
the enzyme specifically modifies glycoproteins and glycolipids which contain the sequence beta-D-Gal-(1->3)-beta-D-GalNAc to form the sequence alpha-Neu5Ac-(2->3)-beta-D-Gal-(1->3)-beta-D-GalNAc
-
-
?
CMP-N-acetyl-beta-neuraminate + [porcine submaxillary asialo-mucin]-(O-3-(beta-D-Gal-(1->3)-alpha-D-GalNAc-(1->)))-L-serine
CMP + [porcine submaxillary asialo-mucin]-(O-3-(alpha-Neu5Ac-(2->3)-beta-D-Gal-(1->3)-alpha-D-GalNAc-(1->)))-L-serine
-
-
-
?
CMP-N-acetyl-beta-neuraminate + [porcine submaxillary asialo-mucin]-(O-3-(beta-D-Gal-(1->3)-alpha-D-GalNAc-(1->)))-L-threonine
CMP + [porcine submaxillary asialo-mucin]-(O-3-(alpha-Neu5Ac-(2->3)-beta-D-Gal-(1->3)-alpha-D-GalNAc-(1->)))-L-threonine
-
-
-
?
CMP-N-acetylneuraminate + 4-methylumbelliferyl 4-O-beta-D-galactosyl-beta-D-glucoside
CMP + 4-methylumbelliferyl alpha-N-acetylneuraminyl-(2->3)-beta-D-galactosyl-(1->4)-beta-D-glucoside
-
best substrate, about 37% conversion
-
-
-
CMP-N-acetylneuraminate + 4-nitrophenyl beta-D-Gal-(1->3)-alpha-D-GalNAc
CMP + 4-nitrophenyl alpha-Neu5Ac-(2->3)-beta-D-Gal-(1->3)-alpha-D-GalNAc
-
-
-
-
?
CMP-N-acetylneuraminate + beta-D-Gal-(1->3)-beta-D-GalNAc
CMP + alpha-Neu5Ac-(2->3)-beta-D-Gal-(1->3)-beta-D-GalNAc
-
best acceptor substrate
-
-
?
CMP-N-acetylneuraminate + beta-D-galactosyl-(1->3)-N-acetyl-alpha-D-galactosaminyl-R
CMP + alpha-N-acetylneuraminyl-(2->3)-beta-D-galactosyl-(1->3)-N-acetyl-alpha-D-galactosaminyl-R
-
the enzyme is involved in O-linked glycosylation pathway for synthesis of core 1 and core 2 oligosaccharides
-
-
?
CMP-N-acetylneuraminate + lactose
CMP + NeuAcalpha(2->3)Galbeta(1->4)Glc
-
-
-
-
?
additional information
?
-
-
with glycoprotein and ganglioside acceptors the substrate specificity is strict, with the sequence beta-D-Gal-(1->3)-alpha-D-GalNAc serving as the exclusive acceptor. The enzyme has an equilibrium random order mechanism
-
-
-
CMP-N-acetyl-beta-neuraminate + [antifreeze glycoprotein]-(O-3-(beta-D-Gal-(1->3)-alpha-D-GalNAc-(1->)))-L-threonine
CMP + [antifreeze glycoprotein]-(O-3-(alpha-Neu5Ac-(2->3)-beta-D-Gal-(1->3)-alpha-D-GalNAc-(1->)))-L-threonine
-
-
-
-
?
CMP-N-acetyl-beta-neuraminate + [antifreeze glycoprotein]-(O-3-(beta-D-Gal-(1->3)-alpha-D-GalNAc-(1->)))-L-threonine
CMP + [antifreeze glycoprotein]-(O-3-(alpha-Neu5Ac-(2->3)-beta-D-Gal-(1->3)-alpha-D-GalNAc-(1->)))-L-threonine
-
the enzyme specifically modifies glycoproteins and glycolipids which contain the sequence beta-D-Gal-(1->3)-beta-D-GalNAc to form the sequence alpha-Neu5Ac-(2->3)-beta-D-Gal-(1->3)-beta-D-GalNAc
-
-
?
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NATURAL SUBSTRATES
NATURAL PRODUCTS
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
CMP-N-acetyl-beta-neuraminate + [antifreeze glycoprotein]-(O-3-(beta-D-Gal-(1->3)-alpha-D-GalNAc-(1->)))-L-serine
CMP + [antifreeze glycoprotein]-(O-3-(alpha-Neu5Ac-(2->3)-beta-D-Gal-(1->3)-alpha-D-GalNAc-(1->)))-L-serine
-
the enzyme specifically modifies glycoproteins and glycolipids which contain the sequence beta-D-Gal-(1->3)-beta-D-GalNAc to form the sequence alpha-Neu5Ac-(2->3)-beta-D-Gal-(1->3)-beta-D-GalNAc
-
-
?
CMP-N-acetyl-beta-neuraminate + [antifreeze glycoprotein]-(O-3-(beta-D-Gal-(1->3)-alpha-D-GalNAc-(1->)))-L-threonine
CMP + [antifreeze glycoprotein]-(O-3-(alpha-Neu5Ac-(2->3)-beta-D-Gal-(1->3)-alpha-D-GalNAc-(1->)))-L-threonine
-
the enzyme specifically modifies glycoproteins and glycolipids which contain the sequence beta-D-Gal-(1->3)-beta-D-GalNAc to form the sequence alpha-Neu5Ac-(2->3)-beta-D-Gal-(1->3)-beta-D-GalNAc
-
-
?
CMP-N-acetyl-beta-neuraminate + [asialoglycoprotein]-(O-3-(beta-D-Gal-(1->3)-alpha-D-GalNAc-(1->)))-L-serine
CMP + [asialoglycoprotein]-(O-3-(alpha-Neu5Ac-(2->3)-beta-D-Gal-(1->3)-alpha-D-GalNAc-(1->)))-L-serine
-
-
-
-
?
CMP-N-acetyl-beta-neuraminate + [asialoglycoprotein]-(O-3-(beta-D-Gal-(1->3)-alpha-D-GalNAc-(1->)))-L-threonine
CMP + [asialoglycoprotein]-(O-3-(alpha-Neu5Ac-(2->3)-beta-D-Gal-(1->3)-alpha-D-GalNAc-(1->)))-L-threonine
-
the enzyme specifically modifies glycoproteins and glycolipids which contain the sequence beta-D-Gal-(1->3)-beta-D-GalNAc to form the sequence alpha-Neu5Ac-(2->3)-beta-D-Gal-(1->3)-beta-D-GalNAc
-
-
?
CMP-N-acetylneuraminate + beta-D-galactosyl-(1->3)-N-acetyl-alpha-D-galactosaminyl-R
CMP + alpha-N-acetylneuraminyl-(2->3)-beta-D-galactosyl-(1->3)-N-acetyl-alpha-D-galactosaminyl-R
-
the enzyme is involved in O-linked glycosylation pathway for synthesis of core 1 and core 2 oligosaccharides
-
-
?
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Sodium citrate
direct sialylation using CMP-N-acetyl-beta-neuraminate
additional information
-
overexpression of N-acetylglucosaminyltransferase III significantly inhibits alpha2,3-sialylation
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
lysophosphatidylcholine
-
C16-18 acyl derivatives of lysophosphatidylcholine stimulate the activity of enzyme form A more extensively than the C14 acyl derivative, and the C12 acyl derivative is without effect on enzyme form A
phospholipid/octylglucoside liposomes
-
incorporation into phospholipid/octylglucoside liposomes activates enzyme form A
-
Triton X-100
-
stimulates activity of enzyme form A. Enzyme form B is fully active in absence of detergents. Detergents stimulate the activity of enzyme form A by lowering the KD and KM of CMP-N-acetylneuraminate and increasing the Vmax of the reaction
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.35 - 0.39
[antifreeze glycoprotein]-(O-3-(beta-D-Gal-(1->3)-alpha-D-GalNAc-(1->)))-L-threonine
-
0.54
4-methylumbelliferyl 4-O-beta-D-galactosyl-beta-D-glucoside
-
mutant enzyme E271F/R313Y, in Tris-HCl buffer (100 mM, pH 8.5), at 37°C
0.67
4-methylumbelliferyl 4-O-beta-D-galactosyl-beta-D-glucoside
-
mutant enzyme R313Y, in Tris-HCl buffer (100 mM, pH 8.5), at 37°C
0.71
4-methylumbelliferyl 4-O-beta-D-galactosyl-beta-D-glucoside
-
mutant enzyme E271F, in Tris-HCl buffer (100 mM, pH 8.5), at 37°C
1.4
4-methylumbelliferyl 4-O-beta-D-galactosyl-beta-D-glucoside
-
wild type enzyme, in Tris-HCl buffer (100 mM, pH 8.5), at 37°C
0.18
CMP-N-acetylneuraminate
-
mutant enzyme E271F, in Tris-HCl buffer (100 mM, pH 8.5), at 37°C
0.34
CMP-N-acetylneuraminate
-
mutant enzyme E271F/R313Y, in Tris-HCl buffer (100 mM, pH 8.5), at 37°C
0.44
CMP-N-acetylneuraminate
-
wild type enzyme, in Tris-HCl buffer (100 mM, pH 8.5), at 37°C
0.62
CMP-N-acetylneuraminate
-
mutant enzyme R313Y, in Tris-HCl buffer (100 mM, pH 8.5), at 37°C
0.35
[antifreeze glycoprotein]-(O-3-(beta-D-Gal-(1->3)-alpha-D-GalNAc-(1->)))-L-threonine
-
pH 6.5, 37°C, enzyme form A
-
0.39
[antifreeze glycoprotein]-(O-3-(beta-D-Gal-(1->3)-alpha-D-GalNAc-(1->)))-L-threonine
-
pH 6.5, 37°C, enzyme form B
-
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2 - 8
4-methylumbelliferyl 4-O-beta-D-galactosyl-beta-D-glucoside
-
mutant enzyme E271F, in Tris-HCl buffer (100 mM, pH 8.5), at 37°C
17
4-methylumbelliferyl 4-O-beta-D-galactosyl-beta-D-glucoside
-
mutant enzyme E271F/R313Y, in Tris-HCl buffer (100 mM, pH 8.5), at 37°C
19
4-methylumbelliferyl 4-O-beta-D-galactosyl-beta-D-glucoside
-
mutant enzyme R313Y, in Tris-HCl buffer (100 mM, pH 8.5), at 37°C
47
4-methylumbelliferyl 4-O-beta-D-galactosyl-beta-D-glucoside
-
wild type enzyme, in Tris-HCl buffer (100 mM, pH 8.5), at 37°C
19
CMP-N-acetylneuraminate
-
mutant enzyme R313Y, in Tris-HCl buffer (100 mM, pH 8.5), at 37°C
23
CMP-N-acetylneuraminate
-
mutant enzyme E271F/R313Y, in Tris-HCl buffer (100 mM, pH 8.5), at 37°C
26
CMP-N-acetylneuraminate
-
mutant enzyme E271F, in Tris-HCl buffer (100 mM, pH 8.5), at 37°C
32
CMP-N-acetylneuraminate
-
wild type enzyme, in Tris-HCl buffer (100 mM, pH 8.5), at 37°C
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
28
4-methylumbelliferyl 4-O-beta-D-galactosyl-beta-D-glucoside
-
mutant enzyme R313Y, in Tris-HCl buffer (100 mM, pH 8.5), at 37°C
32
4-methylumbelliferyl 4-O-beta-D-galactosyl-beta-D-glucoside
-
mutant enzyme E271F/R313Y, in Tris-HCl buffer (100 mM, pH 8.5), at 37°C
34
4-methylumbelliferyl 4-O-beta-D-galactosyl-beta-D-glucoside
-
wild type enzyme, in Tris-HCl buffer (100 mM, pH 8.5), at 37°C
39
4-methylumbelliferyl 4-O-beta-D-galactosyl-beta-D-glucoside
-
mutant enzyme E271F, in Tris-HCl buffer (100 mM, pH 8.5), at 37°C
30
CMP-N-acetylneuraminate
-
mutant enzyme R313Y, in Tris-HCl buffer (100 mM, pH 8.5), at 37°C
69
CMP-N-acetylneuraminate
-
mutant enzyme E271F/R313Y, in Tris-HCl buffer (100 mM, pH 8.5), at 37°C
73
CMP-N-acetylneuraminate
-
wild type enzyme, in Tris-HCl buffer (100 mM, pH 8.5), at 37°C
140
CMP-N-acetylneuraminate
-
mutant enzyme E271F, in Tris-HCl buffer (100 mM, pH 8.5), at 37°C
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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PDB
SCOP
CATH
UNIPROT
ORGANISM
Pasteurella multocida;
Sus scrofa;
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
50000
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
full-length ST3Gal III DNA fragment subcloned into the pEF6/V5-His TOPO expression vector. SKOV-3 cells transfected with ST3Gal III-EF6
-
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
taxol treatment upregulates ST3Gal III expression and forces expression of ST3Gal III attenuated taxol induced apoptosis. Taxol induces the expression of ST3Gal III by a post-transcriptional mechanism in SKOV-3 ovarian cancer cells
-
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
E271F
-
the mutation does not affect alpha2-3-sialyltransferase activity
E271F/R313Y
-
the mutations do not affect alpha2-3-sialyltransferase activity
R313Y
-
the mutation does not affect alpha2-3-sialyltransferase activity
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
drug development
-
ST3Gal III can serve as a therapeutic target of taxol therapy
synthesis
synthesis
the enzyme can be exploited for the enzymatic synthesis of diverse sialyl products
synthesis
-
chemoenzymatic synthesis of sialylated oligosaccharides for their evaluation in a polysialyltransferase assay
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LINKS TO OTHER DATABASES (specific for EC-Number 2.4.99.4)
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