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Information on EC 2.4.99.4 - beta-galactoside alpha-2,3-sialyltransferase
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EC Tree
2.4.99.4 beta-galactoside alpha-2,3-sialyltransferaseIUBMB Comments
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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Word Map
- 2.4.99.4
-
sialylation
- st6gal
- alpha-2,6-sialyltransferase
- o-glycans
- lipooligosaccharide
-
st8sia
-
st6galnac
-
cmp-n-acetylneuraminic
- alpha-1,3-fucosyltransferase
- drug development
- synthesis
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Reaction Schemes
Synonyms
alpha 2,3-ST 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
alpha 2,3-ST
-
-
-
-
alpha2-->3 sialyltransferase
-
-
-
-
alpha2-3-sialyltransferase 1
-
multifunctional enzyme which has alpha2-6-sialyltransferase, alpha2-3-sialidase, and alpha2-3-trans-sialidase activities in addition to its major alpha2-3-sialyltransferase activity
alpha3-SA-T
-
-
-
-
alpha3SA-T
beta-D-Gal-(1-3)-D-GalNAc alpha-(2-3)-sialyltransferase
-
-
-
-
beta-galactoside alpha-2,3-sialyltransferase
-
-
-
-
CMP-N-acetylneuraminate:beta-D-galactoside alpha2-3 sialyltransferase
-
-
-
-
CMP-Neu5Ac:Glbeta1-3GalNAc alpha2,3-sialyltransferase
-
-
-
-
CMP-NeuAc:galactoside(alpha2-3)-sialyltransferase
-
-
-
-
CMP-SA:Galbeta3GalNAc-R alpha3-sialyltransferase
-
-
-
-
CMP-sialic acid:Galbeta1-3GalNAc-R alpha3-sialyltransferase
-
-
-
-
Gal-beta-1,3-GalNAc-alpha-2,3-sialyltransferase
-
-
-
-
Gal-NAc6S
-
-
-
-
Galbeta1,3GalNAc alpha2,3-sialyltransferase
-
-
-
-
galbeta1,3galNAcalpha2,3-sialyltransferase
-
-
-
-
NeuAc alpha-2,3-sialyltransferase
-
-
-
-
sialyltransferase, cytidine monophosphoacetylneuraminate-beta-galactoside alpha2-->3-
-
-
-
-
SIATFL
-
-
-
-
ST3Gal I
-
-
-
-
ST3Gal III
ST3GalA.1
-
-
-
-
ST3GalIA
-
-
-
-
ST3O
-
-
-
-
alpha3SA-T
-
-
-
-
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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 SOURCE
PATHWAYS
KEGG
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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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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 SUBSTRATE
NATURAL 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-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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INHIBITOR
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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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Adenocarcinoma
Expression and function of alpha 2,3-sialyl- and alpha 1,3/1,4-fucosyltransferases in colon adenocarcinoma cell lines: role in synthesis of E-selectin counter-receptors.
beta-galactoside alpha-2,3-sialyltransferase deficiency
Sialyltransferase specificity in selectin ligand formation.
Brain Neoplasms
Effect of Golgi membrane phospholipid composition on the molecular species of GM3 gangliosides synthesized by rat liver sialyltransferase.
Breast Neoplasms
Multiplex reverse transcription polymerase chain reaction assessment of sialyltransferase expression in human breast cancer.
Breast Neoplasms
Prognostic value of tumoral sialyltransferase expression and circulating E-selectin concentrations in node-negative breast cancer patients.
Carcinoma
alpha-2,3-Sialyltransferase type 3N and alpha-1,3-fucosyltransferase type VII are related to sialyl Lewis(x) synthesis and patient survival from lung carcinoma.
Carcinoma
Altered mRNA expression of sialyltransferase in squamous cell carcinomas of the cervix.
Carcinoma
Expression of ST3Gal, ST6Gal, ST6GalNAc and ST8Sia in human hepatic carcinoma cell lines, HepG-2 and SMMC-7721 and normal hepatic cell line, L-02.
Carcinoma
MiR-193a-3p and miR-224 mediate renal cell carcinoma progression by targeting alpha-2,3-sialyltransferase IV and the phosphatidylinositol 3 kinase/Akt pathway.
Carcinoma
Overexpression of sialyltransferase CMP-sialic acid:Galbeta1,3GalNAc-R alpha6-Sialyltransferase is related to poor patient survival in human colorectal carcinomas.
Carcinoma, Hepatocellular
Molecular cloning and expression of Galbeta1,3GalNAc alpha2, 3-sialyltransferase from human fetal liver.
Carcinoma, Renal Cell
MiR-193a-3p and miR-224 mediate renal cell carcinoma progression by targeting alpha-2,3-sialyltransferase IV and the phosphatidylinositol 3 kinase/Akt pathway.
Carcinoma, Squamous Cell
Altered mRNA expression of sialyltransferase in squamous cell carcinomas of the cervix.
Carcinoma, Squamous Cell
Enhanced sialyltransferases transcription in cervical intraepithelial neoplasia.
Hypertension, Pulmonary
Multiplex reverse transcription polymerase chain reaction assessment of sialyltransferase expression in peripheral blood mononuclear cells in systemic sclerosis.
Infections
Alpha-2,3-sialyltransferase enhances Neisseria gonorrhoeae survival during experimental murine genital tract infection.
Insulin Resistance
Mice lacking sialyltransferase ST3Gal-II develop late-onset obesity and insulin resistance.
Leukemia, Myeloid, Acute
Effect of ST3GAL 4 and FUT 7 on sialyl Lewis X synthesis and multidrug resistance in human acute myeloid leukemia.
Neoplasms
Alpha2,6-sialylation of cell-surface N-glycans inhibits glioma formation in vivo.
Neoplasms
Characterization of Cancer Associated Mucin Type O-Glycans Using the Exchange Sialylation Properties of Mammalian Sialyltransferase ST3Gal-II.
Neoplasms
Prognostic value of tumoral sialyltransferase expression and circulating E-selectin concentrations in node-negative breast cancer patients.
Neuroblastoma
Effect of Golgi membrane phospholipid composition on the molecular species of GM3 gangliosides synthesized by rat liver sialyltransferase.
Obesity
Mice lacking sialyltransferase ST3Gal-II develop late-onset obesity and insulin resistance.
Ovarian Neoplasms
Human beta-galactoside alpha-2,3-sialyltransferase (ST3Gal III) attenuated Taxol-induced apoptosis in ovarian cancer cells by downregulating caspase-8 activity.
Ovarian Neoplasms
Human GM3 Synthase Attenuates Taxol-Triggered Apoptosis Associated with Downregulation of Caspase-3 in Ovarian Cancer Cells.
Prostatic Neoplasms
Androgen-regulated transcriptional control of sialyltransferases in prostate cancer cells.
Reproductive Tract Infections
Alpha-2,3-sialyltransferase enhances Neisseria gonorrhoeae survival during experimental murine genital tract infection.
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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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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
T-lymphocytes, Epstein-Barr virus immortalized B-lymphocytes
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
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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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
Sequence
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
50000
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PROTEIN VARIANTS
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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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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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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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Huang, S.; Day, T.W.; Choi, M.R.; Safa, A.R.
Human beta-galactoside alpha-2,3-sialyltransferase (ST3Gal III) attenuated Taxol-induced apoptosis in ovarian cancer cells by downregulating caspase-8 activity
Mol. Cell. Biochem.
331
81-88
2009
Homo sapiens
brenda
Sugiarto, G.; Lau, K.; Li, Y.; Khedri, Z.; Yu, H.; Le, D.T.; Chen, X.
Decreasing the sialidase activity of multifunctional Pasteurella multocida alpha2-3-sialyltransferase 1 (PmST1) by site-directed mutagenesis
Mol. Biosyst.
7
3021-3027
2011
Pasteurella multocida
brenda
Perez-Garay, M.; Arteta, B.; Pages, L.; de Llorens, R.; de Bolos, C.; Vidal-Vanaclocha, F.; Peracaula, R.
alpha2,3-Sialyltransferase ST3Gal III modulates pancreatic cancer cell motility and adhesion in vitro and enhances its metastatic potential in vivo
PLoS ONE
5
e12524
2010
Homo sapiens
brenda
Lu, J.; Isaji, T.; Im, S.; Fukuda, T.; Kameyama, A.; Gu, J.
Expression of N-acetylglucosaminyltransferase III suppresses alpha2,3-sialylation, and its distinctive functions in cell migration are attributed to alpha2,6-sialylation levels
J. Biol. Chem.
291
5708-5720
2016
Homo sapiens
brenda
Chandrasekaran, E.V.; Xue, J.; Xia, J.; Locke, R.D.; Matta, K.L.; Neelamegham, S.
Reversible sialylation synthesis of cytidine 5-monophospho-N-acetylneuraminic acid from cytidine 5-monophosphate with alpha2,3-sialyl O-glycan-, glycolipid-, and macromolecule-based donors yields diverse sialylated products
Biochemistry
47
320-330
2008
Rattus norvegicus (Q11205)
brenda
Shigeta, S.; Winter, H.C.; Goldstein, I.J.
alpha-(2->3)- and alpha-(2->6)-Sialyltransferase activities present in three variants of Ehrlich tumor cells identification of the products derived from N-acetyllactosamine and beta-D-Gal-(1->3)-alpha-D-GalNAc-(1->O)-Bn
Carbohydr. Res.
264
111-121
1994
Mus musculus
brenda
Sadler, J.E.; Rearick, J.I.; Paulson, J.C.; Hill, R.L.
Purification to homogeneity of a beta-galactoside alpha2 leads to 3 sialyltransferase and partial purification of an alpha-N-acetylgalactosaminide alpha2 leads to 6 sialyltransferase from porcine submaxillary glands
J. Biol. Chem.
254
4434-4443
1979
Sus scrofa (Q02745)
brenda
Rearick, J.I.; Sadler, J.E.; Paulson, J.C.; Hill, R.L.
Enzymatic characterization of beta D-galactoside alpha2 leads to 3 sialyltransferase from porcine submaxillary gland
J. Biol. Chem.
254
4444-4451
1979
Sus scrofa (Q02745)
brenda
Westcott, K.R.; Hill, R.L.
Reconstitution of a porcine submaxillary gland beta-D-galactoside alpha 2-3 sialyltransferase into liposomes
J. Biol. Chem.
260
13116-13121
1985
Sus scrofa (Q02745)
brenda
Higgins, E.A.; Siminovitch, K.A.; Zhuang, D.; Brockhausen, I.; Dennis, J.W.
Aberrant O-linked oligosaccharide biosynthesis in lymphocytes and platelets from patients with the Wiskott-Aldrich syndrome
J. Biol. Chem.
266
6280-6290
1991
Homo sapiens
brenda
Sengupta, P.; Misra, A.K.; Suzuki, M.; Fukuda, M.; Hindsgaul, O.
Chemoenzymatic synthesis of sialylated oligosaccharides for their evaluation in a polysialyltransferase assay
Tetrahedron Lett.
44
6037-6042
2003
Rattus norvegicus
-
brenda
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