Information on EC 2.4.99.4 - beta-galactoside alpha-2,3-sialyltransferase

for references in articles please use BRENDA:EC2.4.99.4
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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria

EC NUMBER
COMMENTARY hide
2.4.99.4
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RECOMMENDED NAME
GeneOntology No.
beta-galactoside alpha-2,3-sialyltransferase
REACTION
REACTION DIAGRAM
COMMENTARY hide
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
show the reaction diagram
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-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
glycosyl group transfer
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-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
ganglio-series glycosphingolipids biosynthesis
-
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globo-series glycosphingolipids biosynthesis
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mucin core 1 and core 2 O-glycosylation
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Mucin type O-glycan biosynthesis
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Glycosaminoglycan biosynthesis - keratan sulfate
-
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Glycosphingolipid biosynthesis - lacto and neolacto series
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Glycosphingolipid biosynthesis - globo and isoglobo series
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Glycosphingolipid biosynthesis - ganglio series
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Metabolic pathways
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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.
CAS REGISTRY NUMBER
COMMENTARY hide
71124-51-1
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
-
Manually annotated by BRENDA team
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SwissProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
physiological function
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
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]
show the reaction diagram
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
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-
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
show the reaction diagram
-
-
-
-
?
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
show the reaction diagram
-
-
-
-
?
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
show the reaction diagram
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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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-
?
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
show the reaction diagram
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
show the reaction diagram
-
-
-
-
?
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
show the reaction diagram
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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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-
?
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
show the reaction diagram
-
-
-
?
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
show the reaction diagram
-
-
-
?
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
show the reaction diagram
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best substrate, about 37% conversion
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-
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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
show the reaction diagram
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-
-
-
?
CMP-N-acetylneuraminate + 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
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best acceptor substrate
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-
?
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
show the reaction diagram
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the enzyme is involved in O-linked glycosylation pathway for synthesis of core 1 and core 2 oligosaccharides
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-
?
CMP-N-acetylneuraminate + lactose
CMP + NeuAcalpha(2->3)Galbeta(1->4)Glc
show the reaction diagram
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-
-
-
?
additional information
?
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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
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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 + [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
show the reaction diagram
-
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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-
?
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
show the reaction diagram
-
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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-
?
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
show the reaction diagram
-
-
-
-
?
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
show the reaction diagram
-
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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-
?
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
show the reaction diagram
-
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 hide
LITERATURE
IMAGE
CDP
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less effective than CTP
CMP
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less effective than CTP
CTP
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most potent inhibitor among cytidine nucleotides
lysophosphatidylglycerol
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inhibition of enzyme form A and B
lysophosphatidylserine
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inhibition of enzyme form A
octyl-D-glucoside
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inhibition of enzyme form A and B
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Sodium citrate
direct sialylation using CMP-N-acetyl-beta-neuraminate
additional information
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overexpression of N-acetylglucosaminyltransferase III significantly inhibits alpha2,3-sialylation
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
lysophosphatidylcholine
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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
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incorporation into phospholipid/octylglucoside liposomes activates enzyme form A
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Triton X-100
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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
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.54 - 1.4
4-methylumbelliferyl 4-O-beta-D-galactosyl-beta-D-glucoside
0.2 - 0.21
beta-D-Gal-(1->3)-beta-D-GalNAc
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0.18 - 0.62
CMP-N-acetylneuraminate
0.35 - 0.39
[antifreeze glycoprotein]-(O-3-(beta-D-Gal-(1->3)-alpha-D-GalNAc-(1->)))-L-threonine
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2 - 47
4-methylumbelliferyl 4-O-beta-D-galactosyl-beta-D-glucoside
19 - 32
CMP-N-acetylneuraminate
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
28 - 39
4-methylumbelliferyl 4-O-beta-D-galactosyl-beta-D-glucoside
30 - 140
CMP-N-acetylneuraminate
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00022
CTP
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pH and temperature not specified in the publication
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4.8 - 6.4
formation of CMP-N-acetyl-beta-neuraminate from CMP
5.2 - 7.2
direct sialylation using CMP-N-acetyl-beta-neuraminate
6.5
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assay at
7
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assay at
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37
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assay at
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
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T-lymphocytes, Epstein-Barr virus immortalized B-lymphocytes
Manually annotated by BRENDA team
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expresses little ST3Gal III protein
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
PDB
SCOP
CATH
UNIPROT
ORGANISM
Pasteurella multocida;
A5LHX0
Photobacterium phosphoreum;
Sus scrofa;
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
44000
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enzyme form B
49000
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enzyme form A
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, 50% (w/v) glycerol, 6 months, no loss of activity
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Ni2+-NTA column chromatography
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purification of enzyme form A and B
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21 (DE3) cells
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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 hide
LITERATURE
E271F
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the mutation does not affect alpha2-3-sialyltransferase activity
E271F/R313Y
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the mutations do not affect alpha2-3-sialyltransferase activity
R313Y
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the mutation does not affect alpha2-3-sialyltransferase activity
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
drug development
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ST3Gal III can serve as a therapeutic target of taxol therapy
synthesis