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Information on EC 2.4.99.6 - N-acetyllactosaminide alpha-2,3-sialyltransferase
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2.4.99.6 N-acetyllactosaminide alpha-2,3-sialyltransferaseIUBMB Comments
The enzyme recognizes the sequence beta-D-galactosyl-(1->4)-N-acetyl-D-glucosaminyl (known as type 2 histo-blood group precursor disaccharide) in non-reducing termini of glycan moieties in glycoproteins and glycolipids. The enzyme from chicken brain was shown to act on neolactotetraosylceramide, producing ganglioside LM1 .
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Word Map
The enzyme appears in viruses and cellular organisms
Reaction Schemes
Synonyms
alpha2,3(N) sialyltransferase, alpha2,3(N)ST, alpha2,3(O) sialyltransferase, alpha2,3(O)ST, alpha2-->3 sialyltransferase, CMP-NeuAc:Gal beta 1-4GlcNAc-R alpha(2-3)-sialyltransferase, cytidine monophosphoacetylneuraminate-beta-galactosyl(1-->4)acetylglucosaminide alpha2-->3-sialyltransferase, cytidine monophosphoacetylneuraminate-neolactotetraosylceramide sialyltransferase, Gal beta-1,3(4) GlcNAc alpha-2,3 sialyltransferase, Galbeta(1->4)GlcNAc-R alpha(2->3)sialyltransferase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
alpha2-->3 sialyltransferase
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cytidine monophosphoacetylneuraminate-beta-galactosyl(1-->4)acetylglucosaminide alpha2-->3-sialyltransferase
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cytidine monophosphoacetylneuraminate-neolactotetraosylceramide sialyltransferase
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Gal beta-1,3(4) GlcNAc alpha-2,3 sialyltransferase
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Galbeta(1->4)GlcNAc-R alpha(2->3)sialyltransferase
N-acetyllactosaminide alpha-2,3-sialyltransferase
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SAT-3
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sialyltransferase
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sialyltransferase 3
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sialyltransferase, cytidine monophosphoacetylneuraminate-beta-galactosyl(1-->4)acetylglucosaminide alpha2-->3-
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ST3Gal III
ST3Gal IV
ST3Gal-IV
ST3N
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
CMP-N-acetyl-beta-neuraminate + beta-D-galactosyl-(1->4)-N-acetyl-beta-D-glucosaminyl-R = CMP + N-acetyl-alpha-neuraminyl-(2->3)-beta-D-galactosyl-(1->4)-N-acetyl-beta-D-glucosaminyl-R
acts on beta-D-galactosyl-1,4-N-acetyl-D-glucosaminyl termini on glycoprotein
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CMP-N-acetylneuraminate + beta-D-galactosyl-(1->4)-N-acetyl-beta-D-glucosaminyl-(1->3)-beta-D-galactosyl-(1->4)-D-glucosyl-(1<->1)-ceramide = CMP + alpha-N-acetylneuraminyl-(2->3)-beta-D-galactosyl-(1->4)-N-acetyl-beta-D-glucosaminyl-(1->3)-beta-D-galactosyl-(1->4)-D-glucosyl-(1<->1)-ceramide
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
glycosyl group transfer
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PATHWAY SOURCE
PATHWAYS
KEGG
MetaCyc
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SYSTEMATIC NAME
IUBMB Comments
CMP-N-acetyl-beta-neuraminate:beta-D-galactosyl-(1->4)-N-acetyl-btea-D-glucosaminyl-R (2->3)-N-acetyl-alpha-neuraminyltransferase (configuration-inverting)
The enzyme recognizes the sequence beta-D-galactosyl-(1->4)-N-acetyl-D-glucosaminyl (known as type 2 histo-blood group precursor disaccharide) in non-reducing termini of glycan moieties in glycoproteins and glycolipids. The enzyme from chicken brain was shown to act on neolactotetraosylceramide, producing ganglioside LM1 [2].
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CAS REGISTRY NUMBER
COMMENTARY
77537-85-0
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83745-06-6
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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-N-acetyl-beta-neuraminate + 4-methylumbelliferyl beta-D-Gal-(1->4)-beta-D-GlcNAc
CMP + 4-methylumbelliferyl alpha-Neu5Ac-(2->3)-beta-D-Gal-(1->4)-beta-D-GlcNAc
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?
CMP-N-acetyl-beta-neuraminate + 4-methylumbelliferyl beta-lactoside
CMP + alpha-Neu5Ac-(2->3)-beta-D-Gal-(1->4)-beta-D-Glc
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?
CMP-N-acetyl-beta-neuraminate + 4-methylumbelliferyl beta-Lewis x
CMP + 4-methylumbelliferyl alpha-Neu5Ac-(2->3)-beta-D-Gal-(1->4)-[alpha-L-Fuc-(1->3)]-beta-D-GlcNAc
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?
CMP-N-acetyl-beta-neuraminate + 4-nitrophenyl beta-D-Gal-(1->4)-beta-D-GlcNAc-(1->3)-beta-D-Gal
CMP + 4-nitrophenyl alpha-Neu5Ac-(2->3)-beta-D-Gal-(1->4)-beta-D-GlcNAc-(1->3)-beta-D-Gal
CMP-N-acetyl-beta-neuraminate + 4-nitrophenyl beta-D-Gal-(1->4)-beta-D-GlcNAc-(1->3)-beta-D-Gal-(1->4)-beta-D-GlcNAc
CMP + 4-nitrophenyl alpha-Neu5Ac-(2->3)-beta-D-Gal-(1->4)-beta-D-GlcNAc-(1->3)-beta-D-Gal-(1->4)-beta-D-GlcNAc
CMP-N-acetyl-beta-neuraminate + 8-methoxy-8-oxooctyl beta-D-Gal-(1->4)-beta-D-GlcNAc
CMP + 8-methoxy-8-oxooctyl alpha-Neu5Ac-(2->3)-beta-D-Gal-(1->4)-beta-D-GlcNAc
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?
CMP-N-acetyl-beta-neuraminate + allyl beta-D-Gal-(1->4)-beta-D-GlcNAc
CMP + allyl alpha-Neu5Ac-(2->3)-beta-D-Gal-(1->4)-beta-D-GlcNAc
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alpha2,3(N) sialyltransferase. 4.7.2% 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-(3-F)Gal-(1->4)-beta-D-GlcNAc-(1->6)-[beta-D-Gal-(1->3)]-alpha-D-GalNAc
CMP + benzyl alpha-Neu5Ac-(2->3)-beta-D-(3-F)Gal-(1->4)-beta-D-GlcNAc-(1->6)-[beta-D-Gal-(1->3)]-alpha-D-GalNAc
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7.2% of the activity compared to mucin core 2-based compound benzyl beta-D-Gal-(1->4)-beta-D-GlcNAc-(1->6)-beta-D-(3-O-Me)Gal-(1->3)-alpha-D-GalNAc, alpha2,3(N) sialyltransferase. 102.9% of the activity compared to mucin core 2-based compound 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-(3-O-Me)Gal-(1->4)-beta-D-GlcNAc-(1->6)-[beta-D-Gal-(1->3)]-alpha-D-GalNAc
CMP + benzyl alpha-Neu5Ac-(2->3)-beta-D-(3-O-Me)Gal-(1->4)-beta-D-GlcNAc-(1->6)-[beta-D-Gal-(1->3)]-alpha-D-GalNAc
CMP-N-acetyl-beta-neuraminate + benzyl beta-D-(4-O-Me)Gal-(1->4)-beta-D-GlcNAc
CMP + benzyl alpha-Neu5Ac-(2->3)-beta-D-(4-O-Me)Gal-(1->4)-beta-D-GlcNAc
CMP-N-acetyl-beta-neuraminate + benzyl beta-D-(4-O-Me)Gal-(1->4)-beta-D-GlcNAc-(1->6)-[beta-D-Gal-(1->3)]-alpha-D-GalNAc
CMP + benzyl alpha-Neu5Ac-(2->3)-beta-D-(4-O-Me)Gal-(1->4)-beta-D-GlcNAc-(1->6)-[beta-D-Gal-(1->3)]-alpha-D-GalNAc
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99.8% of the activity compared to mucin core 2-based compound benzyl beta-D-Gal-(1->4)-beta-D-GlcNAc-(1->6)-beta-D-(3-O-Me)Gal-(1->3)-alpha-D-GalNAc, alpha2,3(N) sialyltransferase. 103% of the activity compared to mucin core 2-based compound 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->4)-beta-D-GlcNAc-(1->6)-[4-deoxy-4-fluoro-beta-D-Gal-(1->3)]-beta-D-GalNAc
CMP + benzyl alpha-Neu5Ac-(2->3)-beta-D-Gal-(1->4)-beta-D-GlcNAc-(1->6)-[4-deoxy-4-fluoro-beta-D-Gal-(1->3)]-beta-D-GalNAc
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?
CMP-N-acetyl-beta-neuraminate + benzyl beta-D-Gal-(1->4)-beta-D-GlcNAc-(1->6)-[beta-D-(3-F)Gal-(1->3)]-alpha-D-GalNAc
CMP + benzyl alpha-Neu5Ac-(2->3)-beta-D-Gal-(1->4)-beta-D-GlcNAc-(1->6)-[beta-D-(3-F)Gal-(1->3)]-alpha-D-GalNAc
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96.9% of the activity compared to mucin core 2-based compound benzyl beta-D-Gal-(1->4)-beta-D-GlcNAc-(1->6)-beta-D-(3-O-Me)Gal-(1->3)-alpha-D-GalNAc, alpha2,3(N) sialyltransferase. 77.2% of the activity compared to mucin core 2-based compound 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->4)-beta-D-GlcNAc-(1->6)-[beta-D-(3-O-Me)Gal-(1->3)]-alpha-D-GalNAc
CMP + benzyl alpha-Neu5Ac-(2->3)-beta-D-Gal-(1->4)-beta-D-GlcNAc-(1->6)-[beta-D-(3-O-Me)Gal-(1->3)]-alpha-D-GalNAc
CMP-N-acetyl-beta-neuraminate + benzyl beta-D-Gal-(1->4)-beta-D-GlcNAc-(1->6)-[beta-D-(4-O-Me)Gal-(1->3)]-alpha-D-GalNAc
CMP + benzyl alpha-Neu5Ac-(2->3)-beta-D-Gal-(1->4)-beta-D-GlcNAc-(1->6)-[beta-D-(4-O-Me)Gal-(1->3)]-alpha-D-GalNAc
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100.6% of the activity compared to mucin core 2-based compound benzyl beta-D-Gal-(1->4)-beta-D-GlcNAc-(1->6)-beta-D-(3-O-Me)Gal-(1->3)-alpha-D-GalNAc, alpha2,3(N) sialyltransferase. 101.3% of the activity compared to mucin core 2-based compound 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->4)-beta-D-GlcNAc-(1->6)-[beta-D-Gal-(1->3)]-alpha-GalNAc
CMP + benzyl alpha-Neu5Ac-(2->3)-beta-D-Gal-(1->4)-beta-D-GlcNAc-(1->6)-[beta-D-Gal-(1->3)]-alpha-GalNAc
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101% of the activity compared to ally beta-D-Gal-(1->4)-beta-D-GlcNAc, alpha2,3(N) sialyltransferase. 94.4% 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->4)-[alpha-D-Fuc-(1->3)]-beta-D-GlcNAc-(1->6)-[alpha-NeuAc-(2->3)-beta-D-Gal-(1->3)]-alpha-D-GalNAc
CMP + benzyl alpha-Neu5Ac-(2->3)-beta-D-Gal-(1->4)-[alpha-D-Fuc-(1->3)]-beta-D-GlcNAc-(1->6)-[alpha-NeuAc-(2->3)-beta-D-Gal-(1->3)]-alpha-D-GalNAc
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27.1% of the activity compared to ally beta-D-Gal-(1->4)-beta-D-GlcNAc, alpha2,3(N) sialyltransferase
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?
CMP-N-acetyl-beta-neuraminate + beta-D-(2-O-Me)Gal-(1->4)-beta-D-GlcNAc
CMP + alpha-Neu5Ac-(2->3)-beta-D-(2-O-Me)Gal-(1->4)-beta-D-GlcNAc
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60% of the activity compared to ally beta-D-Gal-(1->4)-beta-D-GlcNAc, alpha2,3(N) sialyltransferase. 0.2% 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-GlcNAc
CMP + alpha-Neu5Ac-(2->3)-beta-D-Glc-(1->3)-beta-D-GalNAc
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-D-Gal-(1->3)-beta-D-GlcNAc
CMP + alphaNeuAc-(2->3)-beta-D-Gal-(1->3)-beta-D-GlcNAc
A0A1D5NU03, F1NQP1
activity with beta-D-Gal-(1->3)-beta-D-GlcNAc is higher than activity with beta-D-Gal-(1->4)-beta-D-GlcNAc
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?
CMP-N-acetyl-beta-neuraminate + beta-D-Gal-(1->3)-beta-GlcNAc
CMP + alphaNeuAc-(2->3)-beta-D-Gal-(1->3)-beta-D-GlcNAc
A0A1D5NU03, F1NQP1
activity with beta-D-Gal-(1->4)-beta-D-GlcNAc is higher than activity with beta-D-Gal-(1->3)-beta-D-GlcNAc
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?
CMP-N-acetyl-beta-neuraminate + beta-D-Gal-(1->4)-alpha-D-Glc
CMP + alpha-Neu5Ac-(2->3)-beta-D-Gal-(1->4)-alpha-D-Glc
CMP-N-acetyl-beta-neuraminate + beta-D-Gal-(1->4)-beta-D-Glc
CMP + alpha-Neu5Ac-(2->3)-beta-D-Gal-(1->4)-beta-D-Glc
CMP-N-acetyl-beta-neuraminate + beta-D-Gal-(1->4)-beta-D-Glc-(1<->1)-ceramide
CMP + alpha-Neu5Ac-(2->3)-beta-D-Gal-(1->4)-beta-D-Glc-(1<->1)-ceramide
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i.e. lactosylceramide
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?
CMP-N-acetyl-beta-neuraminate + beta-D-Gal-(1->4)-beta-D-GlcNAc
CMP + alpha-Neu5Ac-(2->3)-beta-D-Gal-(1->4)-beta-D-GlcNAc
CMP-N-acetyl-beta-neuraminate + beta-D-Gal-(1->4)-beta-D-GlcNAc
CMP + alpha-NeuAc-(2->3)-beta-D-Gal-(1->4)-beta-D-GlcNAc
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i.e. N-acetyllactosamine. Sialyltransferase Hb-ST2 shows monofunctional alpha2,3-sialyltransferase activity with a strong preference for N-acetyllactosamine over lactose and very low levels of activity on 3-linked Gal. No 2,8-sialyltransferase activity
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?
CMP-N-acetyl-beta-neuraminate + beta-D-Gal-(1->4)-beta-D-GlcNAc
CMP + alphaNeuAc-(2->3)-beta-D-Gal-(1->4)-beta-D-GlcNAc
A0A1D5NU03, F1NQP1
activity with beta-D-Gal-(1->3)-beta-D-GlcNAc is higher than activity with beta-D-Gal-(1->4)-beta-D-GlcNAc
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?
CMP-N-acetyl-beta-neuraminate + beta-D-Gal-(1->4)-beta-D-GlcNAc
CMP + alphaNeuAc-(2->3)-beta-Gal-(1->4)-beta-GlcNAc
A0A1D5NU03, F1NQP1
activity with beta-D-Gal-(1->4)-beta-D-GlcNAc is higher than activity with beta-Gal-(1->3)-beta-GlcNAc
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?
CMP-N-acetyl-beta-neuraminate + beta-D-Gal-(1->4)-beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->6)-beta-D-Man-(1->4)-beta-D-GlcNAc
CMP + alpha-Neu5Ac-(2->3)-beta-D-Gal-(1->4)-beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->6)-beta-D-Man-(1->4)-beta-D-GlcNAc
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?
CMP-N-acetyl-beta-neuraminate + beta-D-Gal-(1->4)-beta-D-GlcNAc-(1->3)-beta-D-Gal-(1->4)-beta-D-Glc-(1<->1)-ceramide
CMP + ganglioside LM1
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i.e. neolactotetraosylceramide
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?
CMP-N-acetyl-beta-neuraminate + beta-D-Gal-(1->4)-beta-D-GlcNAc-(1->6)-[beta-D-Gal-(1->3)]-alpha-D-GalNAc-R
CMP + alpha-Neu5Ac-(2->3)-beta-D-Gal-(1->4)-beta-D-GlcNAc-(1->6)-[beta-D-Gal-(1->3)]-alpha-D-GalNAc-R
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?
CMP-N-acetyl-beta-neuraminate + beta-D-Gal-(1->4)-beta-D-GlcNAc-R
CMP + alpha-Neu5Ac-(2->3)-beta-D-Gal-(1->4)-beta-D-GlcNAc-R
CMP-N-acetyl-beta-neuraminate + beta-D-Gal-(1->4)-beta-D-GlcNAc-[protein]
CMP + alpha-Neu5Ac-(2->3)-beta-D-Gal-(1->4)-beta-D-GlcNAc-[protein]
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?
CMP-N-acetyl-beta-neuraminate + beta-D-Gal-(1->4)-N-GlcNAc-R
CMP + alpha-Neu5Ac-(2->3)-beta-D-Gal-(1->4)-N-GlcNAc-R
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CMP-N-acetyl-beta-neuraminate + beta-D-Gal-(1->4)-[alpha-D-Fuc-(1->3)]-beta-D-GlcNAc-[protein]
CMP + alpha-Neu5Ac-(2->3)-beta-D-Gal-(1->4)-[alpha-D-Fuc-(1->3)]-beta-D-GlcNAc-[protein]
i.e. Lewis x epitope
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?
CMP-N-acetyl-beta-neuraminate + beta-D-mannopyranoside
CMP + alpha-Neu5Ac-(2->3)-beta-D-Man
CMP-N-acetyl-beta-neuraminate + beta-D-N-acetylgalactosamine
CMP + alpha-Neu5Ac-(2->3)-beta-D-GalNAc
CMP-N-acetyl-beta-neuraminate + beta-D-N-acetylglucosamine
CMP + alpha-Neu5Ac-(2->3)-beta-D-GlcNAc
CMP-N-acetyl-beta-neuraminate + FCHASE beta-D-Gal-(1->4)-beta-D-GlcNAc
CMP + FCHASE alpha-Neu5Ac-(2->3)-beta-D-Gal-(1->4)-beta-D-GlcNAc
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?
CMP-N-acetyl-beta-neuraminate + methyl beta-D-Gal-(1->3)-beta-D-GlcNAc
CMP + methyl alpha-Neu5Ac-(2->3)-beta-D-Gal-(1->4)-beta-D-GlcNAc
CMP-N-acetyl-beta-neuraminate + methyl beta-D-Gal-(1->4)-beta-D-(6-O-sulfo)GlcNAc-(1->6)-[alphaNeu5Ac-(2->3)-beta-D-Gal-(1->3)]-alpha-GalNAc
CMP + methyl alpha-Neu5Ac-(2->3)-beta-D-Gal-(1->4)-beta-D-(6-O-sulfo)GlcNAc-(1->6)-[alphaNeu5Ac-(2->3)-beta-D-Gal-(1->3)]-alpha-GalNAc
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50.8% of the activity compared to ally beta-D-Gal-(1->4)-beta-D-GlcNAc, alpha2,3(N) sialyltransferase
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?
CMP-N-acetyl-beta-neuraminate + methyl beta-D-Gal-(1->4)-beta-D-(6-O-sulfo)GlcNAc-(1->6)-[beta-D-Gal-(1->3)]-alpha-D-GalNAc
CMP + methyl alpha-Neu5Ac-(2->3)-beta-D-Gal-(1->4)-beta-D-(6-O-sulfo)GlcNAc-(1->6)-[beta-D-Gal-(1->3)]-alpha-D-GalNAc
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28.1% of the activity compared to ally beta-D-Gal-(1->4)-beta-D-GlcNAc, alpha2,3(N) sialyltransferase
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-
?
CMP-N-acetyl-beta-neuraminate + methyl beta-D-Gal-(1->4)-beta-D-GlcNAc
CMP + methyl alpha-Neu5Ac-(2->3)-beta-D-Gal-(1->4)-beta-D-GlcNAc
CMP-N-acetyl-beta-neuraminate + methyl beta-D-Gal-(1->4)-[alpha-D-Fuc-(1->3)]-beta-D-GlcNAc-(1->6)-[beta-D-Gal-(1->3)]-alpha-D-GalNAc
CMP + methyl alpha-Neu5Ac-(2->3)-beta-D-Gal-(1->4)-[alpha-D-Fuc-(1->3)]-beta-D-GlcNAc-(1->6)-[beta-D-Gal-(1->3)]-alpha-D-GalNAc
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19% of the activity compared to ally beta-D-Gal-(1->4)-beta-D-GlcNAc, alpha2,3(N) sialyltransferase. 133.4% 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 + methyl beta-D-galactopyranoside
CMP + methyl alpha-Neu5Ac-(2->3)-beta-D-Gal
251% of the activity with beta-D-Gal-(1->4)-beta-D-Glc, truncated recombinant enzyme
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-
?
CMP-N-acetyl-beta-neuraminate + methyl beta-D-galactopyranoside
CMP + methyl alpha-Neu5Ac-(2->3)-beta-D-galactopyranoside
CMP-N-acetyl-beta-neuraminate + methyl beta-D-glucopyranoside
CMP + methyl alpha-Neu5Ac-(2->3)-beta-D-Glc
33% of the activity with beta-D-Gal-(1->4)-beta-D-Glc, truncated recombinant enzyme
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-
?
CMP-N-acetyl-beta-neuraminate + methyl beta-D-glucopyranoside
CMP + methyl alpha-Neu5Ac-(2->3)-beta-D-glucopyranoside
52% of the activity with beta-D-Gal-(1->4)-beta-D-Glc, recombinant enzyme
-
-
?
CMP-N-acetyl-beta-neuraminate + methyl beta-D-mannopyranoside
CMP + methyl alpha-Neu5Ac-(2->3)-beta-D-Man
CMP-N-acetylneuraminate + beta-D-Gal-(1->3)-beta-D-GlcNAc
CMP + alpha-Neu5Ac-(2->3)-beta-D-Gal-(1->3)-beta-D-GlcNAc
Q17WF9
about 25% of the activity with beta-D-Gal-(1->4)-beta-D-GlcNAc
-
-
?
CMP-N-acetylneuraminate + beta-D-Gal-(1->4)-beta-D-GalNAc-R
CMP + alpha-Neu5Ac-(2->3)-beta-D-Gal-(1->4)-beta-D-GalNAc-R
CMP-N-acetylneuraminate + beta-D-Gal-(1->4)-beta-D-Glc
CMP + alpha-Neu5Ac-(2->3)-beta-D-Gal-(1->4)-beta-D-Glc
Q17WF9
about 10% of the activity with beta-D-Gal-(1->4)-beta-D-GlcNAc
-
-
?
CMP-N-acetylneuraminate + beta-D-Gal-(1->4)-beta-D-Glc-R
CMP + alpha-Neu5Ac-(2->3)-beta-D-Gal-(1->4)-beta-D-Glc-R
-
artificial glycopolypeptides carrying beta-D-Gal-(1->4)-beta-D-GlcNAc and beta-D-Gal-(1->4)-beta-D-Glc are further converted to alpha-Neu5Ac-(2->3)-beta-D-Gal-(1->4)-beta-D-GlcNAc and alpha-Neu5Ac-(2->3)-beta-D-Gal-(1->4)-beta-D-Glc sialyloligosaccharides
-
-
?
CMP-N-acetylneuraminate + beta-D-Gal-(1->4)-beta-D-GlcNAc
CMP + alpha-Neu5Ac-(2->3)-beta-D-Gal-(1->4)-beta-D-GlcNAc
CMP-N-acetylneuraminate + beta-D-Gal-(1->4)-beta-D-GlcNAc-R
CMP + alpha-Neu5Ac-(2->3)-beta-D-Gal-(1->4)-beta-D-GlcNAc-R
CMP-N-acetyl-beta-neuraminate + 4-nitrophenyl beta-D-Gal-(1->4)-beta-D-GlcNAc-(1->3)-beta-D-Gal
CMP + 4-nitrophenyl alpha-Neu5Ac-(2->3)-beta-D-Gal-(1->4)-beta-D-GlcNAc-(1->3)-beta-D-Gal
conversion at 16.8% compared to activity with benzyl beta-D-Gal-(1->4)-beta-D-GlcNAc-(1->6)-[4-deoxy-4-fluoro-beta-D-Gal-(1->3)]-beta-D-GalNAc
-
-
?
CMP-N-acetyl-beta-neuraminate + 4-nitrophenyl beta-D-Gal-(1->4)-beta-D-GlcNAc-(1->3)-beta-D-Gal
CMP + 4-nitrophenyl alpha-Neu5Ac-(2->3)-beta-D-Gal-(1->4)-beta-D-GlcNAc-(1->3)-beta-D-Gal
conversion at 79.5% compared to activity with benzyl beta-D-Gal-(1->4)-beta-D-GlcNAc-(1->6)-[4-deoxy-4-fluoro-beta-D-Gal-(1->3)]-beta-D-GalNAc
-
-
?
CMP-N-acetyl-beta-neuraminate + 4-nitrophenyl beta-D-Gal-(1->4)-beta-D-GlcNAc-(1->3)-beta-D-Gal-(1->4)-beta-D-GlcNAc
CMP + 4-nitrophenyl alpha-Neu5Ac-(2->3)-beta-D-Gal-(1->4)-beta-D-GlcNAc-(1->3)-beta-D-Gal-(1->4)-beta-D-GlcNAc
conversion at 15.2% compared to activity with benzyl beta-D-Gal-(1->4)-beta-D-GlcNAc-(1->6)-[4-deoxy-4-fluoro-beta-D-Gal-(1->3)]-beta-D-GalNAc
-
-
?
CMP-N-acetyl-beta-neuraminate + 4-nitrophenyl beta-D-Gal-(1->4)-beta-D-GlcNAc-(1->3)-beta-D-Gal-(1->4)-beta-D-GlcNAc
CMP + 4-nitrophenyl alpha-Neu5Ac-(2->3)-beta-D-Gal-(1->4)-beta-D-GlcNAc-(1->3)-beta-D-Gal-(1->4)-beta-D-GlcNAc
conversion at 20.87% compared to activity with benzyl beta-D-Gal-(1->4)-beta-D-GlcNAc-(1->6)-[4-deoxy-4-fluoro-beta-D-Gal-(1->3)]-beta-D-GalNAc
-
-
?
CMP-N-acetyl-beta-neuraminate + benzyl beta-D-(3-O-Me)Gal-(1->4)-beta-D-GlcNAc-(1->6)-[beta-D-Gal-(1->3)]-alpha-D-GalNAc
CMP + benzyl alpha-Neu5Ac-(2->3)-beta-D-(3-O-Me)Gal-(1->4)-beta-D-GlcNAc-(1->6)-[beta-D-Gal-(1->3)]-alpha-D-GalNAc
-
4.5% of the activity compared to mucin core 2-based compound benzyl beta-D-Gal-(1->4)-beta-D-GlcNAc-(1->6)-beta-D-(3-O-Me)Gal-(1->3)-alpha-D-GalNAc, alpha2,3(N) sialyltransferase
-
-
?
CMP-N-acetyl-beta-neuraminate + benzyl beta-D-(3-O-Me)Gal-(1->4)-beta-D-GlcNAc-(1->6)-[beta-D-Gal-(1->3)]-alpha-D-GalNAc
CMP + benzyl alpha-Neu5Ac-(2->3)-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. 50.8% of the activity compared to ally beta-D-Gal-(1->4)-beta-D-GlcNAc, alpha2,3(N) sialyltransferase
-
-
?
CMP-N-acetyl-beta-neuraminate + benzyl beta-D-(4-O-Me)Gal-(1->4)-beta-D-GlcNAc
CMP + benzyl alpha-Neu5Ac-(2->3)-beta-D-(4-O-Me)Gal-(1->4)-beta-D-GlcNAc
conversion at 15.6% compared to activity with benzyl beta-D-Gal-(1->4)-beta-D-GlcNAc-(1->6)-[4-deoxy-4-fluoro-beta-D-Gal-(1->3)]-beta-D-GalNAc
-
-
?
CMP-N-acetyl-beta-neuraminate + benzyl beta-D-(4-O-Me)Gal-(1->4)-beta-D-GlcNAc
CMP + benzyl alpha-Neu5Ac-(2->3)-beta-D-(4-O-Me)Gal-(1->4)-beta-D-GlcNAc
conversion at 66.97% compared to activity with benzyl beta-D-Gal-(1->4)-beta-D-GlcNAc-(1->6)-[4-deoxy-4-fluoro-beta-D-Gal-(1->3)]-beta-D-GalNAc
-
-
?
CMP-N-acetyl-beta-neuraminate + benzyl beta-D-Gal-(1->4)-beta-D-GlcNAc-(1->6)-[beta-D-(3-O-Me)Gal-(1->3)]-alpha-D-GalNAc
CMP + benzyl alpha-Neu5Ac-(2->3)-beta-D-Gal-(1->4)-beta-D-GlcNAc-(1->6)-[beta-D-(3-O-Me)Gal-(1->3)]-alpha-D-GalNAc
-
49.6% of the activity compared to mucin core 2-based compound benzyl beta-D-(3-O-Me)Gal-(1->4)-beta-D-GlcNAc-(1->6)-[beta-D-Gal-(1->3)]-alpha-D-GalNAc, alpha2,3(N) sialyltransferase
-
-
?
CMP-N-acetyl-beta-neuraminate + benzyl beta-D-Gal-(1->4)-beta-D-GlcNAc-(1->6)-[beta-D-(3-O-Me)Gal-(1->3)]-alpha-D-GalNAc
CMP + benzyl alpha-Neu5Ac-(2->3)-beta-D-Gal-(1->4)-beta-D-GlcNAc-(1->6)-[beta-D-(3-O-Me)Gal-(1->3)]-alpha-D-GalNAc
-
95.3% of the activity compared to ally beta-D-Gal-(1->4)-beta-D-GlcNAc, alpha2,3(N) sialyltransferase. 49.6% 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
-
-
?
CMP-N-acetyl-beta-neuraminate + beta-D-Gal-(1->4)-alpha-D-Glc
CMP + alpha-Neu5Ac-(2->3)-beta-D-Gal-(1->4)-alpha-D-Glc
-
i.e. lactose
-
-
?
CMP-N-acetyl-beta-neuraminate + beta-D-Gal-(1->4)-alpha-D-Glc
CMP + alpha-Neu5Ac-(2->3)-beta-D-Gal-(1->4)-alpha-D-Glc
-
i.e. lactose
-
-
?
CMP-N-acetyl-beta-neuraminate + beta-D-Gal-(1->4)-alpha-D-Glc
CMP + alpha-Neu5Ac-(2->3)-beta-D-Gal-(1->4)-alpha-D-Glc
-
i.e. lactose
-
-
?
CMP-N-acetyl-beta-neuraminate + beta-D-Gal-(1->4)-beta-D-Glc
CMP + alpha-Neu5Ac-(2->3)-beta-D-Gal-(1->4)-beta-D-Glc
-
-
-
?
CMP-N-acetyl-beta-neuraminate + beta-D-Gal-(1->4)-beta-D-Glc
CMP + alpha-Neu5Ac-(2->3)-beta-D-Gal-(1->4)-beta-D-Glc
-
-
-
?
CMP-N-acetyl-beta-neuraminate + beta-D-Gal-(1->4)-beta-D-Glc
CMP + alpha-Neu5Ac-(2->3)-beta-D-Gal-(1->4)-beta-D-Glc
-
-
-
?
CMP-N-acetyl-beta-neuraminate + beta-D-Gal-(1->4)-beta-D-Glc
CMP + alpha-Neu5Ac-(2->3)-beta-D-Gal-(1->4)-beta-D-Glc
-
-
-
?
CMP-N-acetyl-beta-neuraminate + beta-D-Gal-(1->4)-beta-D-GlcNAc
CMP + alpha-Neu5Ac-(2->3)-beta-D-Gal-(1->4)-beta-D-GlcNAc
-
i.e. N-acetyllactosamine
-
-
?
CMP-N-acetyl-beta-neuraminate + beta-D-Gal-(1->4)-beta-D-GlcNAc
CMP + alpha-Neu5Ac-(2->3)-beta-D-Gal-(1->4)-beta-D-GlcNAc
-
i.e. N-acetyllactosamine
-
-
?
CMP-N-acetyl-beta-neuraminate + beta-D-Gal-(1->4)-beta-D-GlcNAc
CMP + alpha-Neu5Ac-(2->3)-beta-D-Gal-(1->4)-beta-D-GlcNAc
-
i.e. N-acetyllactosamine
-
-
?
CMP-N-acetyl-beta-neuraminate + beta-D-Gal-(1->4)-beta-D-GlcNAc
CMP + alpha-Neu5Ac-(2->3)-beta-D-Gal-(1->4)-beta-D-GlcNAc
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
-
-
?
CMP-N-acetyl-beta-neuraminate + beta-D-Gal-(1->4)-beta-D-GlcNAc
CMP + alpha-Neu5Ac-(2->3)-beta-D-Gal-(1->4)-beta-D-GlcNAc
relative Vmax is 4:2:1 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 as substrate, respectively
-
-
?
CMP-N-acetyl-beta-neuraminate + beta-D-Gal-(1->4)-beta-D-GlcNAc
CMP + alpha-Neu5Ac-(2->3)-beta-D-Gal-(1->4)-beta-D-GlcNAc
103% of the activity with beta-D-Gal-(1->4)-beta-D-Glc, truncated recombinant enzyme
-
-
?
CMP-N-acetyl-beta-neuraminate + beta-D-Gal-(1->4)-beta-D-GlcNAc
CMP + alpha-Neu5Ac-(2->3)-beta-D-Gal-(1->4)-beta-D-GlcNAc
103% of the activity with beta-D-Gal-(1->4)-beta-D-Glc, truncated recombinant enzyme
-
-
?
CMP-N-acetyl-beta-neuraminate + beta-D-Gal-(1->4)-beta-D-GlcNAc
CMP + alpha-Neu5Ac-(2->3)-beta-D-Gal-(1->4)-beta-D-GlcNAc
96% of the activity with beta-D-Gal-(1->4)-beta-D-Glc, recombinant enzyme
-
-
?
CMP-N-acetyl-beta-neuraminate + beta-D-Gal-(1->4)-beta-D-GlcNAc
CMP + alpha-Neu5Ac-(2->3)-beta-D-Gal-(1->4)-beta-D-GlcNAc
the recombinant enzyme transfers sialyl residues to beta-D-Gal-(1->3)-beta-D-GlcNAc as well as to beta-D-Gal-(1->4)-beta-D-GlcNAc partial structures in gangliosides
-
-
?
CMP-N-acetyl-beta-neuraminate + beta-D-Gal-(1->4)-beta-D-GlcNAc
CMP + alpha-Neu5Ac-(2->3)-beta-D-Gal-(1->4)-beta-D-GlcNAc
127% of the activity with beta-D-Gal-(1->4)-beta-D-Glc, recombinant enzyme
-
-
?
CMP-N-acetyl-beta-neuraminate + beta-D-Gal-(1->4)-beta-D-GlcNAc-R
CMP + alpha-Neu5Ac-(2->3)-beta-D-Gal-(1->4)-beta-D-GlcNAc-R
-
asialo-alpha1-acid glycoprotein
-
-
?
CMP-N-acetyl-beta-neuraminate + beta-D-Gal-(1->4)-beta-D-GlcNAc-R
CMP + alpha-Neu5Ac-(2->3)-beta-D-Gal-(1->4)-beta-D-GlcNAc-R
-
asialo-alpha1-acid glycoprotein
-
-
?
CMP-N-acetyl-beta-neuraminate + beta-D-Gal-(1->4)-beta-D-GlcNAc-R
CMP + alpha-Neu5Ac-(2->3)-beta-D-Gal-(1->4)-beta-D-GlcNAc-R
-
asialo-alpha1-acid glycoprotein
-
-
?
CMP-N-acetyl-beta-neuraminate + beta-D-Gal-(1->4)-beta-D-GlcNAc-R
CMP + alpha-Neu5Ac-(2->3)-beta-D-Gal-(1->4)-beta-D-GlcNAc-R
-
the enzyme prefers type 2 chain (Gal beta 1-4GlcNAc) over type 1 chain (Gal beta 1-3GlcNAc) acceptors. Oligosaccharides and glycopeptides are better acceptor substrates than glycoproteins. Of the branched oligosaccharides, those with a bisected N-acetylglucosamine (GlcNAc) structure appear to be poorer substrates, while triantennary structures containing a beta-D-Gal-(1->4)-beta-D-GlcNAc-(1->4)-alpha-Man-(1->3)-beta-D-Man branch are preferred
-
-
?
CMP-N-acetyl-beta-neuraminate + beta-D-mannopyranoside
CMP + alpha-Neu5Ac-(2->3)-beta-D-Man
43% of the activity with beta-D-Gal-(1->4)-beta-D-Glc, truncated recombinant enzyme
-
-
?
CMP-N-acetyl-beta-neuraminate + beta-D-mannopyranoside
CMP + alpha-Neu5Ac-(2->3)-beta-D-Man
43% of the activity with beta-D-Gal-(1->4)-beta-D-Glc, truncated recombinant enzyme
-
-
?
CMP-N-acetyl-beta-neuraminate + beta-D-N-acetylgalactosamine
CMP + alpha-Neu5Ac-(2->3)-beta-D-GalNAc
76% of the activity with beta-D-Gal-(1->4)-beta-D-Glc, recombinant enzyme
-
-
?
CMP-N-acetyl-beta-neuraminate + beta-D-N-acetylgalactosamine
CMP + alpha-Neu5Ac-(2->3)-beta-D-GalNAc
58% of the activity with beta-D-Gal-(1->4)-beta-D-Glc, recombinant enzyme
-
-
?
CMP-N-acetyl-beta-neuraminate + beta-D-N-acetylglucosamine
CMP + alpha-Neu5Ac-(2->3)-beta-D-GlcNAc
40% of the activity with beta-D-Gal-(1->4)-beta-D-Glc, truncated recombinant enzyme
-
-
?
CMP-N-acetyl-beta-neuraminate + beta-D-N-acetylglucosamine
CMP + alpha-Neu5Ac-(2->3)-beta-D-GlcNAc
40% of the activity with beta-D-Gal-(1->4)-beta-D-Glc, truncated recombinant enzyme
-
-
?
CMP-N-acetyl-beta-neuraminate + beta-D-N-acetylglucosamine
CMP + alpha-Neu5Ac-(2->3)-beta-D-GlcNAc
55% of the activity with beta-D-Gal-(1->4)-beta-D-Glc, recombinant enzyme
-
-
?
CMP-N-acetyl-beta-neuraminate + methyl beta-D-Gal-(1->3)-beta-D-GlcNAc
CMP + methyl alpha-Neu5Ac-(2->3)-beta-D-Gal-(1->4)-beta-D-GlcNAc
192% of the activity with beta-D-Gal-(1->4)-beta-D-Glc, recombinant enzyme
-
-
?
CMP-N-acetyl-beta-neuraminate + methyl beta-D-Gal-(1->3)-beta-D-GlcNAc
CMP + methyl alpha-Neu5Ac-(2->3)-beta-D-Gal-(1->4)-beta-D-GlcNAc
124% of the activity with beta-D-Gal-(1->4)-beta-D-Glc, recombinant enzyme
-
-
?
CMP-N-acetyl-beta-neuraminate + methyl beta-D-Gal-(1->4)-beta-D-GlcNAc
CMP + methyl alpha-Neu5Ac-(2->3)-beta-D-Gal-(1->4)-beta-D-GlcNAc
129% of the activity with beta-D-Gal-(1->4)-beta-D-Glc, truncated recombinant enzyme
-
-
?
CMP-N-acetyl-beta-neuraminate + methyl beta-D-Gal-(1->4)-beta-D-GlcNAc
CMP + methyl alpha-Neu5Ac-(2->3)-beta-D-Gal-(1->4)-beta-D-GlcNAc
129% of the activity with beta-D-Gal-(1->4)-beta-D-Glc, truncated recombinant enzyme
-
-
?
CMP-N-acetyl-beta-neuraminate + methyl beta-D-galactopyranoside
CMP + methyl alpha-Neu5Ac-(2->3)-beta-D-galactopyranoside
343% of the activity with beta-D-Gal-(1->4)-beta-D-Glc, recombinant enzyme
-
-
?
CMP-N-acetyl-beta-neuraminate + methyl beta-D-galactopyranoside
CMP + methyl alpha-Neu5Ac-(2->3)-beta-D-galactopyranoside
114% of the activity with beta-D-Gal-(1->4)-beta-D-Glc, recombinant enzyme
-
-
?
CMP-N-acetyl-beta-neuraminate + methyl beta-D-mannopyranoside
CMP + methyl alpha-Neu5Ac-(2->3)-beta-D-Man
63% of the activity with beta-D-Gal-(1->4)-beta-D-Glc, truncated recombinant enzyme
-
-
?
CMP-N-acetyl-beta-neuraminate + methyl beta-D-mannopyranoside
CMP + methyl alpha-Neu5Ac-(2->3)-beta-D-Man
57% of the activity with beta-D-Gal-(1->4)-beta-D-Glc, recombinant enzyme
-
-
?
CMP-N-acetylneuraminate + beta-D-Gal-(1->4)-beta-D-GalNAc-R
CMP + alpha-Neu5Ac-(2->3)-beta-D-Gal-(1->4)-beta-D-GalNAc-R
-
type II disaccharides are preferred substrates
-
-
?
CMP-N-acetylneuraminate + beta-D-Gal-(1->4)-beta-D-GalNAc-R
CMP + alpha-Neu5Ac-(2->3)-beta-D-Gal-(1->4)-beta-D-GalNAc-R
type II disaccharides are preferred substrates
-
-
?
CMP-N-acetylneuraminate + beta-D-Gal-(1->4)-beta-D-GlcNAc
CMP + alpha-Neu5Ac-(2->3)-beta-D-Gal-(1->4)-beta-D-GlcNAc
Q17WF9
-
-
-
?
CMP-N-acetylneuraminate + beta-D-Gal-(1->4)-beta-D-GlcNAc
CMP + alpha-Neu5Ac-(2->3)-beta-D-Gal-(1->4)-beta-D-GlcNAc
i.e. N-acetyllactosamine
-
-
?
CMP-N-acetylneuraminate + beta-D-Gal-(1->4)-beta-D-GlcNAc-R
CMP + alpha-Neu5Ac-(2->3)-beta-D-Gal-(1->4)-beta-D-GlcNAc-R
the alpha-2,3-sialyltransferase ST3Gal-IV can sialylate the type II glycan chains (beta-D-Gal-(1->4)-beta-D-GlcNAc) that are part of the glycan linkages of sialyl Lewis X
-
-
?
CMP-N-acetylneuraminate + beta-D-Gal-(1->4)-beta-D-GlcNAc-R
CMP + alpha-Neu5Ac-(2->3)-beta-D-Gal-(1->4)-beta-D-GlcNAc-R
broad substrate specificity, the viral enzyme utilizes disaccharides type I-III and also fucosylated Lewis a and Lewis x
-
-
?
CMP-N-acetylneuraminate + beta-D-Gal-(1->4)-beta-D-GlcNAc-R
CMP + alpha-Neu5Ac-(2->3)-beta-D-Gal-(1->4)-beta-D-GlcNAc-R
-
artificial glycopolypeptides carrying beta-D-Gal-(1->4)-beta-D-GlcNAc and beta-D-Gal-(1->4)-beta-D-Glc are further converted to alpha-Neu5Ac-(2->3)-beta-D-Gal-(1->4)-beta-D-GlcNAc and alpha-Neu5Ac-(2->3)-beta-D-Gal-(1->4)-beta-D-Glc sialyloligosaccharides
-
-
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
NaCl
NaCl
native and recombinant enzymes are twice as active in the presence of NaCl at 500, 750, and 1000 mM as in the absence of NaCl
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Adenocarcinoma
?2,3-sialyltransferase ST3Gal IV promotes migration and metastasis in pancreatic adenocarcinoma cells and tends to be highly expressed in pancreatic adenocarcinoma tissues.
Adenocarcinoma
alpha2,3-sialyltransferase ST3Gal III modulates pancreatic cancer cell motility and adhesion in vitro and enhances its metastatic potential in vivo.
Adenocarcinoma
Pancreatic cancer cell glycosylation regulates cell adhesion and invasion through the modulation of ?2?1 integrin and E-cadherin function.
Autoimmune Diseases
The expanding role of ?2-3 sialylation for leukocyte trafficking in vivo.
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.
Breast Neoplasms
Regulation of sialyltransferase expression by estradiol and 4-OH-tamoxifen in the human breast cancer cell MCF-7.
Breast Neoplasms
ST3Gal III modulates breast cancer cell adhesion and invasion by altering the expression of invasion-related molecules.
Carcinogenesis
Elevation of alpha2-->6 sialyltransferase and alpha1-->2 fucosyltransferase activities in human choriocarcinoma.
Carcinogenesis
Glycosyltransferase expression in human colonic tissue examined by oligonucleotide arrays.
Carcinoma
Altered mRNA expression of glycosyltransferases in human colorectal carcinomas and liver metastases.
Carcinoma
Altered mRNA expression of sialyltransferase in squamous cell carcinomas of the cervix.
Carcinoma
Characterization of two glycolipid: alpha 2-3sialyltransferases, SAT-3 (CMP-NeuAc:nLcOse4Cer alpha 2-3sialyltransferase) and SAT-4 (CMP-NeuAc:GgOse4Cer alpha 2-3sialyltransferase), from human colon carcinoma (Colo 205) cell line.
Carcinoma
Cloning and expression of SAT-3 involved in SA-Le(x) biosynthesis: inhibition studies with polyclonal antibody against GST-SAT-3 fusion protein.
Carcinoma
DNA hypermethylation contributes to incomplete synthesis of carbohydrate determinants in gastrointestinal cancer.
Carcinoma
Expression of sialyltransferase family members in cervix squamous cell carcinoma correlates with lymph node metastasis.
Carcinoma
Expression of ST3GAL4 leads to SLe(x) expression and induces c-Met activation and an invasive phenotype in gastric carcinoma cells.
Carcinoma, Hepatocellular
Differences in CD75s- and iso-CD75s-ganglioside content and altered mRNA expression of sialyltransferases ST6GAL1 and ST3GAL6 in human hepatocellular carcinomas and nontumoral liver tissues.
Carcinoma, Hepatocellular
Interleukin-1beta induces sialyl Lewis X on hepatocellular carcinoma HuH-7 cells via enhanced expression of ST3Gal IV and FUT VI gene.
Carcinoma, Hepatocellular
Sialyltransferase ST3GAL6 mediates the effect of microRNA-26a on cell growth, migration, and invasion in hepatocellular carcinoma through the protein kinase B/mammalian target of rapamycin pathway.
Carcinoma, Renal Cell
Clinical significance of ST3Gal IV expression in human renal cell carcinoma.
Carcinoma, Squamous Cell
Altered mRNA expression of sialyltransferase in squamous cell carcinomas of the cervix.
Carcinoma, Squamous Cell
Expression of sialyltransferase family members in cervix squamous cell carcinoma correlates with lymph node metastasis.
Colorectal Neoplasms
Up-regulation of a set of glycosyltransferase genes in human colorectal cancer.
Epilepsy, Temporal Lobe
Sialyltransferase ST3Gal IV deletion protects against temporal lobe epilepsy.
Hypertension, Pulmonary
Multiplex reverse transcription polymerase chain reaction assessment of sialyltransferase expression in peripheral blood mononuclear cells in systemic sclerosis.
Influenza in Birds
The expression pattern and histological distribution of sialyltransferases ST3Gal III in yellow chicken.
Intellectual Disability
ST3GAL3 mutations impair the development of higher cognitive functions.
Leukemia
UDP-GlcNAc:Galbeta1-->3GalNAc (GlcNAc to GalNAc) beta1-->6N-acetylglucosaminyltransferase holds a key role on the control of CD15s expression in human pre-B lymphoid cell lines.
Leukemia, Myelogenous, Chronic, BCR-ABL Positive
Downregulation of miR-224 and let-7i contribute to cell survival and chemoresistance in chronic myeloid leukemia cells by regulating ST3GAL IV expression.
Melanoma
Characterization of two glycolipid: alpha 2-3sialyltransferases, SAT-3 (CMP-NeuAc:nLcOse4Cer alpha 2-3sialyltransferase) and SAT-4 (CMP-NeuAc:GgOse4Cer alpha 2-3sialyltransferase), from human colon carcinoma (Colo 205) cell line.
Melanoma
Molecular cloning of a novel alpha2,3-sialyltransferase (ST3Gal VI) that sialylates type II lactosamine structures on glycoproteins and glycolipids.
Multiple Myeloma
The sialyltransferase ST3GAL6 influences homing and survival in multiple myeloma.
n-acetyllactosaminide alpha-2,3-sialyltransferase deficiency
A patient-specific induced pluripotent stem cell model for West syndrome caused by ST3GAL3 deficiency.
n-acetyllactosaminide alpha-2,3-sialyltransferase deficiency
Sialyltransferase ST3Gal-IV operates as a dominant modifier of hemostasis by concealing asialoglycoprotein receptor ligands.
n-acetyllactosaminide alpha-2,3-sialyltransferase deficiency
West syndrome caused by ST3Gal-III deficiency.
Neoplasm Metastasis
?2,3-sialyltransferase ST3Gal IV promotes migration and metastasis in pancreatic adenocarcinoma cells and tends to be highly expressed in pancreatic adenocarcinoma tissues.
Neoplasm Metastasis
alpha2,3-sialyltransferase ST3Gal III modulates pancreatic cancer cell motility and adhesion in vitro and enhances its metastatic potential in vivo.
Neoplasm Metastasis
Correlation of glycosyltransferases mRNA expression in extrahepatic bile duct carcinoma with clinical pathological characteristics.
Neoplasm Metastasis
Expression of sialyltransferase family members in cervix squamous cell carcinoma correlates with lymph node metastasis.
Neoplasm Metastasis
Glycosyltransferase expression in human colonic tissue examined by oligonucleotide arrays.
Neoplasms
?2,3-sialyltransferase ST3Gal IV promotes migration and metastasis in pancreatic adenocarcinoma cells and tends to be highly expressed in pancreatic adenocarcinoma tissues.
Neoplasms
Alpha2,3-sialyltransferase III knockdown sensitized ovarian cancer cells to cisplatin-induced apoptosis.
Neoplasms
alpha2,3-sialyltransferase ST3Gal III modulates pancreatic cancer cell motility and adhesion in vitro and enhances its metastatic potential in vivo.
Neoplasms
Altered mRNA expression of glycosyltransferases in human colorectal carcinomas and liver metastases.
Neoplasms
Clinical relevance of sialyltransferases ST6GAL-I and ST3GAL-III in gastric cancer.
Neoplasms
Correlation between Heterogeneous Expression of Sialyltransferases and MUC16 in Ovarian Tumor Tissues.
Neoplasms
Correlation of glycosyltransferases mRNA expression in extrahepatic bile duct carcinoma with clinical pathological characteristics.
Neoplasms
Differences in CD75s- and iso-CD75s-ganglioside content and altered mRNA expression of sialyltransferases ST6GAL1 and ST3GAL6 in human hepatocellular carcinomas and nontumoral liver tissues.
Neoplasms
Expression of ST3GAL4 leads to SLe(x) expression and induces c-Met activation and an invasive phenotype in gastric carcinoma cells.
Neoplasms
Glycosyltransferases as marker genes for the quantitative polymerase chain reaction-based detection of circulating tumour cells from blood samples of patients with breast cancer undergoing adjuvant therapy.
Neoplasms
Hypoxia and serum deprivation induces glycan alterations in triple negative breast cancer cells.
Neoplasms
LncRNA ST3Gal6-AS1/ST3Gal6 axis mediates colorectal cancer progression by regulating ?-2,3 sialylation via PI3K/Akt signaling.
Neoplasms
Multiplex reverse transcription polymerase chain reaction assessment of sialyltransferase expression in human breast cancer.
Neoplasms
Pancreatic cancer cell glycosylation regulates cell adhesion and invasion through the modulation of ?2?1 integrin and E-cadherin function.
Neoplasms
Prognostic value of tumoral sialyltransferase expression and circulating E-selectin concentrations in node-negative breast cancer patients.
Neoplasms
Pseudomonas aeruginosa pyocyanin modulates mucin glycosylation with sialyl-Lewis(x) to increase binding to airway epithelial cells.
Neoplasms
Sialyltransferase ST3GAL6 mediates the effect of microRNA-26a on cell growth, migration, and invasion in hepatocellular carcinoma through the protein kinase B/mammalian target of rapamycin pathway.
Neoplasms
The PRMT5/WDR77 complex regulates alternative splicing through ZNF326 in breast cancer.
Neoplasms
The sialyltransferase ST3GAL6 influences homing and survival in multiple myeloma.
Neoplasms
Unexpected distribution of CA19.9 and other type 1 chain Lewis antigens in normal and cancer tissues of colon and pancreas: Importance of the detection method and role of glycosyltransferase regulation.
Ovarian Neoplasms
Alpha2,3-sialyltransferase III knockdown sensitized ovarian cancer cells to cisplatin-induced apoptosis.
Ovarian Neoplasms
Correlation between Heterogeneous Expression of Sialyltransferases and MUC16 in Ovarian Tumor Tissues.
Pancreatic Neoplasms
alpha2,3-sialyltransferase ST3Gal III modulates pancreatic cancer cell motility and adhesion in vitro and enhances its metastatic potential in vivo.
Pneumonia
Sialyltransferase ST3Gal-III regulates Siglec-F ligand formation and eosinophilic lung inflammation in mice.
Prostatic Neoplasms
Analysis of the specificity of sialyltransferases toward mucin core 2, globo, and related structures. identification of the sialylation sequence and the effects of sulfate, fucose, methyl, and fluoro substituents of the carbohydrate chain in the biosynthesis of selectin and siglec ligands, and novel sialylation by cloned alpha2,3(O)sialyltransferase.
Seizures
Differential expression of mRNAs for sialyltransferase isoenzymes induced in the hippocampus of mouse following kindled seizures.
Spasms, Infantile
A patient-specific induced pluripotent stem cell model for West syndrome caused by ST3GAL3 deficiency.
Stomach Neoplasms
Altered mRNA expressions of sialyltransferases in human gastric cancer tissues.
Stomach Neoplasms
Clinical relevance of sialyltransferases ST6GAL-I and ST3GAL-III in gastric cancer.
Stomach Neoplasms
DNA hypermethylation contributes to incomplete synthesis of carbohydrate determinants in gastrointestinal cancer.
Thrombocytopenia
Sialyltransferase ST3Gal-IV operates as a dominant modifier of hemostasis by concealing asialoglycoprotein receptor ligands.
Uterine Cervical Neoplasms
Altered mRNA expression of sialyltransferase in squamous cell carcinomas of the cervix.
Uterine Cervical Neoplasms
Expression of sialyltransferase family members in cervix squamous cell carcinoma correlates with lymph node metastasis.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.11
8-methoxy-8-oxooctyl beta-D-Gal-(1->4)-beta-D-GlcNAc
pH and temperature not specified in the publication
0.5
beta-D-Gal-(1->4)-beta-D-GlcNAc-(1->3)-beta-D-Gal-(1->4)-beta-D-Glc-(1<->1)-ceramide
-
pH 6.4, 37°C
-
0.1085
FCHASE beta-D-Gal-(1->4)-beta-D-GlcNAc
-
pH and temperature not specified in the publication
0.79
4-methylumbelliferyl beta-lactoside
mutant enzyme M144H, in Tris-HCl buffer (200 mM, pH 8.5), at 37°C
1.4
4-methylumbelliferyl beta-lactoside
wild type enzyme, in Tris-HCl buffer (200 mM, pH 8.5), at 37°C
12
4-methylumbelliferyl beta-lactoside
mutant enzyme M144D, in Tris-HCl buffer (200 mM, pH 8.5), at 37°C
8.1
4-methylumbelliferyl beta-Lewis x
mutant enzyme M144H, in Tris-HCl buffer (200 mM, pH 8.5), at 37°C
13
4-methylumbelliferyl beta-Lewis x
mutant enzyme M144D, in Tris-HCl buffer (200 mM, pH 8.5), at 37°C
17
4-methylumbelliferyl beta-Lewis x
wild type enzyme, in Tris-HCl buffer (200 mM, pH 8.5), at 37°C
0.14
4-nitrophenyl beta-D-Gal-(1->4)-beta-D-GlcNAc-(1->3)-beta-D-Gal
pH and temperature not specified in the publication
0.83
4-nitrophenyl beta-D-Gal-(1->4)-beta-D-GlcNAc-(1->3)-beta-D-Gal
pH and temperature not specified in the publication
0.08761
beta-D-Gal-(1->4)-beta-D-GlcNAc
pH and temperature not specified in the publication
0.1255
CMP-N-acetyl-beta-neuraminate
-
pH and temperature not specified in the publication
0.3
CMP-N-acetyl-beta-neuraminate
mutant enzyme M144D, using 4-methylumbelliferyl beta-lactoside as cosubstrate, in Tris-HCl buffer (200 mM, pH 8.5), at 37°C
0.39
CMP-N-acetyl-beta-neuraminate
wild type enzyme, using 4-methylumbelliferyl beta-Lewis x as cosubstrate, in Tris-HCl buffer (200 mM, pH 8.5), at 37°C
0.4
CMP-N-acetyl-beta-neuraminate
mutant enzyme M144H, using 4-methylumbelliferyl beta-Lewis x as cosubstrate, in Tris-HCl buffer (200 mM, pH 8.5), at 37°C
0.44
CMP-N-acetyl-beta-neuraminate
wild type enzyme, using 4-methylumbelliferyl beta-lactoside as cosubstrate, in Tris-HCl buffer (200 mM, pH 8.5), at 37°C
0.81
CMP-N-acetyl-beta-neuraminate
mutant enzyme M144H, using 4-methylumbelliferyl beta-lactoside as cosubstrate, in Tris-HCl buffer (200 mM, pH 8.5), at 37°C
1.4
CMP-N-acetyl-beta-neuraminate
mutant enzyme D141A, in Tris-HCl buffer (200 mM, pH 8.5), at 37°C
1.5
CMP-N-acetyl-beta-neuraminate
wild type enzyme, in Tris-HCl buffer (200 mM, pH 8.5), at 37°C
1.8
CMP-N-acetyl-beta-neuraminate
mutant enzyme H311A, in Tris-HCl buffer (200 mM, pH 8.5), at 37°C
2.1
CMP-N-acetyl-beta-neuraminate
mutant enzyme M144D, using 4-methylumbelliferyl beta-Lewis x as cosubstrate, in Tris-HCl buffer (200 mM, pH 8.5), at 37°C
7.3
CMP-N-acetyl-beta-neuraminate
mutant enzyme M144D, in Tris-HCl buffer (200 mM, pH 8.5), at 37°C
13
CMP-N-acetyl-beta-neuraminate
mutant enzyme M144H, in Tris-HCl buffer (200 mM, pH 8.5), at 37°C
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
21
4-methylumbelliferyl beta-lactoside
mutant enzyme M144H, in Tris-HCl buffer (200 mM, pH 8.5), at 37°C
22
4-methylumbelliferyl beta-lactoside
mutant enzyme M144D, in Tris-HCl buffer (200 mM, pH 8.5), at 37°C
47
4-methylumbelliferyl beta-lactoside
wild type enzyme, in Tris-HCl buffer (200 mM, pH 8.5), at 37°C
4
4-methylumbelliferyl beta-Lewis x
mutant enzyme M144D, in Tris-HCl buffer (200 mM, pH 8.5), at 37°C
6.7
4-methylumbelliferyl beta-Lewis x
wild type enzyme, in Tris-HCl buffer (200 mM, pH 8.5), at 37°C
8.4
4-methylumbelliferyl beta-Lewis x
mutant enzyme M144H, in Tris-HCl buffer (200 mM, pH 8.5), at 37°C
0.025
CMP-N-acetyl-beta-neuraminate
mutant enzyme D141A, in Tris-HCl buffer (200 mM, pH 8.5), at 37°C
0.55
CMP-N-acetyl-beta-neuraminate
wild type enzyme, using 4-methylumbelliferyl beta-Lewis x as cosubstrate, in Tris-HCl buffer (200 mM, pH 8.5), at 37°C
0.59
CMP-N-acetyl-beta-neuraminate
mutant enzyme M144D, using 4-methylumbelliferyl beta-Lewis x as cosubstrate, in Tris-HCl buffer (200 mM, pH 8.5), at 37°C
0.93
CMP-N-acetyl-beta-neuraminate
mutant enzyme M144H, using 4-methylumbelliferyl beta-Lewis x as cosubstrate, in Tris-HCl buffer (200 mM, pH 8.5), at 37°C
1.9
CMP-N-acetyl-beta-neuraminate
mutant enzyme M144D, using 4-methylumbelliferyl beta-lactoside as cosubstrate, in Tris-HCl buffer (200 mM, pH 8.5), at 37°C
2.1
CMP-N-acetyl-beta-neuraminate
mutant enzyme H311A, in Tris-HCl buffer (200 mM, pH 8.5), at 37°C
6.5
CMP-N-acetyl-beta-neuraminate
mutant enzyme M144D, in Tris-HCl buffer (200 mM, pH 8.5), at 37°C
21
CMP-N-acetyl-beta-neuraminate
mutant enzyme M144H, using 4-methylumbelliferyl beta-lactoside as cosubstrate, in Tris-HCl buffer (200 mM, pH 8.5), at 37°C
27
CMP-N-acetyl-beta-neuraminate
wild type enzyme, in Tris-HCl buffer (200 mM, pH 8.5), at 37°C
32
CMP-N-acetyl-beta-neuraminate
wild type enzyme, using 4-methylumbelliferyl beta-lactoside as cosubstrate, in Tris-HCl buffer (200 mM, pH 8.5), at 37°C
71
CMP-N-acetyl-beta-neuraminate
mutant enzyme M144H, in Tris-HCl buffer (200 mM, pH 8.5), at 37°C
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1.9
4-methylumbelliferyl beta-lactoside
mutant enzyme M144D, in Tris-HCl buffer (200 mM, pH 8.5), at 37°C
27
4-methylumbelliferyl beta-lactoside
mutant enzyme M144H, in Tris-HCl buffer (200 mM, pH 8.5), at 37°C
34
4-methylumbelliferyl beta-lactoside
wild type enzyme, in Tris-HCl buffer (200 mM, pH 8.5), at 37°C
0.32
4-methylumbelliferyl beta-Lewis x
mutant enzyme M144D, in Tris-HCl buffer (200 mM, pH 8.5), at 37°C
0.38
4-methylumbelliferyl beta-Lewis x
wild type enzyme, in Tris-HCl buffer (200 mM, pH 8.5), at 37°C
1
4-methylumbelliferyl beta-Lewis x
mutant enzyme M144H, in Tris-HCl buffer (200 mM, pH 8.5), at 37°C
0.018
CMP-N-acetyl-beta-neuraminate
mutant enzyme D141A, in Tris-HCl buffer (200 mM, pH 8.5), at 37°C
0.28
CMP-N-acetyl-beta-neuraminate
mutant enzyme M144D, using 4-methylumbelliferyl beta-Lewis x as cosubstrate, in Tris-HCl buffer (200 mM, pH 8.5), at 37°C
0.89
CMP-N-acetyl-beta-neuraminate
mutant enzyme M144D, in Tris-HCl buffer (200 mM, pH 8.5), at 37°C
1.1
CMP-N-acetyl-beta-neuraminate
mutant enzyme H311A, in Tris-HCl buffer (200 mM, pH 8.5), at 37°C
1.4
CMP-N-acetyl-beta-neuraminate
wild type enzyme, using 4-methylumbelliferyl beta-Lewis x as cosubstrate, in Tris-HCl buffer (200 mM, pH 8.5), at 37°C
2.2
CMP-N-acetyl-beta-neuraminate
mutant enzyme M144H, using 4-methylumbelliferyl beta-Lewis x as cosubstrate, in Tris-HCl buffer (200 mM, pH 8.5), at 37°C
5.5
CMP-N-acetyl-beta-neuraminate
mutant enzyme M144H, in Tris-HCl buffer (200 mM, pH 8.5), at 37°C
6.1
CMP-N-acetyl-beta-neuraminate
mutant enzyme M144D, using 4-methylumbelliferyl beta-lactoside as cosubstrate, in Tris-HCl buffer (200 mM, pH 8.5), at 37°C
18
CMP-N-acetyl-beta-neuraminate
wild type enzyme, in Tris-HCl buffer (200 mM, pH 8.5), at 37°C
27
CMP-N-acetyl-beta-neuraminate
mutant enzyme M144H, using 4-methylumbelliferyl beta-lactoside as cosubstrate, in Tris-HCl buffer (200 mM, pH 8.5), at 37°C
73
CMP-N-acetyl-beta-neuraminate
wild type enzyme, using 4-methylumbelliferyl beta-lactoside as cosubstrate, in Tris-HCl buffer (200 mM, pH 8.5), at 37°C
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5 - 5.5
6.8
5 - 5.5
native enzyme and the full-length recombinant enzyme
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5 - 11
active between pH 5.0 and pH 11.0, native enzyme and recombinant enzyme
5 - 9
pH 5: about 40% of maximal activity, pH 9: about 60% of maximal actzivity
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
20 - 25
native enzyme and the full-length recombinant enzyme
25 - 30
37
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
10 - 30
10°C: 65% of maximal activity, 30°C: 80% of maximal activity
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
Capan-1 cell, Panc-1 cell, MDAPanc-3 cell, Capan-1 cell. The level of the ST3Gal III transcripts can not be associated with the degree of differentiation of the tumours from which the cell lines are derived
brenda
-
from peripheral blood mononuclear cells, enzyme level stimulated by phytohemagglutinin
brenda
A0A1D5NU03, F1NQP1
the expression level of ST3Gal6 in the magnum of the oviduct is almost a half that in the liver
brenda
-
normal pancreas has around 40% less quantity of ST3Gal IV transcript compared to the positive tumour cell lines. The level of the ST3Gal III transcripts can not be associated with the degree of differentiation of the tumours from which the cell lines are derived
brenda
-
restricted expression: moderate in several thalamic nuclei and cerebellar Purkinje cell layer; widespread expression: high in olfactory bulb, hippocampal formation, red nuclei, pontine nuclei, and cerebellar Purkinje cell layer
brenda
-
recombinant enzyme expressed in Spodoptera frugiperda cells
brenda
A0A1D5NU03, F1NQP1
; expression of chicken ST3Gal3 is generally low in all the organs tested, although a certain level of expression is observed with ST3Gal3 in the liver
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
metabolism
physiological function
malfunction
-
enzyme-deficient mice display reduced leukocyte adhesion in trauma-stimulated cremaster muscle venules, reduced induction of leukocyte arrest in cremaster muscle venules after systemic injection of CXCR2 chemokines CXCL1 and CXCL8, reduced leukocyte extravasation into inflamed cremaster muscle tissue, and reduced leukocyte extravasation in the thioglycollate-induced peritonitis model
malfunction
-
absence of both alpha-2,3-sialyltransferase ST3Gal-VI and alpha-2,3-sialyltransferase ST3Gal-IV results in total loss of E-selectin ligands but incomplete loss of P-selectin ligands. Loss of ST3Gal-VI and ST3Gal-IV leads to reduced cellularity of secondary lymphatic tissue
metabolism
-
alpha-2,3-sialyltransferase ST3Gal-VI and alpha-2,3-sialyltransferase ST3Gal-IV participate in leukocyte sialylation. ST3Gal-IV and -VI contribute to leukocyte rolling during inflammation. ST3Gal-IV and ST3Gal-VI have a critical role in neutrophil, but not in monocyte, recruitment during inflammation. ST3Gal-VI and ST3Gal-IV have a critical role in L-selectin ligand synthesis in high endothelial venules. ST3Gal-VI and ST3Gal-IV regulate lymphocyte homing to lymph nodes and Peyer patches in vivo. Coordinated participation of both alpha-2,3-sialyltransferase ST3Gal-VI and alpha-2,3-sialyltransferase ST3Gal-IV in the synthesis of functional selectin ligands
physiological function
-
the enzyme significantly influences chemokine-triggered firmleukocyte arrest. The enzyme mediates reduced E-selectin-dependent rolling and increased E-selectin-mediated rolling velocity in inflamed cremaster muscle venules
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
LST_HAEIN
Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)
304
0
35706
Swiss-Prot
LST_NEIMA
Neisseria meningitidis serogroup A / serotype 4A (strain Z2491)
371
1
42554
Swiss-Prot
LST_NEIMB
Neisseria meningitidis serogroup B (strain MC58)
371
1
42611
Swiss-Prot
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PDB
SCOP
CATH
UNIPROT
ORGANISM
Neisseria meningitidis serogroup B (strain MC58)
Neisseria meningitidis serogroup B (strain MC58)
Neisseria meningitidis serogroup B (strain MC58)
Neisseria meningitidis serogroup B (strain MC58)
Neisseria meningitidis serogroup B (strain MC58)
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
43921
MALDI-TOF of truncated enzyme with N-terminal Lys2 to Cys22 deletion
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
?
x * 43921, MALDI-TOF of truncated enzyme with N-terminal Lys2 to Cys22 deletion
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
D141A
the mutation results in 1000fold decrease in the efficiency of alpha2-3-sialyltransferase activity
E271F/R313Y
the mutant does not efficiently sialylate fucose-containing oligosaccharides such as Lex
H311A
the mutation results in 16fold decrease in the efficiency of alpha2-3-sialyltransferase activity
M144D
the mutant shows 20000fold decreased donor hydrolysis activity without significantly affecting its alpha2-3-sialylation activity when a poor fucose-containing acceptor substrate is used
M144H
the mutation results in 3fold decrease in the efficiency of alpha2-3-sialyltransferase activity
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
4°C, partially purified enzyme preparation in 20% (v/v) glycerol, at least 1 week
-
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PURIFICATION/commentary
ORGANISM
UNIPROT
LITERATURE
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CLONED/commentary
ORGANISM
UNIPROT
LITERATURE
expressed in Chinese hamster ovary (CHO) and human embryonic kidney (HEK293T) cells with a C-terminal human Fc and His-tag; expressed in Chinese hamster ovary (CHO) and human embryonic kidney (HEK293T) cells with a C-terminal human Fc and His-tag
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
-
expression of full-length and truncated protein in Escherichia coli
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
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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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
-
the enzyme is a drug target for modulating leukocyte trafficking in human disorders, including autoimmune diseases and cancer
synthesis
synthesis
-
the enzyme is useful for chemoenzymatic synthesis of artificial glycopolypeptides containing multivalent sialyloligosaccharides with a gamma-polyglutamic acid backbone. These sialyloligosaccharides are effective in inhibition of infections of cells by influenza viruses, which bind preferentially to alpha2,3-linked Neu5Ac
synthesis
-
enzymatic synthesis of 4-methylumbelliferyl derivatives of N-acetyllactosaminide and sialyl N-acetyllactosaminides from 4-methylumbelliferyl N-acetyl-beta-D-glucosaminide by beta-galactosidase and sialyltransferase. The fluorescent synthesized compounds are useful for the assay of neuraminidase, sialyltransferase, and fucosyltransferase
synthesis
-
chemical-enzymatic synthesis of sialyl-Lewis x-containing hexasaccharides found on O-linked glycoproteins, process involves several enzymes of the pathway
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Sugiarto, G.; Lau, K.; Qu, J.; Li, Y.; Lim, S.; Mu, S.; Ames, J.B.; Fisher, A.J.; Chen, X.
A sialyltransferase mutant with decreased donor hydrolysis and reduced sialidase activities for directly sialylating Lewisx
ACS Chem. Biol.
7
1232-1240
2012
Pasteurella multocida, Pasteurella multocida (Q15KI8)
brenda
Sperandio, M.
The expanding role of alpha2-3 sialylation for leukocyte trafficking in vivo
Ann. N. Y. Acad. Sci.
1253
201-205
2012
Mus musculus
brenda
Gupta, R.; Matta, K.L.; Neelamegham, S.
A systematic analysis of acceptor specificity and reaction kinetics of five human alpha(2,3)sialyltransferases Product inhibition studies illustrate reaction mechanism for ST3Gal-I
Biochem. Biophys. Res. Commun.
469
606-612
2016
Homo sapiens, Homo sapiens (Q11203), Homo sapiens (Q11206)
brenda
Basu, S.K.; Whisler, R.L.; Yates, A.J.
Effects of lectin activation on sialyltransferase activities in human lymphocytes
Biochemistry
25
2577-2581
1986
Homo sapiens
brenda
Chandrasekaran, E.V.; Xue, J.; Xia, J.; Chawda, R.; Piskorz, C.; Locke, R.D.; Neelamegham, S.; Matta, K.L.
Analysis of the specificity of sialyltransferases toward mucin core 2, globo, and related structures. Identification of the sialylation sequence and the effects of sulfate, fucose, methyl, and fluoro substituents of the carbohydrate chain in the biosynthesis of selectin and siglec ligands, and novel sialylation by cloned alpha2,3(O)sialyltransferase
Biochemistry
44
15619-15635
2005
Rattus norvegicus
brenda
Bauvois, B.; Montreuil, J.; Verbert, A.
Characterization of a sialyl alpha 2-3 transferase and a sialyl alpha 2-6 transferase from human platelets occurring in the sialylation of the N-glycosylproteins
Biochim. Biophys. Acta
788
234-240
1984
Homo sapiens
brenda
Ogata, M.; Murata, T.; Murakami, K.; Suzuki, T.; Hidari, K.I.; Suzuki, Y.; Usui, T.
Chemoenzymatic synthesis of artificial glycopolypeptides containing multivalent sialyloligosaccharides with a gamma-polyglutamic acid backbone and their effect on inhibition of infection by influenza viruses
Bioorg. Med. Chem.
15
1383-1393
2007
Rattus norvegicus
brenda
Zeng, X.; Sun, Y.; Uzawa, H.
Efficient enzymatic synthesis of 4-methylumbelliferyl N-acetyllactosaminide and 4-methylumbelliferyl sialyl N-acetyllactosaminides employing beta-D-galactosidase and sialyltransferases
Biotechnol. Lett.
27
1461-1465
2005
Rattus norvegicus
brenda
Yang, W.H.; Nussbaum, C.; Grewal, P.K.; Marth, J.D.; Sperandio, M.
Coordinated roles of ST3Gal-VI and ST3Gal-IV sialyltransferases in the synthesis of selectin ligands
Blood
120
1015-1026
2012
Mus musculus (Q91Y74)
brenda
Oehrlein, R.; Hindsgaul, O.; Palcic, M.M.
Use of the core-2-N-acetylglucosaminyltransferase in the chemical-enzymic synthesis of a sialyl-LeX-containing hexasaccharide found on O-linked glycoproteins
Carbohydr. Res.
244
149-159
1993
Rattus norvegicus
brenda
Nemansky, M.; Schiphorst, W.E.C.M.; Koeleman, C.A.M.; Van den Eijnden, D.H.
Human liver and human placenta both contain CMP-NeuAcGal beta 1->4GlcNAc-R alpha 2->3- as well as alpha 2->6-sialyltransferase activity
FEBS Lett.
312
31-36
1992
Homo sapiens
brenda
Sujino, K.; Jackson, R.J.; Chan, N.W.C.; Tsuji, S.; Palcic, M.M.
A novel viral alpha2,3-sialyltransferase (v-ST3Gal I) transfer of sialic acid to fucosylated acceptors
Glycobiology
10
313-320
2000
myxoma virus, myxoma virus (Q9YJT3)
brenda
Schur, M.J.; Lameignere, E.; Strynadka, N.C.; Wakarchuk, W.W.
Characterization of alpha2,3- and alpha2,6-sialyltransferases from Helicobacter acinonychis
Glycobiology
22
997-1006
2012
Helicobacter acinonychis, Helicobacter acinonychis (Q17WF9)
brenda
Kono, M.; Ohyama, Y.; Lee, Y.C.; Hamamoto, T.; Kojima, N.; Tsuji, S.
Mouse beta-galactoside alpha2,3-sialyltransferases comparison of in vitro substrate specificities and tissue specific expression
Glycobiology
7
469-479
1997
Mus musculus, Mus musculus (P97325), Mus musculus (Q91Y74)
brenda
Peracaula, R.; Tabares, G.; Lopez-Ferrer, A.; Brossmer, R.; de Bolos, C.; de Llorens, R.
Role of sialyltransferases involved in the biosynthesis of Lewis antigens in human pancreatic tumour cells
Glycoconj. J.
22
135-144
2005
Homo sapiens, Homo sapiens (Q11206)
brenda
Nemansky, M.; Van den Eijnden, D.H.
Enzymic characterization of CMP-NeuAcGal-beta-1,4GlcNAc-R alpha(2,3)-sialyltransferase from human placenta
Glycoconjugate J.
10
99-108
1993
Homo sapiens
brenda
Kondadi, P.K.; Rossi, M.; Twelkmeyer, B.; Schur, M.J.; Li, J.; Schott, T.; Paulin, L.; Auvinen, P.; Haenninen, M.L.; Schweda, E.K.; Wakarchuk, W.
Identification and characterization of a lipopolysaccharide alpha,2,3-sialyltransferase from the human pathogen Helicobacter bizzozeronii
J. Bacteriol.
194
2540-2550
2012
Helicobacter bizzozeronii
brenda
Takakura, Y.; Tsukamoto, H.; Yamamoto, T.
Molecular cloning, expression and properties of an alpha/beta-galactoside alpha2,3-sialyltransferase from Vibrio sp. JT-FAJ-16
J. Biochem.
142
403-412
2007
Vibrio sp. JT-FAJ-16 (A8R0Y0)
brenda
Tsukamoto, H.; Takakura, Y.; Mine, T.; Yamamoto, T.
Photobacterium sp. JT-ISH-224 produces two sialyltransferases, alpha-/beta-galactoside alpha2,3-sialyltransferase and beta-galactoside alpha2,6-sialyltransferase
J. Biochem.
143
187-197
2008
Photobacterium sp. JT-ISH-224 (A8QYL0)
brenda
Van den Eijnden, D.H.; Schiphorst, W.E.C.M.
Detection of beta-galactosyl(1->4)N-acetylglucosaminide alpha(2->3)-sialyltransferase activity in fetal calf liver and other tissues
J. Biol. Chem.
256
3159-3162
1981
Bos taurus, Gallus gallus, Homo sapiens
brenda
Basu, M.; Basu, S.; Stoffyn, A.; Stoffyn, P.
Biosynthesis in vitro of sialyl(alpha 2-3)neolactotetraosylceramide by a sialyltransferase from embryonic chicken brain
J. Biol. Chem.
257
12765-12769
1982
Gallus gallus
brenda
Tsukamoto, H.; Takakura, Y.; Yamamoto, T.
Purification, cloning, and expression of an alpha/beta-galactoside alpha-2,3-sialyltransferase from a luminous marine bacterium, Photobacterium phosphoreum
J. Biol. Chem.
282
29794-29802
2007
Photobacterium phosphoreum (A5LHX0), Photobacterium phosphoreum JT-ISH-467 (A5LHX0)
brenda
Kojima, Y.; Mizutani, A.; Okuzaki, Y.; Nishijima, K.; Kaneoka, H.; Sasamoto, T.; Miyake, K.; Iijima, S.
Analyses of chicken sialyltransferases related to N-glycosylation
J. Biosci. Bioeng.
119
623-628
2015
Gallus gallus (A0A1D5NU03), Gallus gallus (F1NQP1), Gallus gallus
brenda
Schwardt, O.; Gao, G.P.; Visekruna, T.; Rabbani, S.; Gassmann, E.; Ernst, B.
Substrate specificity and preparative use of recombinant rat ST3Gal III
J. Carbohydr. Chem.
23
1-26
2004
Rattus norvegicus (Q02734)
-
brenda
Matsuhashi, H.; Horii, Y.; Kato, K.
Region-specific and epileptogenic-dependent expression of six subtypes of alpha2,3-sialyltransferase in the adult mouse brain
J. Neurochem.
84
53-66
2003
Mus musculus, Mus musculus (P97325), Mus musculus (Q91Y74)
brenda
Petit, D.; Teppa, E.; Mir, A.M.; Vicogne, D.; Thisse, C.; Thisse, B.; Filloux, C.; Harduin-Lepers, A.
Integrative view of alpha2,3-sialyltransferases (ST3Gal) molecular and functional evolution in deuterostomes significance of lineage-specific losses
Mol. Biol. Evol.
32
906-927
2015
Mus musculus (P97325), Mus musculus (Q91Y74)
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 (Q9Y2A9)
brenda
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