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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 III, alpha2-->3 sialyltransferase, beta-galactoside alpha2,3-sialyltransferase, beta-galactoside-a2,3-sialyltransferase III, beta-galactoside-alpha2,3-sialyltransferase III, CMP-NeuAc:Gal beta 1-4GlcNAc-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
ST3Gal3
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
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
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
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
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 + epidermal growth factor receptor
CMP + ?
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?
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
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-
?
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
about 25% of the activity with beta-D-Gal-(1->4)-beta-D-GlcNAc
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-
?
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
about 10% of the activity with beta-D-Gal-(1->4)-beta-D-GlcNAc
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-
?
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
-
-
-
?
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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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 + epidermal growth factor receptor
CMP + ?
-
-
-
?
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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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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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
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
brenda
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
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
malfunction
-
enzyme downregulation significantly impairs the receptive ability of human endometrial RL95-2 cells to trophoblastic cells in vitro and inhibited implantation in pregnant mice
malfunction
enzyme knockdown sensitizes ovarian cancer cells to cisplatin-induced apoptosis
malfunction
the phosphorylation levels of AKT and ERK are significantly decreased and the cell growth and colony formation are significantly suppressed in enzyme knockout cells. The expression levels of E-cadherin and claudin-1 are enhanced in enzyme knockout cells
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
metabolism
-
ST3Gal3 is the key enzyme responsible for sialyl Lewis X oligosaccharide biosynthesis
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
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 facilitates endometrial receptivity through increasing sLeX oligosaccharide
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). SIA4C_HUMAN
333
1
38045
Swiss-Prot
Secretory Pathway (Reliability: 1)
SIA4C_MOUSE
333
1
38058
Swiss-Prot
Secretory Pathway (Reliability: 1)
SIA4C_PANTR
328
1
37274
Swiss-Prot
Secretory Pathway (Reliability: 1)
SIA4C_RAT
333
1
38043
Swiss-Prot
Secretory Pathway (Reliability: 1)
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 DSM 15465 / Z2491)
371
1
42554
Swiss-Prot
-
LST_NEIMB
Neisseria meningitidis serogroup B (strain MC58)
371
1
42611
Swiss-Prot
-
SIAT6_HUMAN
375
1
42171
Swiss-Prot
Secretory Pathway (Reliability: 1)
SIAT6_MOUSE
374
1
42132
Swiss-Prot
Secretory Pathway (Reliability: 1)
SIAT6_PANTR
375
1
42171
Swiss-Prot
Secretory Pathway (Reliability: 1)
SIAT6_RAT
374
1
42082
Swiss-Prot
Secretory Pathway (Reliability: 1)
Q6H8M8_BOVIN
374
1
42085
TrEMBL
Secretory Pathway (Reliability: 1)
Q70D54_PIG
374
1
41959
TrEMBL
Secretory Pathway (Reliability: 1)
Q9QXF6_MESAU
359
1
40523
TrEMBL
Secretory Pathway (Reliability: 1)
Q9YN04_9POXV
290
0
33524
TrEMBL
Secretory Pathway (Reliability: 2)
Q9QXF5_MESAU
321
1
36678
TrEMBL
Secretory Pathway (Reliability: 1)
Q5ND64_ORYLA
356
1
40439
TrEMBL
Secretory Pathway (Reliability: 1)
Q9YJT3_9POXV
290
0
33284
TrEMBL
Secretory Pathway (Reliability: 2)
Q70D55_XENLA
360
1
40906
TrEMBL
Secretory Pathway (Reliability: 1)
Q9YJT5_9POXV
290
0
33283
TrEMBL
Secretory Pathway (Reliability: 2)
Q17WF9_HELAH
Helicobacter acinonychis (strain Sheeba)
395
0
47148
TrEMBL
-
B3GN3_HUMAN
372
1
42534
Swiss-Prot
Secretory Pathway (Reliability: 1)
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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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
-70°C, purified enzyme, over 50 days, isoform ST2 remains stable
-
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 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
human endometrial tissues at secretory phase express a 4fold higher enzyme level relative to the tissues at proliferative phase
-
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
-
chemical-enzymatic synthesis of sialyl-Lewis x-containing hexasaccharides found on O-linked glycoproteins, process involves several enzymes of the pathway
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
-
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
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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 (Q15KI8), Pasteurella multocida
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 (Q11203), Homo sapiens (Q11206), Homo sapiens
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-NeuAc Gal 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 (Q9YJT3), myxoma virus
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 (Q17WF9), Helicobacter acinonychis
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 (P97325), Mus musculus (Q91Y74), Mus musculus
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 (Q11206), Homo sapiens
brenda
Nemansky, M.; Van den Eijnden, D.H.
Enzymic characterization of CMP-NeuAc Gal-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 (P97325), Mus musculus (Q91Y74), Mus musculus
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
Wang, X.; Zhang, Y.; Lin, H.; Liu, Y.; Tan, Y.; Lin, J.; Gao, F.; Lin, S.
Alpha2,3-sialyltransferase III knockdown sensitized ovarian cancer cells to cisplatin-induced apoptosis
Biochem. Biophys. Res. Commun.
482
758-763
2017
Homo sapiens (Q11203)
brenda
Fessner, W.D.; Mertsch, A.; He, N.; Yi, D.; Kickstein, M.
An alpha2,3-sialyltransferase from Photobacterium phosphoreum with broad substrate scope Controlling hydrolytic activity by directed evolution
Chem. Eur. J.
26
11614-11624
2020
Homo sapiens
brenda
Qi, F.; Isaji, T.; Duan, C.; Yang, J.; Wang, Y.; Fukuda, T.; Gu, J.
ST3GAL3, ST3GAL4, and ST3GAL6 differ in their regulation of biological functions via the specificities for the alpha2,3-sialylation of target proteins
FASEB J.
34
881-897
2020
Homo sapiens (Q11203)
brenda
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