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Enzyme Nomenclature
Information on EC 2.4.99.6 - N-acetyllactosaminide alpha-2,3-sialyltransferase
for references in articles please use BRENDA:EC2.4.99.6
Word Map on EC 2.4.99.6
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The enzyme appears in viruses and cellular organisms
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EC NUMBER 
COMMENTARY 
2.4.99.6
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RECOMMENDED NAME
GeneOntology No.
N-acetyllactosaminide alpha-2,3-sialyltransferase
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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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-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
glycosyl group transfer
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-
-
-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
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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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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
metabolism
physiological function
malfunction
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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
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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
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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
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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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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
-
-
-
-
?
CMP-N-acetyl-beta-neuraminate + 4-methylumbelliferyl beta-lactoside
CMP + alpha-Neu5Ac-(2->3)-beta-D-Gal-(1->4)-beta-D-Glc
-
-
-
?
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
-
-
-
?
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
-
-
-
?
CMP-N-acetyl-beta-neuraminate + ally beta-D-Gal-(1->4)-beta-D-GlcNAc
CMP + allyl alpha-Neu5Ac-(2->3)-beta-D-Gal-(1->4)-beta-D-GlcNAc
-
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
-
-
?
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
-
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
-
-
?
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 + benzy 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
CMP-N-acetyl-beta-neuraminate + benzyl beta-D-(4-O-Me)Gal-beta-D-(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-beta-D-(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
-
-
?
CMP-N-acetyl-beta-neuraminate + benzyl beta-D-Gal-(1->4)-beta-D-GlcNAc-(1->6)-(4-O-Me)Gal-beta-D-(1->3)-alpha-D-GalNAc
CMP + benzyl alpha-Neu5Ac-(2->3)-beta-D-Gal-(1->4)-beta-D-GlcNAc-(1->6)-(4-O-Me)Gal-beta-D-(1->3)-alpha-D-GalNAc
-
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
-
-
?
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
-
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
-
-
?
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)-[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
-
-
-
?
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
-
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
-
-
?
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
-
27.1% of the activity compared to ally beta-D-Gal-(1->4)-beta-D-GlcNAc, alpha2,3(N) sialyltransferase
-
-
?
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
-
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
-
-
?
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
-
-
?
CMP-N-acetyl-beta-neuraminate + beta-D-Gal-(1->3)-beta-D-GlcNAc
CMP + alphaNeuAc-(2->3)-beta-D-Gal-(1->3)-beta-D-GlcNA
activity with beta-D-Gal-(1->3)-beta-D-GlcNAc is higher than activity with beta-D-Gal-(1->4)-beta-D-GlcNAc
-
-
?
CMP-N-acetyl-beta-neuraminate + beta-D-Gal-(1->3)-beta-GlcNAc
CMP + alphaNeuAc-(2->3)-beta-D-Gal-(1->3)-beta-D-GlcNA
activity with beta-D-Gal-(1->4)-beta-D-GlcNAc is higher than activity with beta-D-Gal-(1->3)-beta-D-GlcNAc
-
-
?
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
-
i.e. lactosylceramide
-
-
?
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-GlcNA
-
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
-
-
?
CMP-N-acetyl-beta-neuraminate + beta-D-Gal-(1->4)-beta-D-GlcNAc
CMP + alphaNeuAc-(2->3)-beta-D-Gal-(1->4)-beta-D-GlcNA
activity with beta-D-Gal-(1->3)-beta-D-GlcNAc is higher than activity with beta-D-Gal-(1->4)-beta-D-GlcNAc
-
-
?
CMP-N-acetyl-beta-neuraminate + beta-D-Gal-(1->4)-beta-D-GlcNAc
CMP + alphaNeuAc-(2->3)-beta-Gal-(1->4)-beta-GlcNA
activity with beta-D-Gal-(1->4)-beta-D-GlcNAc is higher than activity with beta-Gal-(1->3)-beta-GlcNAc
-
-
?
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-GlNAc
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-GlNAc
-
-
-
-
?
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
-
i.e. neolactotetraosylceramide
-
-
?
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
-
-
-
-
?
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]
-
-
-
-
?
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
-
-
-
-
-
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
-
-
?
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
-
-
-
-
?
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
-
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 + 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
-
28.1% of the activity compared to ally beta-D-Gal-(1->4)-beta-D-GlcNAc, alpha2,3(N) sialyltransferase
-
-
?
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
-
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
-
-
?
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
-
-
?
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
-
-
?
CMP-N-acetyl-beta-neuraminate + methyl beta-D-glucopyranoside
CMP + methyl alpha-Neu5Ac-(2->3)-beta-D-glucopyranoside
A8R0Y0
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
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
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-(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
A8R0Y0
-
-
-
?
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
A8R0Y0
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
A8R0Y0
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
A8R0Y0
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
A8R0Y0
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
A8R0Y0
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
A8R0Y0
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
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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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INHIBITORS
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
A8R0Y0
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
A8R0Y0
10°C: 65% of maximal activity, 30°C: 80% of maximal activity
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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
-
from peripheral blood mononuclear cells, enzyme level stimulated by phytohemagglutinin
the expression level of ST3Gal6 in the magnum of the oviduct is almost a half that in the liver
-
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
-
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
-
recombinant enzyme expressed in Spodoptera frugiperda cells
; 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
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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PDB
SCOP
CATH
ORGANISM
UNIPROT
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
A8R0Y0
MALDI-TOF of truncated enzyme with N-terminal Lys2 to Cys22 deletion
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
?
A8R0Y0
x * 43921, MALDI-TOF of truncated enzyme with N-terminal Lys2 to Cys22 deletion
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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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ENGINEERING
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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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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LINKS TO OTHER DATABASES (specific for EC-Number 2.4.99.6)
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