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Information on EC 2.4.3.1 - beta-galactoside alpha-(2,6)-sialyltransferase
for references in articles please use BRENDA:EC2.4.3.1
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EC Tree 2 Transferases
2.4 Glycosyltransferases
2.4.3 Sialyltransferases
2.4.3.1 beta-galactoside alpha-(2,6)-sialyltransferase
IUBMB Comments
The enzyme acts on the terminal non-reducing β-D-galactosyl residue of the oligosaccharide moiety of glycoproteins and glycolipids.
The enzyme appears in viruses and cellular organisms
Reaction Schemes
showSynonyms
st6gal i, st6gal1, alpha 2,6-sialyltransferase, st6gal-1, st6gal, alpha-2,6-sialyltransferase, st6galnac2, st6gali, siat1, alpha 2,6-st, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
(alpha-N-acetyl-neuraminyl-2,3-beta-galactosyl-1,3)-N-acetylgalactosaminide alpha2,6-sialyltransferase 5
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6STase
alpha 2,6-sialyltransferase
alpha 2,6-ST
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alpha(2,6)-sialyltransferase
alpha(2,6)-ST
alpha-(2->6)-sialyltransferase
alpha-2,6-sialyltransferase
alpha2,6 sialyltransferase
alpha2,6-sialyltransferase
alpha2,6-ST
alpha2-6 sialyltransferase
antigens, CD75
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B-cell antigen CD75
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beta-galactoside alpha-2,6-sialyltransferase
beta-galactoside alpha2,6-sialyltransferase
beta-galactoside alpha2-6-sialyltransferase-1
CMP-acetylneuraminate-galactosylglycoprotein sialyltransferase
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CMP-acetylneuraminate-glycoprotein sialyltransferase
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CMP-acetylneuraminate-lactosylceramide-sialyltransferase
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CMP-N-acetylneuraminate:beta-D-galactosyl-(1->4)-N-acetyl-beta-D-glucosamine alpha-(2->6)-N-acetylneuraminyltransferase
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CMP-N-acetylneuraminate:beta-D-galactosyl-1,4-N-acetyl-beta-D-glucosamine alpha-2,6-N-acetylneuraminyltransferase
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CMP-N-acetylneuraminic acid-glycoprotein sialyltransferase
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CMP-N-acetylneuraminic acid:lactosylceramide sialyltransferase
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CMP-sialic acid:lactosylceramide sialyltransferase
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cytidine monophosphoacetylneuraminate-galactosylglycoprotein sialyltransferase
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cytidine monophosphoacetylneuraminate-lactosylceramide sialyltransferase
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EC 2.4.99.1
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formerly
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EC 2.4.99.11
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formerly
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GM3-synthase
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HAC1268
lactosylceramide alpha-2,6-N-sialyltransferase
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sialotransferase
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sialyltransferase
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sialyltransferase, cytidine monophosphoacetylneuraminate-galactosylglycoprotein
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sialyltransferase, cytidine monophosphoacetylneuraminate-lactosylceramide
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ST6Gal
ST6Gal I
ST6Gal II
ST6Gal-1
ST6Gal-I
ST6Gal1
additional information
alpha2-6 sialyltransferase
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-
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-
additional information
ST6Gal I-IV subfamilies of the sialyltransferase family ST6Gal
additional information
ST6Gal I-IV subfamilies of the sialyltransferase family ST6Gal
additional information
ST6Gal I-IV subfamilies of the sialyltransferase family ST6Gal
additional information
ST6Gal I-IV subfamilies of the sialyltransferase family ST6Gal
additional information
ST6Gal I-IV subfamilies of the sialyltransferase family ST6Gal
additional information
ST6Gal I-IV subfamilies of the sialyltransferase family ST6Gal
additional information
ST6Gal I-IV subfamilies of the sialyltransferase family ST6Gal
additional information
ST6Gal I-IV subfamilies of the sialyltransferase family ST6Gal
additional information
ST6Gal I-IV subfamilies of the sialyltransferase family ST6Gal
additional information
ST6Gal I-IV subfamilies of the sialyltransferase family ST6Gal
additional information
ST6Gal I-IV subfamilies of the sialyltransferase family ST6Gal
additional information
ST6Gal I-IV subfamilies of the sialyltransferase family ST6Gal
additional information
ST6Gal I-IV subfamilies of the sialyltransferase family ST6Gal
additional information
ST6Gal I-IV subfamilies of the sialyltransferase family ST6Gal
additional information
ST6Gal I-IV subfamilies of the sialyltransferase family ST6Gal
additional information
ST6Gal I-IV subfamilies of the sialyltransferase family ST6Gal
additional information
ST6Gal I-IV subfamilies of the sialyltransferase family ST6Gal
additional information
ST6Gal I-IV subfamilies of the sialyltransferase family ST6Gal
additional information
ST6Gal I-IV subfamilies of the sialyltransferase family ST6Gal
additional information
ST6Gal I-IV subfamilies of the sialyltransferase family ST6Gal
additional information
ST6Gal I-IV subfamilies of the sialyltransferase family ST6Gal
additional information
ST6Gal I-IV subfamilies of the sialyltransferase family ST6Gal
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
CMP-N-acetyl-beta-neuraminate + beta-D-galactosyl-R = CMP + N-acetyl-alpha-neuraminyl-(2->6)-beta-D-galactosyl-R
CMP-N-acetyl-beta-neuraminate + beta-D-galactosyl-R = CMP + N-acetyl-alpha-neuraminyl-(2->6)-beta-D-galactosyl-R
Val220 participates in binding the common cytidine moiety in substrate CMP-NeuAc and inhibitor CDP
CMP-N-acetyl-beta-neuraminate + beta-D-galactosyl-R = CMP + N-acetyl-alpha-neuraminyl-(2->6)-beta-D-galactosyl-R
mechanism
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CMP-N-acetyl-beta-neuraminate + beta-D-galactosyl-R = CMP + N-acetyl-alpha-neuraminyl-(2->6)-beta-D-galactosyl-R
The terminal beta-D-galactosyl residue of the oligosaccharide of glycoproteins, as well as lactose, can act as acceptor
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
glycosyl group transfer
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PATHWAY SOURCE
PATHWAYS
MetaCyc
complex N-linked glycan biosynthesis (vertebrates), ganglio-series glycosphingolipids biosynthesis, lacto-series glycosphingolipids biosynthesis, neolacto-series glycosphingolipids biosynthesis, terminal O-glycans residues modification (via type 2 precursor disaccharide)
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SYSTEMATIC NAME
IUBMB Comments
CMP-N-acetyl-beta-neuraminate:beta-D-galactoside alpha-(2->6)-N-acetylneuraminyltransferase (configuration-inverting)
The enzyme acts on the terminal non-reducing beta-D-galactosyl residue of the oligosaccharide moiety of glycoproteins and glycolipids.
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CAS REGISTRY NUMBER
COMMENTARY
55071-95-9
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9075-81-4
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
asialo-alpha1-acidglycoprotein + CMP-Neu5Ac
?
Substrates: membrane-bound and soluble protein, 34% and 25% relative activity, respectively
Products: -
Products: -
?
CMP-9''-benzamido-Neu5Ac + N-acetyllactosamine
?
-
Substrates: -
Products: -
Products: -
?
CMP-9''-phenylacetamido-Neu5Ac + N-acetyllactosamine
?
-
Substrates: -
Products: -
Products: -
?
CMP-9''-phenylhexanamido-Neu5Ac + N-acetyllactosamine
?
-
Substrates: -
Products: -
Products: -
?
CMP-9''-phenylpropionamido-Neu5Ac + lactose
?
-
Substrates: -
Products: -
Products: -
?
CMP-9''-phenylpropionamido-Neu5Ac + N-acetyllactosamine
?
-
Substrates: -
Products: -
Products: -
?
CMP-9-acetamido-N-acetylneuraminate + asialo-alpha1-acid glycoprotein
?
-
Substrates: -
Products: -
Products: -
?
CMP-9-amino-N-acetylneuraminate + asialo-alpha1-acid glycoprotein
?
-
Substrates: -
Products: -
Products: -
?
CMP-9-azido-N-acetylneuraminate + asialo-alpha1-acid glycoprotein
?
-
Substrates: -
Products: -
Products: -
?
CMP-9-benzamido-N-acetylneuraminate + asialo-alpha1-acid glycoprotein
?
-
Substrates: -
Products: -
Products: -
?
CMP-9-fluoresceinyl-N-acetylneuraminate + asialofetuin
?
Substrates: -
Products: -
Products: -
?
CMP-9-hexanoylamido-N-acetylneuraminate + asialo-alpha1-acid glycoprotein
?
-
Substrates: -
Products: -
Products: -
?
CMP-9-O-acetyl-N-acetylneuraminate + asialo-alpha1-acid glycoprotein
CMP + ?
-
Substrates: -
Products: -
Products: -
?
CMP-N-acetyl-beta-neuraminate + alpha-1-antitrypsin
CMP + ?
-
Substrates: -
Products: -
Products: -
?
CMP-N-acetyl-beta-neuraminate + asialofetuin
CMP + fetuin
Substrates: -
Products: -
Products: -
?
CMP-N-acetyl-beta-neuraminate + beta-D-galactosyl-R
CMP + N-acetyl-alpha-neuraminyl-(2->6)-beta-D-galactosyl-R
CMP-N-acetyl-beta-neuraminate + desialylated fetuin
CMP + ?
Substrates: -
Products: -
Products: -
?
CMP-N-acetyl-beta-neuraminate + integrin-beta1
CMP + ?
Substrates: -
Products: -
Products: -
?
CMP-N-acetyl-beta-neuraminate + intercellular adhesion molecule-1
CMP + ?
-
Substrates: the enzyme can increase the stability of intercellular adhesion molecule-1 through sialylation
Products: -
Products: -
?
CMP-N-acetyl-beta-neuraminate + methyl beta-D-N-acetyllactosaminide
CMP + methyl alpha-N-acetylneuraminyl-(2->6)-beta-D-galactopyranosyl-(1->4)-2-acetamido-2-deoxy-beta-D-glucopyranoside
-
Substrates: -
Products: -
Products: -
?
CMP-N-acetyl-beta-neuraminate + N-acetyllactosamin-butyl
CMP + ?
Substrates: -
Products: -
Products: -
?
CMP-N-acetyl-beta-neuraminate + PrPSc
CMP + ?
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Substrates: brain-, spleen- and N2a-cell-derived PrPSc is predominantly 2,6-sialylated
Products: -
Products: -
?
CMP-N-acetylneuraminate + (2S,3S,4R,5R,6R)-5-acetylamino-4-hydroxy-6-methoxy-3-((2S,3R,4S,5R,6R)-3,4,5-trihydroxy-6-hydroxymethyl-tetrahydro-pyran-2-yloxy)-tetrahydro-pyran-2-carboxylic acid methyl ester
CMP + ?
CMP-N-acetylneuraminate + (2S,3S,4R,5R,6R)-5-acetylamino-4-hydroxy-6-methoxy-3-((2S,3R,4S,5R,6R)-3,4,5-trihydroxy-6-hydroxymethyl-tetrahydro-pyran-2-yloxy)-tetrahydro-pyran-2-carboxylic acid methylamide
CMP + ?
-
Substrates: 0.2% of the activity with Galbeta(1-3)GlcNAcbeta-O-Me
Products: -
Products: -
?
CMP-N-acetylneuraminate + (Gal-3-O-Me)beta(1-3)(GlcNAc-6-O-Me)beta-O-Me
CMP + ?
-
Substrates: 50% of the activity with Galbeta(1-3)GlcNAcbeta-O-Me
Products: -
Products: -
?
CMP-N-acetylneuraminate + (Gal-3-O-Me)beta(1-3)GlcNAcbeta-O-Me
CMP + ?
-
Substrates: 80% of the activity with Galbeta(1-3)GlcNAcbeta-O-Me
Products: -
Products: -
?
CMP-N-acetylneuraminate + (Galbeta(1,4))2(GlcNAcbeta(1,2))2(Man)3(GlcNAc)2-Asn-Fmoc
?
-
Substrates: 34.9 activity compared to Galbeta(1,4)-GlcNAcbeta-4-nitrophenyl
Products: -
Products: -
?
CMP-N-acetylneuraminate + (GalNAcbeta(1,4))2(GlcNAcbeta(1,2))2(Man)3(GlcNAc)2-Asn-Fmoc
?
-
Substrates: 140 activity compared to Galbeta(1,4)-GlcNAcbeta-4-nitrophenyl
Products: -
Products: -
?
CMP-N-acetylneuraminate + 4-methylumbelliferyl beta-D-lactoside
?
-
Substrates: -
Products: -
Products: -
?
CMP-N-acetylneuraminate + 4-nitrophenyl beta-D-galactopyranosyl-(1->3)-N-acetyl-beta-D-glucosaminide
CMP + 4-nitrophenyl N-acetyl-alpha-neuraminyl-(2->6)-beta-D-galactopyranosyl-(1->3)-N-acetyl-beta-D-glucosaminide
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Substrates: 2.5% activity compared to Galbeta(1,4)-GlcNAcbeta-4-nitrophenyl
Products: -
Products: -
?
CMP-N-acetylneuraminate + 4-nitrophenyl beta-D-galactosaminyl-(1->4)-N-acetyl-beta-D-glucosaminide
CMP + 4-nitrophenyl N-acetyl-alpha-neuraminyl-(2->6)-beta-D-galactosaminyl-(1->4)-N-acetyl-beta-D-glucosaminide
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Substrates: 100% activity
Products: -
Products: -
?
CMP-N-acetylneuraminate + 4-nitrophenyl N-acetyl-beta-D-galactosaminyl-(1->4)-N-acetyl-beta-D-glucosaminide
CMP + 4-nitrophenyl N-acetyl-alpha-neuraminyl-(2->6)-N-acetyl-beta-D-galactosaminyl-(1->4)-N-acetyl-beta-D-glucosaminide
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Substrates: best acceptor with 371.5% activity compared to Galbeta(1,4)-GlcNAcbeta-4-nitrophenyl
Products: -
Products: -
?
CMP-N-acetylneuraminate + 4-nitrophenyl-D-galactoside
CMP + alpha-N-acetylneuraminyl-2,6-beta-D-galactosyl-(4-nitro)phenol
-
Substrates: -
Products: -
Products: -
?
CMP-N-acetylneuraminate + 5-(5-dimethylaminonaphthalene-1-sulfonyl-2-(2-aminoethoxy))ethyl beta-lactose
CMP + ?
Substrates: -
Products: -
Products: -
?
CMP-N-acetylneuraminate + 5-(5-dimethylaminonaphthalene-1-sulfonyl-2-(2-aminoethoxy))ethyl beta-N-acetyllactosamine
CMP + 5-(5-dimethylaminonaphthalene-1-sulfonyl-2-(2-aminoethoxy)) ethyl beta-N-acetylneuraminic acid alpha-2,6-N-acetyllactosamine
Substrates: -
Products: -
Products: -
?
CMP-N-acetylneuraminate + 6'-sialyl-N-acetyl-D-lactosamine
?
Substrates: -
Products: -
Products: -
?
CMP-N-acetylneuraminate + alpha1-acid glycoprotein
CMP + ?
-
Substrates: 20.6% of the activity with beta-D-galactosyl-1,4-N-acetyl-beta-D-glucosamine
Products: -
Products: -
?
CMP-N-acetylneuraminate + asialo-agalacto-prothrombin
CMP + agalacto-prothrombin
-
Substrates: -
Products: -
Products: -
?
CMP-N-acetylneuraminate + asialo-alpha1-acid glycoprotein
CMP + ?
-
Substrates: 12.3% of the activity with beta-D-galactosyl-1,4-N-acetyl-beta-D-glucosamine
Products: -
Products: -
?
CMP-N-acetylneuraminate + asialo-apoceruloplasmin
CMP + apoceruloplasmin
-
Substrates: best substrate
Products: -
Products: -
?
CMP-N-acetylneuraminate + asialo-chorionic gonadotropin
CMP + chorionic gonadotropin
-
Substrates: acceptor protein from human source
Products: -
Products: -
?
CMP-N-acetylneuraminate + asialo-fibrinogen
CMP + fibrinogen
-
Substrates: -
Products: -
Products: -
?
CMP-N-acetylneuraminate + asialo-immunoglobulin G
CMP + immunoglobulin G
-
Substrates: -
Products: -
Products: -
?
CMP-N-acetylneuraminate + asialo-immunoglobulin M
CMP + immunoglobulin M
-
Substrates: -
Products: -
Products: -
?
CMP-N-acetylneuraminate + asialo-proteose peptone
CMP + proteose peptone
-
Substrates: -
Products: -
Products: -
?
CMP-N-acetylneuraminate + asialo-Tamm-Horsfall glycoprotein
CMP + Tamm-Horsfall glycoprotein
-
Substrates: -
Products: -
Products: -
?
CMP-N-acetylneuraminate + asialo-thyroglobulin glycopeptide
CMP + thyroglobulin glycopeptide
-
Substrates: -
Products: -
Products: -
?
CMP-N-acetylneuraminate + asialoovomucoid
CMP + ?
-
Substrates: 9.1% of the activity with beta-D-galactosyl-1,4-N-acetyl-beta-D-glucosamine
Products: -
Products: -
?
CMP-N-acetylneuraminate + beta-D-galactosyl-(1->4)-N-acetyl-beta-D-glucosamine
CMP + alpha-N-acetylneuraminyl-(2->6)-beta-D-galactosyl-(1->4)-N-acetyl-beta-D-glucosamine
CMP-N-acetylneuraminate + beta-D-galactosyl-1,3-N-acetyl-beta-D-glucosamine
CMP + alpha-N-acetylneuraminyl-2,6-beta-D-galactosyl-1,3-N-acetyl-beta-D-glucosamine
-
Substrates: 36% of the activity with beta-D-galactosyl-1,4-N-acetyl-beta-D-glucosamine
Products: -
Products: -
?
CMP-N-acetylneuraminate + beta-D-galactosyl-1,3-N-acetyl-beta-D-glucosaminyl-1,3-galactosyl-beta-1,4-D-glucose
CMP + alpha-N-acetylneuraminyl-2,6-beta-D-galactosyl-1,3-N-acetyl-beta-D-glucosaminyl-1,3-galactosyl-beta-1,4-D-glucose
CMP-N-acetylneuraminate + beta-D-galactosyl-1,4-beta-D-glucosylceramide
CMP + alpha-N-acetylneuraminyl-2,6-beta-D-galactosyl-1,4-beta-D-glucosylceramide
CMP-N-acetylneuraminate + beta-D-galactosyl-1,4-N-acetyl-beta-D-glucosamine
CMP + alpha-N-acetylneuraminyl-2,6-beta-D-galactosyl-1,4-N-acetyl-beta-D-glucosamine
CMP-N-acetylneuraminate + beta-D-galactosyl-1,4-N-acetyl-beta-D-glucosamine-R
CMP + alpha-N-acetylneuraminyl-2,6-beta-D-galactosyl-1,4-N-acetyl-beta-D-glucosamine-R
-
Substrates: exhibits highest activity toward GalNAcbeta1,4GlcNAc carbohydrate structures at the non-reducing termini of oligosaccharides and glycoprotein glycans. Oligosaccharides are preferred over glycoproteins as acceptors, and no activity toward glycolipid acceptors is detected. Recombinant Drosophila SiaT expressed in cultured insect cells possesses in vivo and in vitro autosialylation activity toward beta-linked GalNAc termini of its own N-linked glycans
Products: -
Products: -
?
CMP-N-acetylneuraminate + beta-D-galactosyl-1,4-N-acetyl-beta-D-glucosaminyl-1,2-alpha-mannosyl-1,6-beta-mannosyl-1,4-N-acetylglucosamine
CMP + alpha-N-acetylneuraminyl-2,6-beta-D-galactosyl-1,4-N-acetyl-beta-D-glucosaminyl-1,2-alpha-mannosyl-1,6-beta-mannosyl-1,4-N-acetylglucosamine
-
Substrates: -
Products: -
Products: -
?
CMP-N-acetylneuraminate + beta-D-galactosyl-1,4-N-acetyl-beta-D-glucosaminyl-1,4-beta-D-galactosyl-1,4-beta-D-glucosyl-beta1-ceramide
CMP + alpha-N-acetylneuraminyl-2,6-beta-D-galactosyl-1,4-N-acetyl-beta-D-glucosaminyl-1,4-beta-D-galactosyl-1,4-beta-D-glucosyl-beta1-ceramide
-
Substrates: i.e. paragloboside
Products: i.e. alpha-2,6-sialylparagloboside
Products: i.e. alpha-2,6-sialylparagloboside
?
CMP-N-acetylneuraminate + beta-D-galactosyl-1,4-N-acetyl-beta-D-glucosaminyl-R
CMP + alpha-N-acetylneuraminyl-2,6-beta-D-galactosyl-1,4-N-acetyl-beta-D-glucosaminyl-R
CMP-N-acetylneuraminate + formic acid (2R,3R,4S,5R,6R)-2-((2R,3R,4R,5R,6R)-3-acetylamino-5-hydroxy-2-methoxy-6-methylaminomethyl-tetrahydro-pyran-4-yloxy)-4,5-dihydroxy-6-hydroxymethyl-tetrahydro-pyran-3-yl ester
CMP + ?
-
Substrates: as active as Galbeta(1-3)GlcNAcbeta-O-Me
Products: -
Products: -
?
CMP-N-acetylneuraminate + fucosyl-alpha-1,2-D-galactosyl-beta-1,4-D-glucose
?
-
Substrates: -
Products: -
Products: -
?
CMP-N-acetylneuraminate + fucosyllactose
CMP + alpha-N-acetylneuraminyl-2,6-[alpha-L-fucopyranosyl-1,2]-beta-D-galactopyranosyl-1,4-D-glucopyranose
-
Substrates: also pyridylaminated
Products: -
Products: -
?
CMP-N-acetylneuraminate + Gal-beta-1,3-GlcNAc-beta-OMe
?
Substrates: 77% of the activity with lactose
Products: -
Products: -
?
CMP-N-acetylneuraminate + Galbeta(1-3)(GlcNAc-6-O-Me)beta-O-Me
CMP + ?
-
Substrates: 80% of the activity with Galbeta(1-3)GlcNAcbeta-O-Me
Products: -
Products: -
?
CMP-N-acetylneuraminate + Galbeta(1-3)-GlcNAcbeta(1-3)Galbeta(1-4)Glc
CMP + NeuNAcalpha(2-6)-Galbeta(1-3)GlcNAcbeta(1-3)Galbeta(1-4)Glc
-
Substrates: 30% of the activity with beta-D-galactosyl-1,4-N-acetyl-beta-D-glucosamine
Products: -
Products: -
?
CMP-N-acetylneuraminate + Galbeta(1-3)GlcNAcbeta-O-Me
CMP + NeuAcalpha(2-6)Galbeta(1-3)GlcNAcbeta-O-Me
-
Substrates: -
Products: -
Products: -
?
CMP-N-acetylneuraminate + Galbeta(1-4)GlcNAcbeta(1-3)Galbeta(1-4)Glc
CMP + alpha-N-acetylneuraminyl-(2-6)Galbeta(1-4)GlcNAcbeta(1-3)Galbeta(1-4)Glc
-
Substrates: 79% of the activity with beta-D-galactosyl-1,4-N-acetyl-beta-D-glucosamine
Products: -
Products: -
?
CMP-N-acetylneuraminate + Galbeta(1->3)GalNAc
CMP + NeuAcalpha(2->6)Galbeta(1->3)GalNAc
Substrates: 10% activity compared to beta-D-galactosyl-1,4-N-acetyl-beta-D-glucosamine
Products: -
Products: -
?
CMP-N-acetylneuraminate + Galbeta(1->3)GlcNAc
CMP + NeuAcalpha(2->6)Galbeta(1->3)GlcNAc
Substrates: 2% activity compared to beta-D-galactosyl-1,4-N-acetyl-beta-D-glucosamine
Products: -
Products: -
?
CMP-N-acetylneuraminate + Galbeta(1->4)GlcNAcbeta(1->2)Manalpha(1->6)[Galbeta(1->4)GlcNAcbeta(1>2)Manalpha(1->3)]Manbeta(1->4)GlcNAcbeta(1->4)GlcNAc-pyridylamine
CMP + NeuAcalpha(2->6)Galbeta(1->4)GlcNAcbeta(1->2)Manalpha(1->6)[Galbeta(1->4)GlcNAcbeta(1>2)Manalpha(1->3)]Manbeta(1->4)GlcNAcbeta(1->4)GlcNAc-pyridylamine
-
Substrates: -
Products: -
Products: -
?
CMP-N-acetylneuraminate + Galbeta(1->4)GlcNAcbeta(1->3)Galbeta(1->4)Glcbeta(1<->1)ceramide
CMP + NeuAcalpha(2->6)Galbeta(1->4)GlcNAcbeta(1->3)Galbeta(1->4)Glcbeta(1<->1)ceramide
-
Substrates: -
Products: -
Products: -
?
CMP-N-acetylneuraminate + Galbeta-4-nitrophenyl
?
-
Substrates: 26.4% activity compared to Galbeta(1,4)-GlcNAcbeta-4-nitrophenyl
Products: -
Products: -
?
CMP-N-acetylneuraminate + GalNAcbeta-4-nitrophenyl
?
-
Substrates: 120.4% activity compared to Galbeta(1,4)-GlcNAcbeta-4-nitrophenyl
Products: -
Products: -
?
CMP-N-acetylneuraminate + GalNAcbeta1,4-GlcNAc-R
CMP + alpha-N-acetylneuraminyl-2,6-GalNAcbeta1,4-GlcNAc-R
-
Substrates: -
Products: 190% of the activity with beta-D-galactosyl-1,4-N-acetyl-beta-D-glucosamine
Products: 190% of the activity with beta-D-galactosyl-1,4-N-acetyl-beta-D-glucosamine
?
CMP-N-acetylneuraminate + glycano-(1->3)-(N-acetyl-alpha-D-galactosaminyl)-glycoprotein
CMP + glycano-[(2->6)-alpha-N-acetylneuraminyl]-(N-acetyl-D-galactosaminyl)-glycoprotein
Substrates: -
Products: -
Products: -
?
CMP-N-acetylneuraminate + lacto-N-neotetraose
CMP + ?
Substrates: 108% activity compared to beta-D-galactosyl-1,4-N-acetyl-beta-D-glucosamine
Products: -
Products: -
?
CMP-N-acetylneuraminate + lactose
CMP + alpha-N-acetylneuraminyl-2,6-beta-D-galactosyl-1,4-beta-D-glucose
-
Substrates: 15.5% of the activity with beta-D-galactosyl-1,4-N-acetyl-beta-D-glucosamine
Products: -
Products: -
?
CMP-N-acetylneuraminate + methanesulfonic acid (2R,3S,4R,5R,6R)-5-acetylamino-4-hydroxy-6-methoxy-3-((2S,3R,4S,5R,6R)-3,4,5-trihydroxy-6-hydroxymethyl-tetrahydro-pyran-2-yloxy)-tetrahydro-pyran-2-ylmethyl ester
CMP + ?
-
Substrates: 90% of the activity with Galbeta(1-3)GlcNAcbeta-O-Me
Products: -
Products: -
?
CMP-N-acetylneuraminate + methyl-alpha-D-galactopyranoside
?
Substrates: 2% of the activity with lactose
Products: -
Products: -
?
CMP-N-acetylneuraminate + methyl-beta-D-galactopyranoside
?
Substrates: 59% of the activity with lactose
Products: -
Products: -
?
CMP-N-acetylneuraminate + methyl-beta-D-galactopyranoside
CMP + alpha-N-acetylneuraminyl-2,6-beta-D-methylgalactopyranoside
-
Substrates: -
Products: -
Products: -
?
CMP-N-acetylneuraminate + N-((1R,3R,5R,6R,7S,8R,13R,15R,16R,17S)-6,7,17-trihydroxy-5-hydroxymethyl-15-methoxy-2,4,9,11,14-pentaoxa-tricyclo[11.3.1.03,8]heptadec-16-yl)-acetamide
CMP + ?
-
Substrates: as active as Galbeta(1-3)GlcNAcbeta-O-Me
Products: -
Products: -
?
CMP-N-acetylneuraminate + N-((1R,3R,5R,6R,7S,8R,14R,16R,17R,18R)-6,7,18-trihydroxy-5-hydroxymethyl-16-methoxy-11-oxo-2,4,9,15-tetraoxa-12-aza-tricyclo[12.3.1.03,8]octadec-17-yl)-acetamide
CMP + ?
-
Substrates: 110% of the activity with Galbeta(1-3)GlcNAcbeta-O-Me
Products: -
Products: -
?
CMP-N-acetylneuraminate + N-((1R,3R,5R,6R,7S,8R,14R,16R,17R,18S)-6,7,18-trihydroxy-5-hydroxymethyl-16-methoxy-2,4,9,12,15-pentaoxa-tricyclo[12.3.1.03,8]octadec-17-yl)-acetamide
CMP + ?
-
Substrates: 130% of the activity with Galbeta(1-3)GlcNAcbeta-O-Me
Products: -
Products: -
?
CMP-N-acetylneuraminate + N-acetyl-D-galactosamine
?
Substrates: 12% of the activity with lactose
Products: -
Products: -
?
CMP-N-acetylneuraminate + N-[(2R,3R,4R,5S,6R)-4-hydroxy-6-(methanesulfonylamino-methyl)-2-methoxy-5-((2S,3R,4S,5R,6R)-3,4,5-trihydroxy-6-hydroxymethyl-tetrahydro-pyran-2-yloxy)-tetrahydro-pyran-3-yl]-acetamide
CMP + ?
-
Substrates: 70% of the activity with Galbeta(1-3)GlcNAcbeta-O-Me
Products: -
Products: -
?
CMP-N-acetylneuraminate + N-[(2R,3R,4R,5S,6R)-5-((2S,3R,4S,5R,6R)-4,5-dihydroxy-6-hydroxymethyl-3-methoxy-tetrahydro-pyran-2-yloxy)-6-formylaminomethyl-4-hydroxy-2-methoxy-tetrahydro-pyran-3-yl]-acetamide
CMP + ?
-
Substrates: as active as Galbeta(1-3)GlcNAcbeta-O-Me
Products: -
Products: -
?
CMP-N-acetylneuraminate + N-[(2R,3R,4R,5S,6R)-6-(acetylamino-methyl)-4-hydroxy-2-methoxy-5-((2S,3R,4S,5R,6R)-3,4,5-trihydroxy-6-hydroxymethyl-tetrahydro-pyran-2-yloxy)-tetrahydro-pyran-3-yl]-acetamide
CMP + ?
-
Substrates: 60% of the activity with Galbeta(1-3)GlcNAcbeta-O-Me
Products: -
Products: -
?
CMP-N-acetylneuraminate + N-[(2R,3R,4R,5S,6R)-6-aminomethyl-4-hydroxy-2-methoxy-5-((2S,3R,4S,5R,6R)-3,4,5-trihydroxy-6-hydroxymethyl-tetrahydro-pyran-2-yloxy)-tetrahydro-pyran-3-yl]-acetamide
CMP + ?
-
Substrates: 50% of the activity with Galbeta(1-3)GlcNAcbeta-O-Me
Products: -
Products: -
?
CMP-N-acetylneuraminate + Neu5Acalpha-2,3-Galbeta-1,4-Glc
CMP + alpha-N-acetylneuraminyl-2,6-(Neu5Acalpha-2,3-)Galbeta-1,4-Glc
-
Substrates: also pyridylaminated
Products: -
Products: -
?
CMP-N-acetylneuraminate + ovomucoid
CMP + ?
-
Substrates: 8.4% of the activity with beta-D-galactosyl-1,4-N-acetyl-beta-D-glucosamine
Products: -
Products: -
?
CMP-N-acetylneuraminate + pyridylamine-type 2H
CMP + alpha2,6-sialylated blood group type 2H antigen
Substrates: 2% activity compared to pyridylaminyl-lacto-N-neotetraose
Products: -
Products: -
?
CMP-N-acetylneuraminate + pyridylamino-lactose
CMP + alpha-N-acetylneuraminyl-2,6-beta-D-galactosyl-1,4-beta-D-glucosyl-pyridylaminoside
-
Substrates: recombinant enzyme
Products: -
Products: -
?
CMP-N-acetylneuraminate + pyridylamino-N-acetyllactosamine
?
-
Substrates: -
Products: -
Products: -
?
CMP-N-acetylneuraminate + pyridylaminyl-lacto-N-neotetraose
CMP + ?
Substrates: 100% activity
Products: -
Products: -
?
CMP-N-acetylneuraminate + tumor necrosis factor receptor 1
CMP + alpha2,6-sialyated tumor necrosis factor receptor 1
CMP-N-alpha-neuraminate + pyridylaminated ganglioside nLc4Cer
?
-
Substrates: -
Products: -
Products: -
?
CMP-NeuNAc + Galbeta(1->4)GIcNAc-R
CMP + NeuNAcalpha(2->6)Galbeta(l->4)GlcNAc-R
-
Substrates: -
Products: -
Products: -
?
cytidine 5'-monophosphate 3-(axial)-fluoro-N-acetylneuraminic acid + alpha-lactose
?
-
Substrates: [15N]Phe-labeled ST6Gal-I with a 15fold excess of CMP-3FNeuAc
Products: -
Products: -
?
cytidine 5'-monophosphate 4-O-(4-carboxy-2,2,6,6-tetramethylpiperidine-1-oxyl) + alpha-N-acetyllactosamine
?
-
Substrates: -
Products: -
Products: -
?
cytidine-5'-monophospho-sialic acid + lactose
?
-
Substrates: -
Products: -
Products: -
?
cytidine-5'-monophospho-sialic acid + N-acetyllactosamine
?
-
Substrates: -
Products: -
Products: -
?
cytidine-5'-yl-5-(acetamido)-9-(3-[4-chloro-1,2,3-oxadiazol-3-ium-5-olate]benzamido)-3,5,9-trideoxy-beta-D-glycero-D-galacto-non-2-ulopyranosid-2''-yl phosphate + asialofetuin
CMP + ?
Substrates: CMP-Neu9NSydCl
Products: -
Products: -
?
cytidine-5'-yl-5-(acetamido)-9-(3-[4-chloro-1,2,3-oxadiazol-3-ium-5-olate]benzamido)-3,5,9-trideoxy-beta-D-glycero-D-galacto-non-2-ulopyranosid-2''-yl phosphate + butyl beta-N-acetyllactosaminide
CMP + ?
Substrates: CMP-Neu9NSydCl
Products: -
Products: -
?
cytidine-5'-yl-5-(acetamido)-9-azido-3,5,9-trideoxy-beta-D-glycero-D-galacto-non-2-ulopyranosid-2''-yl phosphate + asialofetuin
CMP + ?
Substrates: CMP-Neu9Az
Products: -
Products: -
?
cytidine-5'-yl-5-(acetamido)-9-azido-3,5,9-trideoxy-beta-D-glycero-D-galacto-non-2-ulopyranosid-2''-yl phosphate + N-acetyllactosamin-butyl
CMP + ?
Substrates: CMP-Neu9Az
Products: -
Products: -
?
Galbeta(1,4)GlcNAc-octyl + CMP-Neu5Ac
?
Substrates: membrane-bound and soluble protein, 100% relative activity
Products: -
Products: -
?
GalNAcbeta(1,4)GlcNAc-octyl + CMP-Neu5Ac
?
Substrates: membrane-bound and soluble protein, 312% and 346% relative activity, respectively
Products: -
Products: -
?
N-acetyllactosamine 4-O-(4-carboxy-2,2,6,6-tetramethylpiperidine-1-oxyl)
?
-
Substrates: [15N]Phe-labeled ST6Gal-I with a 20fold excess of N-acetyllactosamine 4-O-(4-carboxy-2,2,6,6-tetramethylpiperidine-1-oxyl)
Products: -
Products: -
?
Neu5Acalpha-4-nitrophenyl + 4-methylumbelliferyl-beta-D-lactoside
?
-
Substrates: alpha2,6-trans-sialidase activity of DELTA15Pd2,6ST
Products: -
Products: -
?
CMP-9-O-acetyl-N-acetylneuraminate + asialo-alpha1-acid glycoprotein
?
-
Substrates: comparable or even higher transfer rates than with CMP-N-acetylneuraminate
Products: -
Products: -
?
CMP-9-O-acetyl-N-acetylneuraminate + asialo-alpha1-acid glycoprotein
?
-
Substrates: comparable or even higher transfer rates than with CMP-N-acetylneuraminate
Products: -
Products: -
?
CMP-N-acetyl-beta-neuraminate + asialo-alpha-1-antitrypsin
CMP + ?
-
Substrates: -
Products: -
Products: -
?
CMP-N-acetyl-beta-neuraminate + asialo-alpha-1-antitrypsin
CMP + ?
-
Substrates: -
Products: -
Products: -
?
CMP-N-acetyl-beta-neuraminate + asialo-alpha-1-antitrypsin
CMP + ?
Substrates: -
Products: -
Products: -
?
CMP-N-acetyl-beta-neuraminate + asialo-alpha-1-antitrypsin
CMP + ?
-
Substrates: -
Products: -
Products: -
?
CMP-N-acetyl-beta-neuraminate + asialofetuin
CMP + ?
-
Substrates: -
Products: -
Products: -
?
CMP-N-acetyl-beta-neuraminate + asialofetuin
CMP + ?
-
Substrates: -
Products: -
Products: -
?
CMP-N-acetyl-beta-neuraminate + asialofetuin
CMP + ?
Substrates: -
Products: -
Products: -
?
CMP-N-acetyl-beta-neuraminate + asialofetuin
CMP + ?
-
Substrates: -
Products: -
Products: -
?
CMP-N-acetyl-beta-neuraminate + beta-D-galactosyl-R
CMP + N-acetyl-alpha-neuraminyl-(2->6)-beta-D-galactosyl-R
-
Substrates: -
Products: -
Products: -
?
CMP-N-acetyl-beta-neuraminate + beta-D-galactosyl-R
CMP + N-acetyl-alpha-neuraminyl-(2->6)-beta-D-galactosyl-R
Substrates: -
Products: -
Products: -
?
CMP-N-acetyl-beta-neuraminate + beta-D-galactosyl-R
CMP + N-acetyl-alpha-neuraminyl-(2->6)-beta-D-galactosyl-R
-
Substrates: -
Products: -
Products: -
?
CMP-N-acetyl-beta-neuraminate + beta-D-galactosyl-R
CMP + N-acetyl-alpha-neuraminyl-(2->6)-beta-D-galactosyl-R
Substrates: -
Products: -
Products: -
?
CMP-N-acetyl-beta-neuraminate + human butyrylcholinesterase
CMP + ?
-
Substrates: -
Products: -
Products: -
?
CMP-N-acetyl-beta-neuraminate + human butyrylcholinesterase
CMP + ?
-
Substrates: -
Products: -
Products: -
?
CMP-N-acetyl-beta-neuraminate + human butyrylcholinesterase
CMP + ?
Substrates: -
Products: -
Products: -
?
CMP-N-acetyl-beta-neuraminate + human butyrylcholinesterase
CMP + ?
-
Substrates: -
Products: -
Products: -
?
CMP-N-acetyl-beta-neuraminate + N-acetyl-D-lactosamine
?
-
Substrates: -
Products: -
Products: -
?
CMP-N-acetyl-beta-neuraminate + N-acetyl-D-lactosamine
?
-
Substrates: -
Products: -
Products: -
?
CMP-N-acetyl-beta-neuraminate + N-acetyl-D-lactosamine
?
Substrates: -
Products: -
Products: -
?
CMP-N-acetyl-beta-neuraminate + N-acetyl-D-lactosamine
?
-
Substrates: -
Products: -
Products: -
?
CMP-N-acetyl-beta-neuraminate + recombinant alpha-1-antitrypsin
CMP + ?
Substrates: -
Products: -
Products: -
?
CMP-N-acetyl-beta-neuraminate + recombinant alpha-1-antitrypsin
CMP + ?
-
Substrates: -
Products: -
Products: -
?
CMP-N-acetylneuraminate + (2S,3S,4R,5R,6R)-5-acetylamino-4-hydroxy-6-methoxy-3-((2S,3R,4S,5R,6R)-3,4,5-trihydroxy-6-hydroxymethyl-tetrahydro-pyran-2-yloxy)-tetrahydro-pyran-2-carboxylic acid methyl ester
CMP + ?
-
Substrates: 160% of the activity with Galbeta(1-3)GlcNAcbeta-O-Me
Products: -
Products: -
?
CMP-N-acetylneuraminate + (2S,3S,4R,5R,6R)-5-acetylamino-4-hydroxy-6-methoxy-3-((2S,3R,4S,5R,6R)-3,4,5-trihydroxy-6-hydroxymethyl-tetrahydro-pyran-2-yloxy)-tetrahydro-pyran-2-carboxylic acid methyl ester
CMP + ?
-
Substrates: -
Products: -
Products: -
?
CMP-N-acetylneuraminate + AA-labeled 6'-sialyllactose
?
Substrates: -
Products: -
Products: -
?
CMP-N-acetylneuraminate + AA-labeled 6'-sialyllactose
?
Substrates: -
Products: -
Products: -
?
CMP-N-acetylneuraminate + AA-labeled 6'-sialyllactose
?
Substrates: -
Products: -
Products: -
?
CMP-N-acetylneuraminate + AA-labeled 6'-sialyllactose
?
Substrates: -
Products: -
Products: -
?
CMP-N-acetylneuraminate + AA-labeled G2 glycan
?
Substrates: -
Products: -
Products: -
?
CMP-N-acetylneuraminate + AA-labeled G2 glycan
?
Substrates: -
Products: -
Products: -
?
CMP-N-acetylneuraminate + AA-labeled G2 glycan
?
Substrates: -
Products: -
Products: -
?
CMP-N-acetylneuraminate + AA-labeled G2 glycan
?
Substrates: -
Products: -
Products: -
?
CMP-N-acetylneuraminate + asialo-alpha1-acid glycoprotein
CMP + alpha1-acid glycoprotein
-
Substrates: 176% of the activity with beta-D-galactosyl-1,4-N-acetyl-beta-D-glucosamine
Products: -
Products: -
?
CMP-N-acetylneuraminate + asialo-alpha1-acid glycoprotein
CMP + alpha1-acid glycoprotein
Substrates: -
Products: -
Products: -
?
CMP-N-acetylneuraminate + asialo-ceruloplasmin
CMP + ceruloplasmin
-
Substrates: -
Products: -
Products: -
?
CMP-N-acetylneuraminate + asialo-ceruloplasmin
CMP + ceruloplasmin
-
Substrates: -
Products: -
Products: -
?
CMP-N-acetylneuraminate + asialo-fetuin
CMP + fetuin
-
Substrates: -
Products: -
Products: -
?
CMP-N-acetylneuraminate + asialo-fetuin
CMP + fetuin
-
Substrates: -
Products: -
Products: -
?
CMP-N-acetylneuraminate + asialo-fetuin
CMP + fetuin
-
Substrates: -
Products: -
Products: -
?
CMP-N-acetylneuraminate + asialo-fetuin
CMP + fetuin
-
Substrates: -
Products: -
Products: -
?
CMP-N-acetylneuraminate + asialo-fetuin
CMP + fetuin
-
Substrates: best substrate
Products: -
Products: -
?
CMP-N-acetylneuraminate + asialo-fetuin
CMP + fetuin
-
Substrates: 21% of the activity with beta-D-galactosyl-1,4-N-acetyl-beta-D-glucosamine
Products: -
Products: -
?
CMP-N-acetylneuraminate + asialo-fetuin
CMP + fetuin
-
Substrates: 106% of the activity with beta-D-galactosyl-1,4-N-acetyl-beta-D-glucosamine
Products: -
Products: -
?
CMP-N-acetylneuraminate + asialo-fetuin
CMP + fetuin
-
Substrates: -
Products: -
Products: -
?
CMP-N-acetylneuraminate + asialo-fetuin
CMP + fetuin
-
Substrates: recombinant isoform STcys is somewhat more active then the recombinant isoform STtyr
Products: -
Products: -
?
CMP-N-acetylneuraminate + asialo-fetuin
CMP + fetuin
-
Substrates: -
Products: -
Products: -
?
CMP-N-acetylneuraminate + asialo-orosomucoid
CMP + orosomucoid
-
Substrates: -
Products: -
Products: -
?
CMP-N-acetylneuraminate + asialo-orosomucoid
CMP + orosomucoid
-
Substrates: best substrate
Products: -
Products: -
?
CMP-N-acetylneuraminate + asialo-orosomucoid
CMP + orosomucoid
-
Substrates: CMP-N-acetylneuraminate can be replaced with comparable or even higher transfer rates by CMP-N-glycolylneuraminate, CMP-9-O-acetyl-N-acetylneuraminate
Products: -
Products: -
?
CMP-N-acetylneuraminate + asialo-orosomucoid
CMP + orosomucoid
-
Substrates: i.e. asialo-alpha1 acid glycoprotein
Products: -
Products: -
?
CMP-N-acetylneuraminate + asialo-orosomucoid
CMP + orosomucoid
-
Substrates: best substrate
Products: -
Products: -
?
CMP-N-acetylneuraminate + asialo-orosomucoid
CMP + orosomucoid
-
Substrates: i.e. asialo-alpha1 acid glycoprotein
Products: -
Products: -
?
CMP-N-acetylneuraminate + asialo-orosomucoid
CMP + orosomucoid
-
Substrates: i.e. asialo-alpha1 acid glycoprotein
Products: -
Products: -
?
CMP-N-acetylneuraminate + asialo-orosomucoid
CMP + orosomucoid
-
Substrates: i.e. asialo-alpha1 acid glycoprotein
Products: -
Products: -
?
CMP-N-acetylneuraminate + asialo-orosomucoid
CMP + orosomucoid
-
Substrates: about half as effective as asialofetuin
Products: -
Products: -
?
CMP-N-acetylneuraminate + asialo-orosomucoid
CMP + orosomucoid
-
Substrates: -
Products: -
Products: -
?
CMP-N-acetylneuraminate + asialo-orosomucoid
CMP + orosomucoid
-
Substrates: CMP-N-acetylneuraminate can be replaced with comparable or even higher transfer rates by CMP-N-glycolylneuraminate, CMP-9-O-acetyl-N-acetylneuraminate
Products: -
Products: -
?
CMP-N-acetylneuraminate + asialo-orosomucoid
CMP + orosomucoid
-
Substrates: i.e. asialo-alpha1 acid glycoprotein
Products: -
Products: -
?
CMP-N-acetylneuraminate + asialo-orosomucoid
CMP + orosomucoid
Substrates: i.e. asialo-alpha1 acid glycoprotein
Products: -
Products: -
?
CMP-N-acetylneuraminate + asialo-orosomucoid
CMP + orosomucoid
-
Substrates: i.e. asialo-alpha1 acid glycoprotein
Products: -
Products: -
?
CMP-N-acetylneuraminate + asialo-prothrombin
CMP + prothrombin
-
Substrates: -
Products: -
Products: -
?
CMP-N-acetylneuraminate + asialo-prothrombin
CMP + prothrombin
-
Substrates: -
Products: -
Products: -
?
CMP-N-acetylneuraminate + asialo-prothrombin
CMP + prothrombin
-
Substrates: -
Products: -
Products: -
?
CMP-N-acetylneuraminate + asialo-thyroglobulin
CMP + thyroglobulin
-
Substrates: low activity
Products: -
Products: -
?
CMP-N-acetylneuraminate + asialo-thyroglobulin
CMP + thyroglobulin
-
Substrates: -
Products: -
Products: -
?
CMP-N-acetylneuraminate + asialo-transferrin
CMP + transferrin
-
Substrates: -
Products: -
Products: -
?
CMP-N-acetylneuraminate + asialo-transferrin
CMP + transferrin
-
Substrates: -
Products: -
Products: -
?
CMP-N-acetylneuraminate + asialo-transferrin
CMP + transferrin
-
Substrates: -
Products: -
Products: -
?
CMP-N-acetylneuraminate + asialo-transferrin
CMP + transferrin
-
Substrates: -
Products: -
Products: -
?
CMP-N-acetylneuraminate + asialo-transferrin
CMP + transferrin
-
Substrates: poor substrate
Products: -
Products: -
?
CMP-N-acetylneuraminate + asialo-transferrin
CMP + transferrin
-
Substrates: -
Products: -
Products: -
?
CMP-N-acetylneuraminate + asialofetuin
?
Substrates: -
Products: -
Products: -
?
CMP-N-acetylneuraminate + asialofetuin
?
Substrates: -
Products: -
Products: -
?
CMP-N-acetylneuraminate + asialofetuin
?
Substrates: -
Products: -
Products: -
?
CMP-N-acetylneuraminate + asialofetuin
?
Substrates: -
Products: -
Products: -
?
CMP-N-acetylneuraminate + beta-D-galactosyl-(1->4)-N-acetyl-beta-D-glucosamine
CMP + alpha-N-acetylneuraminyl-(2->6)-beta-D-galactosyl-(1->4)-N-acetyl-beta-D-glucosamine
-
Substrates: -
Products: -
Products: -
?
CMP-N-acetylneuraminate + beta-D-galactosyl-(1->4)-N-acetyl-beta-D-glucosamine
CMP + alpha-N-acetylneuraminyl-(2->6)-beta-D-galactosyl-(1->4)-N-acetyl-beta-D-glucosamine
Substrates: -
Products: -
Products: -
?
CMP-N-acetylneuraminate + beta-D-galactosyl-(1->4)-N-acetyl-beta-D-glucosamine
CMP + alpha-N-acetylneuraminyl-(2->6)-beta-D-galactosyl-(1->4)-N-acetyl-beta-D-glucosamine
-
Substrates: -
Products: -
Products: -
?
CMP-N-acetylneuraminate + beta-D-galactosyl-(1->4)-N-acetyl-beta-D-glucosamine
CMP + alpha-N-acetylneuraminyl-(2->6)-beta-D-galactosyl-(1->4)-N-acetyl-beta-D-glucosamine
Substrates: -
Products: -
Products: -
?
CMP-N-acetylneuraminate + beta-D-galactosyl-(1->4)-N-acetyl-beta-D-glucosamine
CMP + alpha-N-acetylneuraminyl-(2->6)-beta-D-galactosyl-(1->4)-N-acetyl-beta-D-glucosamine
-
Substrates: -
Products: -
Products: -
?
CMP-N-acetylneuraminate + beta-D-galactosyl-(1->4)-N-acetyl-beta-D-glucosamine
CMP + alpha-N-acetylneuraminyl-(2->6)-beta-D-galactosyl-(1->4)-N-acetyl-beta-D-glucosamine
Substrates: -
Products: -
Products: -
?
CMP-N-acetylneuraminate + beta-D-galactosyl-(1->4)-N-acetyl-beta-D-glucosamine
CMP + alpha-N-acetylneuraminyl-(2->6)-beta-D-galactosyl-(1->4)-N-acetyl-beta-D-glucosamine
Substrates: -
Products: -
Products: -
?
CMP-N-acetylneuraminate + beta-D-galactosyl-(1->4)-N-acetyl-beta-D-glucosamine
CMP + alpha-N-acetylneuraminyl-(2->6)-beta-D-galactosyl-(1->4)-N-acetyl-beta-D-glucosamine
Substrates: -
Products: -
Products: -
?
CMP-N-acetylneuraminate + beta-D-galactosyl-(1->4)-N-acetyl-beta-D-glucosamine
CMP + alpha-N-acetylneuraminyl-(2->6)-beta-D-galactosyl-(1->4)-N-acetyl-beta-D-glucosamine
Substrates: -
Products: -
Products: -
?
CMP-N-acetylneuraminate + beta-D-galactosyl-(1->4)-N-acetyl-beta-D-glucosamine
CMP + alpha-N-acetylneuraminyl-(2->6)-beta-D-galactosyl-(1->4)-N-acetyl-beta-D-glucosamine
Substrates: -
Products: -
Products: -
?
CMP-N-acetylneuraminate + beta-D-galactosyl-1,3-N-acetyl-beta-D-glucosaminyl-1,3-galactosyl-beta-1,4-D-glucose
CMP + alpha-N-acetylneuraminyl-2,6-beta-D-galactosyl-1,3-N-acetyl-beta-D-glucosaminyl-1,3-galactosyl-beta-1,4-D-glucose
-
Substrates: 129% of the activity with beta-D-galactosyl-1,4-N-acetyl-beta-D-glucosamine
Products: -
Products: -
?
CMP-N-acetylneuraminate + beta-D-galactosyl-1,3-N-acetyl-beta-D-glucosaminyl-1,3-galactosyl-beta-1,4-D-glucose
CMP + alpha-N-acetylneuraminyl-2,6-beta-D-galactosyl-1,3-N-acetyl-beta-D-glucosaminyl-1,3-galactosyl-beta-1,4-D-glucose
-
Substrates: 106% of the activity with beta-D-galactosyl-1,4-N-acetyl-beta-D-glucosamine
Products: -
Products: -
?
CMP-N-acetylneuraminate + beta-D-galactosyl-1,4-beta-D-glucosylceramide
CMP + alpha-N-acetylneuraminyl-2,6-beta-D-galactosyl-1,4-beta-D-glucosylceramide
-
Substrates: -
Products: i.e. ganglioside GM3
Products: i.e. ganglioside GM3
?
CMP-N-acetylneuraminate + beta-D-galactosyl-1,4-beta-D-glucosylceramide
CMP + alpha-N-acetylneuraminyl-2,6-beta-D-galactosyl-1,4-beta-D-glucosylceramide
-
Substrates: -
Products: i.e. ganglioside GM3
Products: i.e. ganglioside GM3
?
CMP-N-acetylneuraminate + beta-D-galactosyl-1,4-beta-D-glucosylceramide
CMP + alpha-N-acetylneuraminyl-2,6-beta-D-galactosyl-1,4-beta-D-glucosylceramide
-
Substrates: -
Products: i.e. ganglioside GM3
Products: i.e. ganglioside GM3
?
CMP-N-acetylneuraminate + beta-D-galactosyl-1,4-beta-D-glucosylceramide
CMP + alpha-N-acetylneuraminyl-2,6-beta-D-galactosyl-1,4-beta-D-glucosylceramide
-
Substrates: i.e. lactosylceramide
Products: i.e. ganglioside GM3
Products: i.e. ganglioside GM3
?
CMP-N-acetylneuraminate + beta-D-galactosyl-1,4-beta-D-glucosylceramide
CMP + alpha-N-acetylneuraminyl-2,6-beta-D-galactosyl-1,4-beta-D-glucosylceramide
-
Substrates: -
Products: i.e. ganglioside GM3
Products: i.e. ganglioside GM3
?
CMP-N-acetylneuraminate + beta-D-galactosyl-1,4-N-acetyl-beta-D-glucosamine
CMP + alpha-N-acetylneuraminyl-2,6-beta-D-galactosyl-1,4-N-acetyl-beta-D-glucosamine
-
Substrates: best substrate
Products: -
Products: -
?
CMP-N-acetylneuraminate + beta-D-galactosyl-1,4-N-acetyl-beta-D-glucosamine
CMP + alpha-N-acetylneuraminyl-2,6-beta-D-galactosyl-1,4-N-acetyl-beta-D-glucosamine
-
Substrates: i.e. N-acetyllactosamine
Products: -
Products: -
?
CMP-N-acetylneuraminate + beta-D-galactosyl-1,4-N-acetyl-beta-D-glucosamine
CMP + alpha-N-acetylneuraminyl-2,6-beta-D-galactosyl-1,4-N-acetyl-beta-D-glucosamine
-
Substrates: most active disaccharide substrate
Products: -
Products: -
?
CMP-N-acetylneuraminate + beta-D-galactosyl-1,4-N-acetyl-beta-D-glucosamine
CMP + alpha-N-acetylneuraminyl-2,6-beta-D-galactosyl-1,4-N-acetyl-beta-D-glucosamine
-
Substrates: i.e. N-acetyllactosamine
Products: -
Products: -
?
CMP-N-acetylneuraminate + beta-D-galactosyl-1,4-N-acetyl-beta-D-glucosamine
CMP + alpha-N-acetylneuraminyl-2,6-beta-D-galactosyl-1,4-N-acetyl-beta-D-glucosamine
-
Substrates: most active disaccharide substrate
Products: -
Products: -
?
CMP-N-acetylneuraminate + beta-D-galactosyl-1,4-N-acetyl-beta-D-glucosamine
CMP + alpha-N-acetylneuraminyl-2,6-beta-D-galactosyl-1,4-N-acetyl-beta-D-glucosamine
Substrates: -
Products: -
Products: -
?
CMP-N-acetylneuraminate + beta-D-galactosyl-1,4-N-acetyl-beta-D-glucosamine
CMP + alpha-N-acetylneuraminyl-2,6-beta-D-galactosyl-1,4-N-acetyl-beta-D-glucosamine
-
Substrates: -
Products: -
Products: -
?
CMP-N-acetylneuraminate + beta-D-galactosyl-1,4-N-acetyl-beta-D-glucosamine
CMP + alpha-N-acetylneuraminyl-2,6-beta-D-galactosyl-1,4-N-acetyl-beta-D-glucosamine
Substrates: highest activity
Products: -
Products: -
?
CMP-N-acetylneuraminate + beta-D-galactosyl-1,4-N-acetyl-beta-D-glucosamine
CMP + alpha-N-acetylneuraminyl-2,6-beta-D-galactosyl-1,4-N-acetyl-beta-D-glucosamine
Substrates: highest activity
Products: -
Products: -
?
CMP-N-acetylneuraminate + beta-D-galactosyl-1,4-N-acetyl-beta-D-glucosamine
CMP + alpha-N-acetylneuraminyl-2,6-beta-D-galactosyl-1,4-N-acetyl-beta-D-glucosamine
-
Substrates: i.e. N-acetyllactosamine
Products: -
Products: -
?
CMP-N-acetylneuraminate + beta-D-galactosyl-1,4-N-acetyl-beta-D-glucosamine
CMP + alpha-N-acetylneuraminyl-2,6-beta-D-galactosyl-1,4-N-acetyl-beta-D-glucosamine
-
Substrates: most active disaccharide substrate
Products: -
Products: -
?
CMP-N-acetylneuraminate + beta-D-galactosyl-1,4-N-acetyl-beta-D-glucosamine
CMP + alpha-N-acetylneuraminyl-2,6-beta-D-galactosyl-1,4-N-acetyl-beta-D-glucosamine
-
Substrates: poor substrate
Products: -
Products: -
?
CMP-N-acetylneuraminate + beta-D-galactosyl-1,4-N-acetyl-beta-D-glucosamine
CMP + alpha-N-acetylneuraminyl-2,6-beta-D-galactosyl-1,4-N-acetyl-beta-D-glucosamine
-
Substrates: i.e. N-acetyllactosamine
Products: -
Products: -
?
CMP-N-acetylneuraminate + beta-D-galactosyl-1,4-N-acetyl-beta-D-glucosamine
CMP + alpha-N-acetylneuraminyl-2,6-beta-D-galactosyl-1,4-N-acetyl-beta-D-glucosamine
-
Substrates: -
Products: -
Products: -
?
CMP-N-acetylneuraminate + beta-D-galactosyl-1,4-N-acetyl-beta-D-glucosamine
CMP + alpha-N-acetylneuraminyl-2,6-beta-D-galactosyl-1,4-N-acetyl-beta-D-glucosamine
-
Substrates: i.e. N-acetyllactosamine
Products: -
Products: -
?
CMP-N-acetylneuraminate + beta-D-galactosyl-1,4-N-acetyl-beta-D-glucosamine
CMP + alpha-N-acetylneuraminyl-2,6-beta-D-galactosyl-1,4-N-acetyl-beta-D-glucosamine
-
Substrates: -
Products: -
Products: -
?
CMP-N-acetylneuraminate + beta-D-galactosyl-1,4-N-acetyl-beta-D-glucosamine
CMP + alpha-N-acetylneuraminyl-2,6-beta-D-galactosyl-1,4-N-acetyl-beta-D-glucosamine
Substrates: 100% activity
Products: -
Products: -
?
CMP-N-acetylneuraminate + beta-D-galactosyl-1,4-N-acetyl-beta-D-glucosamine
CMP + alpha-N-acetylneuraminyl-2,6-beta-D-galactosyl-1,4-N-acetyl-beta-D-glucosamine
Substrates: -
Products: -
Products: -
?
CMP-N-acetylneuraminate + beta-D-galactosyl-1,4-N-acetyl-beta-D-glucosamine
CMP + alpha-N-acetylneuraminyl-2,6-beta-D-galactosyl-1,4-N-acetyl-beta-D-glucosamine
-
Substrates: i.e. N-acetyllactosamine
Products: -
Products: -
?
CMP-N-acetylneuraminate + beta-D-galactosyl-1,4-N-acetyl-beta-D-glucosamine
CMP + alpha-N-acetylneuraminyl-2,6-beta-D-galactosyl-1,4-N-acetyl-beta-D-glucosamine
-
Substrates: i.e. N-acetyllactosamine
Products: -
Products: -
?
CMP-N-acetylneuraminate + beta-D-galactosyl-1,4-N-acetyl-beta-D-glucosamine
CMP + alpha-N-acetylneuraminyl-2,6-beta-D-galactosyl-1,4-N-acetyl-beta-D-glucosamine
-
Substrates: i.e. N-acetyllactosamine
Products: -
Products: -
?
CMP-N-acetylneuraminate + beta-D-galactosyl-1,4-N-acetyl-beta-D-glucosamine
CMP + alpha-N-acetylneuraminyl-2,6-beta-D-galactosyl-1,4-N-acetyl-beta-D-glucosamine
-
Substrates: -
Products: -
Products: -
?
CMP-N-acetylneuraminate + beta-D-galactosyl-1,4-N-acetyl-beta-D-glucosamine
CMP + alpha-N-acetylneuraminyl-2,6-beta-D-galactosyl-1,4-N-acetyl-beta-D-glucosamine
-
Substrates: -
Products: -
Products: -
?
CMP-N-acetylneuraminate + beta-D-galactosyl-1,4-N-acetyl-beta-D-glucosaminyl-R
CMP + alpha-N-acetylneuraminyl-2,6-beta-D-galactosyl-1,4-N-acetyl-beta-D-glucosaminyl-R
-
Substrates: acceptor substrate specificity
Products: -
Products: -
?
CMP-N-acetylneuraminate + beta-D-galactosyl-1,4-N-acetyl-beta-D-glucosaminyl-R
CMP + alpha-N-acetylneuraminyl-2,6-beta-D-galactosyl-1,4-N-acetyl-beta-D-glucosaminyl-R
-
Substrates: R: glycoprotein or glycopeptide
Products: -
Products: -
?
CMP-N-acetylneuraminate + beta-D-galactosyl-1,4-N-acetyl-beta-D-glucosaminyl-R
CMP + alpha-N-acetylneuraminyl-2,6-beta-D-galactosyl-1,4-N-acetyl-beta-D-glucosaminyl-R
-
Substrates: transfers sialic acid to terminal positions on N-linked glycans
Products: -
Products: -
?
CMP-N-acetylneuraminate + beta-D-galactosyl-1,4-N-acetyl-beta-D-glucosaminyl-R
CMP + alpha-N-acetylneuraminyl-2,6-beta-D-galactosyl-1,4-N-acetyl-beta-D-glucosaminyl-R
-
Substrates: sialic acid is linked to C-6 of the galactose residue
Products: -
Products: -
?
CMP-N-acetylneuraminate + beta-D-galactosyl-1,4-N-acetyl-beta-D-glucosaminyl-R
CMP + alpha-N-acetylneuraminyl-2,6-beta-D-galactosyl-1,4-N-acetyl-beta-D-glucosaminyl-R
-
Substrates: transfers sialic acid to the terminal galactose residue of asialo-gyloproteins and peptides
Products: -
Products: -
?
CMP-N-acetylneuraminate + beta-D-galactosyl-1,4-N-acetyl-beta-D-glucosaminyl-R
CMP + alpha-N-acetylneuraminyl-2,6-beta-D-galactosyl-1,4-N-acetyl-beta-D-glucosaminyl-R
-
Substrates: strictly specific for CMP-N-acetylneuraminate, forms only alpha2,6-linkages
Products: -
Products: -
?
CMP-N-acetylneuraminate + beta-D-galactosyl-1,4-N-acetyl-beta-D-glucosaminyl-R
CMP + alpha-N-acetylneuraminyl-2,6-beta-D-galactosyl-1,4-N-acetyl-beta-D-glucosaminyl-R
-
Substrates: high molecular weight substrates are more efficient acceptors than low molecular weight substrates
Products: -
Products: -
?
CMP-N-acetylneuraminate + beta-D-galactosyl-1,4-N-acetyl-beta-D-glucosaminyl-R
CMP + alpha-N-acetylneuraminyl-2,6-beta-D-galactosyl-1,4-N-acetyl-beta-D-glucosaminyl-R
-
Substrates: one of a group of glycosyltransferases which act to assemble the carbohydrate units of thyroglobulin
Products: -
Products: -
?
CMP-N-acetylneuraminate + beta-D-galactosyl-1,4-N-acetyl-beta-D-glucosaminyl-R
CMP + alpha-N-acetylneuraminyl-2,6-beta-D-galactosyl-1,4-N-acetyl-beta-D-glucosaminyl-R
-
Substrates: final step in synthesis of serum-type glycoproteins
Products: -
Products: -
?
CMP-N-acetylneuraminate + beta-D-galactosyl-1,4-N-acetyl-beta-D-glucosaminyl-R
CMP + alpha-N-acetylneuraminyl-2,6-beta-D-galactosyl-1,4-N-acetyl-beta-D-glucosaminyl-R
-
Substrates: acceptor substrate specificity
Products: -
Products: -
?
CMP-N-acetylneuraminate + beta-D-galactosyl-1,4-N-acetyl-beta-D-glucosaminyl-R
CMP + alpha-N-acetylneuraminyl-2,6-beta-D-galactosyl-1,4-N-acetyl-beta-D-glucosaminyl-R
-
Substrates: sialic acid is linked to C-6 of the galactose residue
Products: -
Products: -
?
CMP-N-acetylneuraminate + beta-D-galactosyl-1,4-N-acetyl-beta-D-glucosaminyl-R
CMP + alpha-N-acetylneuraminyl-2,6-beta-D-galactosyl-1,4-N-acetyl-beta-D-glucosaminyl-R
-
Substrates: high molecular weight substrates are more efficient acceptors than low molecular weight substrates
Products: -
Products: -
?
CMP-N-acetylneuraminate + beta-D-galactosyl-1,4-N-acetyl-beta-D-glucosaminyl-R
CMP + alpha-N-acetylneuraminyl-2,6-beta-D-galactosyl-1,4-N-acetyl-beta-D-glucosaminyl-R
-
Substrates: final step in synthesis of serum-type glycoproteins
Products: -
Products: -
?
CMP-N-acetylneuraminate + beta-D-galactosyl-1,4-N-acetyl-beta-D-glucosaminyl-R
CMP + alpha-N-acetylneuraminyl-2,6-beta-D-galactosyl-1,4-N-acetyl-beta-D-glucosaminyl-R
-
Substrates: sialic acid is linked to C-6 of the galactose residue
Products: -
Products: -
?
CMP-N-acetylneuraminate + beta-D-galactosyl-1,4-N-acetyl-beta-D-glucosaminyl-R
CMP + alpha-N-acetylneuraminyl-2,6-beta-D-galactosyl-1,4-N-acetyl-beta-D-glucosaminyl-R
-
Substrates: acceptor substrate specificity
Products: -
Products: -
?
CMP-N-acetylneuraminate + beta-D-galactosyl-1,4-N-acetyl-beta-D-glucosaminyl-R
CMP + alpha-N-acetylneuraminyl-2,6-beta-D-galactosyl-1,4-N-acetyl-beta-D-glucosaminyl-R
-
Substrates: transfers sialic acid to terminal positions on N-linked glycans
Products: -
Products: -
?
CMP-N-acetylneuraminate + beta-D-galactosyl-1,4-N-acetyl-beta-D-glucosaminyl-R
CMP + alpha-N-acetylneuraminyl-2,6-beta-D-galactosyl-1,4-N-acetyl-beta-D-glucosaminyl-R
-
Substrates: sialic acid is linked to C-6 of the galactose residue
Products: -
Products: -
?
CMP-N-acetylneuraminate + beta-D-galactosyl-1,4-N-acetyl-beta-D-glucosaminyl-R
CMP + alpha-N-acetylneuraminyl-2,6-beta-D-galactosyl-1,4-N-acetyl-beta-D-glucosaminyl-R
-
Substrates: substrate specificity for several synthetic trisaccharides
Products: -
Products: -
?
CMP-N-acetylneuraminate + beta-D-galactosyl-1,4-N-acetyl-beta-D-glucosaminyl-R
CMP + alpha-N-acetylneuraminyl-2,6-beta-D-galactosyl-1,4-N-acetyl-beta-D-glucosaminyl-R
-
Substrates: high molecular weight substrates are more efficient acceptors than low molecular weight substrates
Products: -
Products: -
?
CMP-N-acetylneuraminate + beta-D-galactosyl-1,4-N-acetyl-beta-D-glucosaminyl-R
CMP + alpha-N-acetylneuraminyl-2,6-beta-D-galactosyl-1,4-N-acetyl-beta-D-glucosaminyl-R
-
Substrates: CMP-N-acetylneuraminate analogues can serve as donor substrates, i.e. formyl-, trifluoroacetyl-, benzyloxycarbonyl-, and amino acetyl-N-neuraminates
Products: -
Products: -
?
CMP-N-acetylneuraminate + beta-D-galactosyl-1,4-N-acetyl-beta-D-glucosaminyl-R
CMP + alpha-N-acetylneuraminyl-2,6-beta-D-galactosyl-1,4-N-acetyl-beta-D-glucosaminyl-R
-
Substrates: final step in synthesis of serum-type glycoproteins
Products: -
Products: -
?
CMP-N-acetylneuraminate + beta-D-galactosyl-1,4-N-acetyl-beta-D-glucosaminyl-R
CMP + alpha-N-acetylneuraminyl-2,6-beta-D-galactosyl-1,4-N-acetyl-beta-D-glucosaminyl-R
-
Substrates: sialic acid is linked to C-6 of the galactose residue
Products: -
Products: -
?
CMP-N-acetylneuraminate + beta-D-galactosyl-1,4-N-acetyl-beta-D-glucosaminyl-R
CMP + alpha-N-acetylneuraminyl-2,6-beta-D-galactosyl-1,4-N-acetyl-beta-D-glucosaminyl-R
-
Substrates: acceptor substrate specificity
Products: -
Products: -
?
CMP-N-acetylneuraminate + beta-D-galactosyl-1,4-N-acetyl-beta-D-glucosaminyl-R
CMP + alpha-N-acetylneuraminyl-2,6-beta-D-galactosyl-1,4-N-acetyl-beta-D-glucosaminyl-R
-
Substrates: sialic acid is linked to C-6 of the galactose residue
Products: -
Products: -
?
CMP-N-acetylneuraminate + beta-D-galactosyl-1,4-N-acetyl-beta-D-glucosaminyl-R
CMP + alpha-N-acetylneuraminyl-2,6-beta-D-galactosyl-1,4-N-acetyl-beta-D-glucosaminyl-R
-
Substrates: strictly specific for CMP-N-acetylneuraminate, forms only alpha2,6-linkages
Products: -
Products: -
?
CMP-N-acetylneuraminate + beta-D-galactosyl-1,4-N-acetyl-beta-D-glucosaminyl-R
CMP + alpha-N-acetylneuraminyl-2,6-beta-D-galactosyl-1,4-N-acetyl-beta-D-glucosaminyl-R
-
Substrates: sialic acid is linked to C-6 of the galactose residue
Products: -
Products: -
?
CMP-N-acetylneuraminate + beta-D-galactosyl-1,4-N-acetyl-beta-D-glucosaminyl-R
CMP + alpha-N-acetylneuraminyl-2,6-beta-D-galactosyl-1,4-N-acetyl-beta-D-glucosaminyl-R
-
Substrates: strictly specific for CMP-N-acetylneuraminate, forms only alpha2,6-linkages
Products: -
Products: -
?
CMP-N-acetylneuraminate + beta-D-galactosyl-1,4-N-acetyl-beta-D-glucosaminyl-R
CMP + alpha-N-acetylneuraminyl-2,6-beta-D-galactosyl-1,4-N-acetyl-beta-D-glucosaminyl-R
-
Substrates: acceptor substrate specificity
Products: -
Products: -
?
CMP-N-acetylneuraminate + beta-D-galactosyl-1,4-N-acetyl-beta-D-glucosaminyl-R
CMP + alpha-N-acetylneuraminyl-2,6-beta-D-galactosyl-1,4-N-acetyl-beta-D-glucosaminyl-R
-
Substrates: sialic acid is linked to C-6 of the galactose residue
Products: -
Products: -
?
CMP-N-acetylneuraminate + beta-D-galactosyl-1,4-N-acetyl-beta-D-glucosaminyl-R
CMP + alpha-N-acetylneuraminyl-2,6-beta-D-galactosyl-1,4-N-acetyl-beta-D-glucosaminyl-R
-
Substrates: strictly specific for CMP-N-acetylneuraminate, forms only alpha2,6-linkages
Products: -
Products: -
?
CMP-N-acetylneuraminate + beta-D-galactosyl-1,4-N-acetyl-beta-D-glucosaminyl-R
CMP + alpha-N-acetylneuraminyl-2,6-beta-D-galactosyl-1,4-N-acetyl-beta-D-glucosaminyl-R
-
Substrates: acceptor substrate specificity
Products: -
Products: -
?
CMP-N-acetylneuraminate + beta-D-galactosyl-1,4-N-acetyl-beta-D-glucosaminyl-R
CMP + alpha-N-acetylneuraminyl-2,6-beta-D-galactosyl-1,4-N-acetyl-beta-D-glucosaminyl-R
-
Substrates: R: glycoprotein or glycopeptide
Products: -
Products: -
?
CMP-N-acetylneuraminate + beta-D-galactosyl-1,4-N-acetyl-beta-D-glucosaminyl-R
CMP + alpha-N-acetylneuraminyl-2,6-beta-D-galactosyl-1,4-N-acetyl-beta-D-glucosaminyl-R
-
Substrates: transfers sialic acid to terminal positions on N-linked glycans
Products: -
Products: -
?
CMP-N-acetylneuraminate + beta-D-galactosyl-1,4-N-acetyl-beta-D-glucosaminyl-R
CMP + alpha-N-acetylneuraminyl-2,6-beta-D-galactosyl-1,4-N-acetyl-beta-D-glucosaminyl-R
-
636798, 636803, 637267, 637269, 637270, 637271, 637283, 637284, 637285, 637288, 637291, 637293, 637294, 637295, 637297
Substrates: sialic acid is linked to C-6 of the galactose residue
Products: -
Products: -
?
CMP-N-acetylneuraminate + beta-D-galactosyl-1,4-N-acetyl-beta-D-glucosaminyl-R
CMP + alpha-N-acetylneuraminyl-2,6-beta-D-galactosyl-1,4-N-acetyl-beta-D-glucosaminyl-R
Substrates: sialic acid is linked to C-6 of the galactose residue
Products: -
Products: -
?
CMP-N-acetylneuraminate + beta-D-galactosyl-1,4-N-acetyl-beta-D-glucosaminyl-R
CMP + alpha-N-acetylneuraminyl-2,6-beta-D-galactosyl-1,4-N-acetyl-beta-D-glucosaminyl-R
-
Substrates: CMP-N-acetylneuraminate analogues can serve as donor substrates, i.e. the 5''-amino-, the 5''-N-pentanoylamino-, the 5''-glycylamino-, and the 5''-ethoxycarbonylamino derivative and diammonium (cytidin-5'-yl) [(3-deoxy-D-glycero-beta-D-galacto-2-nonulpyranosyl)onate] phosphate
Products: -
Products: -
?
CMP-N-acetylneuraminate + beta-D-galactosyl-1,4-N-acetyl-beta-D-glucosaminyl-R
CMP + alpha-N-acetylneuraminyl-2,6-beta-D-galactosyl-1,4-N-acetyl-beta-D-glucosaminyl-R
-
Substrates: the non-reducing terminal galactosyl residue is essential for activity
Products: -
Products: -
?
CMP-N-acetylneuraminate + beta-D-galactosyl-1,4-N-acetyl-beta-D-glucosaminyl-R
CMP + alpha-N-acetylneuraminyl-2,6-beta-D-galactosyl-1,4-N-acetyl-beta-D-glucosaminyl-R
-
Substrates: substrate specificity for several synthetic trisaccharides
Products: -
Products: -
?
CMP-N-acetylneuraminate + beta-D-galactosyl-1,4-N-acetyl-beta-D-glucosaminyl-R
CMP + alpha-N-acetylneuraminyl-2,6-beta-D-galactosyl-1,4-N-acetyl-beta-D-glucosaminyl-R
-
Substrates: synthetic disaccharides
Products: -
Products: -
?
CMP-N-acetylneuraminate + beta-D-galactosyl-1,4-N-acetyl-beta-D-glucosaminyl-R
CMP + alpha-N-acetylneuraminyl-2,6-beta-D-galactosyl-1,4-N-acetyl-beta-D-glucosaminyl-R
-
Substrates: CMP-N-acetylneuraminate analogues can serve as donor substrates, i.e. formyl-, trifluoroacetyl-, benzyloxycarbonyl-, and amino acetyl-N-neuraminates
Products: -
Products: -
?
CMP-N-acetylneuraminate + beta-D-galactosyl-1,4-N-acetyl-beta-D-glucosaminyl-R
CMP + alpha-N-acetylneuraminyl-2,6-beta-D-galactosyl-1,4-N-acetyl-beta-D-glucosaminyl-R
-
Substrates: donor substrate specificity
Products: -
Products: -
?
CMP-N-acetylneuraminate + beta-D-galactosyl-1,4-N-acetyl-beta-D-glucosaminyl-R
CMP + alpha-N-acetylneuraminyl-2,6-beta-D-galactosyl-1,4-N-acetyl-beta-D-glucosaminyl-R
-
Substrates: R: glycoprotein or glycopeptide
Products: -
Products: -
?
CMP-N-acetylneuraminate + beta-D-galactosyl-1,4-N-acetyl-beta-D-glucosaminyl-R
CMP + alpha-N-acetylneuraminyl-2,6-beta-D-galactosyl-1,4-N-acetyl-beta-D-glucosaminyl-R
-
Substrates: regulation of enzyme expression
Products: -
Products: -
?
CMP-N-acetylneuraminate + beta-D-galactosyl-1,4-N-acetyl-beta-D-glucosaminyl-R
CMP + alpha-N-acetylneuraminyl-2,6-beta-D-galactosyl-1,4-N-acetyl-beta-D-glucosaminyl-R
-
Substrates: R: glycoprotein or glycopeptide
Products: -
Products: -
?
CMP-N-acetylneuraminate + beta-D-galactosyl-1,4-N-acetyl-beta-D-glucosaminyl-R
CMP + alpha-N-acetylneuraminyl-2,6-beta-D-galactosyl-1,4-N-acetyl-beta-D-glucosaminyl-R
-
Substrates: sialic acid is linked to C-6 of the galactose residue
Products: -
Products: -
?
CMP-N-acetylneuraminate + beta-D-galactosyl-1,4-N-acetyl-beta-D-glucosaminyl-R
CMP + alpha-N-acetylneuraminyl-2,6-beta-D-galactosyl-1,4-N-acetyl-beta-D-glucosaminyl-R
-
Substrates: the non-reducing terminal galactosyl residue is essential for activity
Products: -
Products: -
?
CMP-N-acetylneuraminate + beta-D-galactosyl-1,4-N-acetyl-beta-D-glucosaminyl-R
CMP + alpha-N-acetylneuraminyl-2,6-beta-D-galactosyl-1,4-N-acetyl-beta-D-glucosaminyl-R
-
Substrates: acceptor substrate specificity
Products: -
Products: -
?
CMP-N-acetylneuraminate + beta-D-galactosyl-1,4-N-acetyl-beta-D-glucosaminyl-R
CMP + alpha-N-acetylneuraminyl-2,6-beta-D-galactosyl-1,4-N-acetyl-beta-D-glucosaminyl-R
-
Substrates: sialic acid is linked to C-6 of the galactose residue
Products: -
Products: -
?
CMP-N-acetylneuraminate + beta-D-galactosyl-1,4-N-acetyl-beta-D-glucosaminyl-R
CMP + alpha-N-acetylneuraminyl-2,6-beta-D-galactosyl-1,4-N-acetyl-beta-D-glucosaminyl-R
-
Substrates: synthetic disaccharides
Products: -
Products: -
?
CMP-N-acetylneuraminate + fetuin
?
-
Substrates: about 30% as effective as asialofetuin
Products: -
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?
CMP-N-acetylneuraminate + lacto-N-neotetraose
?
-
Substrates: -
Products: -
Products: -
?
CMP-N-acetylneuraminate + lacto-N-tetraose
CMP + ?
-
Substrates: 36.8% of the activity with beta-D-galactosyl-1,4-N-acetyl-beta-D-glucosamine
Products: -
Products: -
?
CMP-N-acetylneuraminate + lacto-N-tetraose
CMP + ?
Substrates: 35% activity compared to beta-D-galactosyl-1,4-N-acetyl-beta-D-glucosamine
Products: -
Products: -
?
CMP-N-acetylneuraminate + lactose
CMP + 6'-sialyllactose
-
Substrates: -
Products: -
Products: -
?
CMP-N-acetylneuraminate + lactose
CMP + 6'-sialyllactose
-
Substrates: no activity
Products: -
Products: -
?
CMP-N-acetylneuraminate + lactose
CMP + 6'-sialyllactose
-
Substrates: poor substrate
Products: -
Products: -
?
CMP-N-acetylneuraminate + lactose
CMP + 6'-sialyllactose
-
Substrates: -
Products: -
Products: -
?
CMP-N-acetylneuraminate + lactose
CMP + 6'-sialyllactose
-
Substrates: -
Products: -
Products: -
?
CMP-N-acetylneuraminate + lactose
CMP + 6'-sialyllactose
Substrates: 14% activity compared to beta-D-galactosyl-1,4-N-acetyl-beta-D-glucosamine
Products: -
Products: -
?
CMP-N-acetylneuraminate + lactose
CMP + 6'-sialyllactose
-
Substrates: -
Products: -
Products: -
?
CMP-N-acetylneuraminate + lactose
CMP + 6'-sialyllactose
-
Substrates: -
Products: -
Products: -
?
CMP-N-acetylneuraminate + lactose
CMP + 6'-sialyllactose
-
Substrates: -
Products: -
Products: -
?
CMP-N-acetylneuraminate + lactose
CMP + 6'-sialyllactose
-
Substrates: -
Products: -
Products: -
?
CMP-N-acetylneuraminate + lactose
CMP + 6'-sialyllactose
Substrates: Asp232 might act as a catalytic base for deprotonation of the acceptor substrate, and His405 might act as a catalytic acid for protonation of the donor substrate
Products: -
Products: -
?
CMP-N-acetylneuraminate + lactose
CMP + 6'-sialyllactose
Substrates: -
Products: -
Products: -
?
CMP-N-acetylneuraminate + lactose
CMP + 6'-sialyllactose
-
Substrates: poor substrate
Products: -
Products: -
?
CMP-N-acetylneuraminate + lactose
CMP + 6'-sialyllactose
-
Substrates: -
Products: -
Products: -
?
CMP-N-acetylneuraminate + N-acetyllactosamine
?
Substrates: 99% of the activity with lactose
Products: -
Products: -
?
CMP-N-acetylneuraminate + N-acetyllactosamine
?
Substrates: -
Products: -
Products: -
?
CMP-N-acetylneuraminate + submaxillary asialo-mucin
CMP + submaxillary mucin
-
Substrates: poor substrates, no activity with ovine acceptor
Products: -
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?
CMP-N-acetylneuraminate + submaxillary asialo-mucin
CMP + submaxillary mucin
-
Substrates: -
Products: -
Products: -
?
CMP-N-acetylneuraminate + tumor necrosis factor receptor 1
CMP + alpha2,6-sialyated tumor necrosis factor receptor 1
Substrates: -
Products: -
Products: -
?
CMP-N-acetylneuraminate + tumor necrosis factor receptor 1
CMP + alpha2,6-sialyated tumor necrosis factor receptor 1
Substrates: -
Products: -
Products: -
?
CMP-N-aminoacetylneuraminate + asialo-alpha1-acid glycoprotein
?
-
Substrates: -
Products: -
Products: -
?
CMP-N-aminoacetylneuraminate + asialo-alpha1-acid glycoprotein
?
-
Substrates: -
Products: -
Products: -
?
CMP-N-formylneuraminate + asialo-alpha1-acid glycoprotein
?
-
Substrates: -
Products: -
Products: -
?
CMP-N-formylneuraminate + asialo-alpha1-acid glycoprotein
?
-
Substrates: -
Products: -
Products: -
?
CMP-N-glycolylneuraminate + asialo-alpha1-acid glycoprotein
?
-
Substrates: comparable or even higher transfer rates than with CMP-N-acetylneuraminate
Products: -
Products: -
?
CMP-N-glycolylneuraminate + asialo-alpha1-acid glycoprotein
?
-
Substrates: comparable or even higher transfer rates than with CMP-N-acetylneuraminate
Products: -
Products: -
?
CMP-Neu5Ac + lactose
CMP + Neu5Acalpha(2-6)Lac
-
Substrates: alpha2,6-sialyltransferase activity
Products: -
Products: -
?
CMP-Neu5Ac + lactose
CMP + Neu5Acalpha(2-6)Lac
-
Substrates: alpha2,6-sialyltransferase activity
Products: -
Products: -
?
CMP-Neu5Ac + methyl-beta-D-galactopyranoside
CMP + Neu5Acalpha(2-6)Gal-alpha-methyl
-
Substrates: alpha2,6-sialyltransferase activity
Products: -
Products: -
?
CMP-Neu5Ac + methyl-beta-D-galactopyranoside
CMP + Neu5Acalpha(2-6)Gal-alpha-methyl
-
Substrates: alpha2,6-sialyltransferase activity
Products: -
Products: -
?
CMP-Neu5Ac + N-acetyllactosamine
CMP + Neu5Acalpha(2-6)LacNAc
-
Substrates: alpha2,6-sialyltransferase activity
Products: -
Products: -
?
CMP-Neu5Ac + N-acetyllactosamine
CMP + Neu5Acalpha(2-6)LacNAc
-
Substrates: alpha2,6-sialyltransferase activity
Products: -
Products: -
?
additional information
?
-
-
Substrates: no activity towards Glcalpha-4-nitrophenyl, Galalpha-4-nitrophenyl, GalNAcalpha-4-nitrophenyl, Galbeta(1,3)-GalNAcbeta-4-nitrophenyl and GalNAcbeta(1,3)-GlcNAcbeta-4-nitrophenyl
Products: -
Products: -
?
additional information
?
-
-
Substrates: no activity with galactosylhydroxylysine and its derivatives, or galactose-containing oligosaccharides linked to Ser/Thr-glycopeptide of earthworm cuticle collagen
Products: -
Products: -
?
additional information
?
-
-
Substrates: no transfer to terminal N-acetyl-D-galactosamine
Products: -
Products: -
?
additional information
?
-
-
Substrates: no activity with beta-methyl-L-arabinopyranoside
Products: -
Products: -
?
additional information
?
-
-
Substrates: no activity with submaxillary asialo-mucin
Products: -
Products: -
?
additional information
?
-
-
Substrates: galactose-free glycopeptides are poor substrates
Products: -
Products: -
?
additional information
?
-
-
Substrates: no activity with antifreeze glycoprotein
Products: -
Products: -
?
additional information
?
-
-
Substrates: poor substrates are the beta-1,3- or beta-1,6-derivatives of beta-D-galactosyl-1,4-N-acetyl-beta-D-glucosamine
Products: -
Products: -
?
additional information
?
-
-
Substrates: no activity with galactose, lactose and N-acetyllactose
Products: -
Products: -
?
additional information
?
-
-
Substrates: no activity with ovine submaxillary asialo-mucin
Products: -
Products: -
?
additional information
?
-
-
Substrates: no activity with ovine submaxillary asialo-mucin
Products: -
Products: -
?
additional information
?
-
Substrates: the enzyme uses the LacdiNAc structure (GalNAcbeta1,4GlcNAc) as a better acceptor substrate than the type II (Galbeta1-4GlcNAc) disaccharide. The enzyme's efficiency is improved when the acceptor substrate is provided as a free oligosaccharide rather than as a protein-bound oligosaccharide. No activity with alpha1-acidglycoprotein and Galbeta13GlcNAc-octyl
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme uses the LacdiNAc structure (GalNAcbeta1,4GlcNAc) as a better acceptor substrate than the type II (Galbeta1-4GlcNAc) disaccharide. The enzyme's efficiency is improved when the acceptor substrate is provided as a free oligosaccharide rather than as a protein-bound oligosaccharide. No activity with alpha1-acidglycoprotein and Galbeta13GlcNAc-octyl
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme prefers to attach sialic acid to the Gal on the Manalpha(1->3)-arm of the core. Galbeta(l->4)GlcNAc and glycopeptides and glycoproteins with Galbeta(l->4)GlcNAc termini are the only good acceptors. Galbeta(l->3)GalNAc-terminal glycoproteins are not acceptors for enzyme
Products: -
Products: -
?
additional information
?
-
-
Substrates: no activity with submaxillary asialo-mucin
Products: -
Products: -
?
additional information
?
-
Substrates: no activity with Gal-beta1,3-GlcNAc, T-antigen Gal-beta1,3-GalNAc-alpha, and NeuAc-alpha2,3-Gal-beta1,4-Glc
Products: -
Products: -
?
additional information
?
-
-
Substrates: no activity with Gal-beta1,3-GlcNAc, T-antigen Gal-beta1,3-GalNAc-alpha, and NeuAc-alpha2,3-Gal-beta1,4-Glc
Products: -
Products: -
?
additional information
?
-
Substrates: no activity with Gal-beta1,3-GlcNAc, T-antigen Gal-beta1,3-GalNAc-alpha, and NeuAc-alpha2,3-Gal-beta1,4-Glc
Products: -
Products: -
?
additional information
?
-
-
Substrates: no activity with Gal-beta1,3-GlcNAc, T-antigen Gal-beta1,3-GalNAc-alpha, and NeuAc-alpha2,3-Gal-beta1,4-Glc
Products: -
Products: -
?
additional information
?
-
-
Substrates: the catalytic domain can proceed with sialic acid transfer with increased efficiency until 80 amino acid are deleted
Products: -
Products: -
?
additional information
?
-
-
Substrates: no activity with N-acetyl-D-galactosamine or N-acetyl-D-glucosamine, and asialo-agalacto-fetuin, and galactose
Products: -
Products: -
?
additional information
?
-
-
Substrates: no activity with Lc4Cer and Lc3Cer
Products: -
Products: -
?
additional information
?
-
-
Substrates: soluble ST6Gal I produced by BACE1 plays, at least in part, a role in the sialylation of soluble glycoproteins
Products: -
Products: -
?
additional information
?
-
Substrates: radiation exposure is found to increase the sialylation of glycoproteins such as integrin beta1 by inducing the expression of ST6Gal I, and increased protein sialylation contributed to cellular radiation resistance
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme transfers Neu5Ac of CMP-Neu5Ac to the 6-hydroxyl group on internal GalNAc on O-glycans with strict specificities towards the O-glycan GalNAcalpha- (Tnantigen), Galbeta1-3GalNAcalpha- (T-antigen) and Neu5Acalpha2-3Galbeta1-3GalNAcalpha- (sialyl T-antigen) structures. hST6GalNAc-I shows activities towards O-linked oligosaccharides attached to peptides of glycoproteins and weak activities towards synthetic non-amino acid aglycons of O-glycans hST6GalNAc-I. hST6GalNAc-I shows strong activities with core 2 glycans (Galbeta1-3GalNAcbeta[GlcNAcbeta1-6]GalNAc). Core 2 O-glycan structures lacking the terminal galactose such as core 6 (GlcNAcbeta1-6GalNAcalpha-) or substituted with other monosaccharides such as core 4 (GlcNAcbeta1-3[GlcNAcbeta1-6]GalNAcalpha-) do not give any signal indicating that hST6GalNAc-I possibly also sialylated the terminal galactose of core 2 glycans. Relative specificities for the acceptors, Galbeta1-3GalNAcalphaOpNP (23%), Galbeta1-3[GlcNAcbeta1-6]GalNAcOalphapNP (12%), Galbeta1-3GalNAcOalphaThr (100%) and Galbeta1-3[GlcNAcbeta1-6]Galalpha2-6GalNAcOalphaThr (alpha2-6sialyl Tn-antigen). Relative specificities of the acceptors, Galbeta1-3GalNAcalphaOpNP (0%), Galbeta1-3[GlcNAcbeta1-6]GalNAcOalphapNP (0%), Galbeta1-3GalNAcOalphaThr (100%) and Galbeta1-3[GlcNAcbeta1-6]GalNAcalphaThr (19%) are found
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme catalyzes the formation of the terminal alpha2,6-sialic acid linkages on gangliosides
Products: -
Products: -
?
additional information
?
-
Substrates: the enzyme catalyzes alpha-2,6-sialylation of galactose on glycoproteins
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme catalyzes alpha-2,6-sialylation of galactose on glycoproteins
Products: -
Products: -
?
additional information
?
-
Substrates: the enzyme cannot transfer a N-acetylneuraminate residue to pyridylaminyl-LNFP I, a type 1 chain derivative of the blood group H antigen
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme cannot transfer a N-acetylneuraminate residue to pyridylaminyl-LNFP I, a type 1 chain derivative of the blood group H antigen
Products: -
Products: -
?
additional information
?
-
-
Substrates: no activity with 6'-sialyllactosamine
Products: -
Products: -
?
additional information
?
-
Substrates: no activity with cytidine-5'-yl-5-(3-[4-Chloro-1,2,3-oxadiazol-3-ium-5-olate]benzamido)-3,5-dideoxy-beta-D-glycero-D-galacto-non-2-ulopyranosid-2''-yl phosphate (CMP-Neu5SydCl)
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme is responsible for the synthesis of 6'-sialylolifosaccharides in milk
Products: -
Products: -
?
additional information
?
-
-
Substrates: ST6Gal II shows no activity towards oligosaccharides such as Galbeta1,3GalNAc, Galbeta1,3GlcNAc, lactose, and lacto-N-tetraose, which do not have the Galbeta1,4GlcNAc structure at the nonreducing end of their carbohydrate groups. Relatively low activity towards some glycoproteins, which are considered to have the Galbeta1,4GlcNAc structure at the nonreducing end of the carbohydrate groups
Products: -
Products: -
?
additional information
?
-
-
Substrates: ST6Gal I sialyltransferase knock-out mouse lacks the main enzyme necessary for the attachment of alpha2,6 sialic acid to N-linked glycoproteins on the cell surface. Even in the absence of detectable alpha2,6 sialic acid in the mouse respiratory tract, human influenza viruses can still infect these mice and grow to similar titers in the lung and trachea as compared to wild-type animals. The presence of a major alpha2,6 sialic acid on N-linked glycoproteins is not essential for human influenza virus infection in mice
Products: -
Products: -
?
additional information
?
-
-
Substrates: low activity with several methylated substrates, no activity with UDP-Gal, UDP-GalNAc and UDP-Glc as donor substrates
Products: -
Products: -
?
additional information
?
-
-
Substrates: enzyme does not recognize type I oligosaccharides
Products: -
Products: -
?
additional information
?
-
-
Substrates: DELTA15Pd2,6ST preferentially cleaves alpha2,6-linked sialic acid
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme exhibits a unique regioselectivity and is able to sialylate internal galactose residues in poly-LacNAc extended glycans
Products: -
Products: -
?
additional information
?
-
-
Substrates: low activity with several methylated substrates, no activity with UDP-Gal, UDP-GalNAc and UDP-Glc as donor substrates
Products: -
Products: -
?
additional information
?
-
-
Substrates: neuraminidase activity is specific for the Neu5Acalpha2,6Gal linkage
Products: -
Products: -
?
additional information
?
-
-
Substrates: neuraminidase activity is specific for the Neu5Acalpha2,6Gal linkage
Products: -
Products: -
?
additional information
?
-
Substrates: no sialidase activity is detected for the alpha2,6-sialyltransferase
Products: -
Products: -
?
additional information
?
-
-
Substrates: thyroglobin is no substrate
Products: -
Products: -
?
additional information
?
-
-
Substrates: no activity with submaxillary asialo-mucin
Products: -
Products: -
?
additional information
?
-
-
Substrates: no activity with submaxillary asialo-mucin
Products: -
Products: -
?
additional information
?
-
-
Substrates: no activity with submaxillary asialo-mucin
Products: -
Products: -
?
additional information
?
-
-
Substrates: very low activity with prothrombin and native alpha1-acid glycoprotein, no activity with transferrin, asialo-agalacto-alpha1-acid glycoprotein
Products: -
Products: -
?
additional information
?
-
-
Substrates: no activity with antifreeze glycoprotein
Products: -
Products: -
?
additional information
?
-
-
Substrates: no activity with antifreeze glycoprotein
Products: -
Products: -
?
additional information
?
-
-
Substrates: no activity with the CMP-NeuAc analogues disodium[(5-acetamido-3,5-dideoxy-D-glycero-beta-D-galacto-2-nonulopyranosyl)onate] (methyl-beta-D-ribofuranosid-5-yl) phosphate and bis(triethylammonium) [(5-acetamido-3,5-dideoxy-D-glycero-beta-D-galacto-2-nonulopyranosyl)onate] [(resorcin-4-yl) (1-deoxy-beta-D-ribofuranosid-5-yl)] phosphate
Products: -
Products: -
?
additional information
?
-
-
Substrates: addition of alpha2,6-linked sialic acid to the Gal1,4GlcNAc sequence, the preferred ligand for galectin-1, inhibits recognition of this saccharide ligand by galectin-1. The enzyme sialylates N-glycans on CD45, a receptor tyrosine phosphatase that is a T cell receptor for galectin-1. ST6Gal I expression abrogates the reduction in CD45 tyrosine phosphatase activity that results from galectin1 binding. Sialylation of CD45 by the ST6Gal I also prevents galectin-1-induced clustering of CD45 on the T cell surface, an initial step in galectin-1 cell death. Regulation of glycoprotein sialylation may control susceptibility to cell death at specific points during T cell development and peripheral activation
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme functions in Golgi vesicles to terminally sialylate the N-linked oligosaccharides of glycoproteins
Products: -
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?
additional information
?
-
-
Substrates: human-like sialylated recombinant thyrotropin with sialic acid bound to galactose by both alpha2-3 and alpha2-6 linkages, similar to the native preparation, obtained in CHO cells modified to produce alpha2,6-sialyltransferase
Products: -
Products: -
?
additional information
?
-
-
Substrates: thyroglobin is no substrate
Products: -
Products: -
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
CMP-N-acetyl-beta-neuraminate + alpha-1-antitrypsin
CMP + ?
-
Substrates: -
Products: -
Products: -
?
CMP-N-acetyl-beta-neuraminate + beta-D-galactosyl-R
CMP + N-acetyl-alpha-neuraminyl-(2->6)-beta-D-galactosyl-R
CMP-N-acetylneuraminate + beta-D-galactosyl-(1->4)-N-acetyl-beta-D-glucosamine
CMP + alpha-N-acetylneuraminyl-(2->6)-beta-D-galactosyl-(1->4)-N-acetyl-beta-D-glucosamine
CMP-N-acetylneuraminate + beta-D-galactosyl-1,4-N-acetyl-beta-D-glucosamine
CMP + alpha-N-acetylneuraminyl-2,6-beta-D-galactosyl-1,4-N-acetyl-beta-D-glucosamine
-
Substrates: -
Products: -
Products: -
?
CMP-N-acetylneuraminate + beta-D-galactosyl-1,4-N-acetyl-beta-D-glucosaminyl-R
CMP + alpha-N-acetylneuraminyl-2,6-beta-D-galactosyl-1,4-N-acetyl-beta-D-glucosaminyl-R
CMP-N-acetylneuraminate + glycano-(1->3)-(N-acetyl-alpha-D-galactosaminyl)-glycoprotein
CMP + glycano-[(2->6)-alpha-N-acetylneuraminyl]-(N-acetyl-D-galactosaminyl)-glycoprotein
Substrates: -
Products: -
Products: -
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CMP-N-acetylneuraminate + tumor necrosis factor receptor 1
CMP + alpha2,6-sialyated tumor necrosis factor receptor 1
CMP-NeuNAc + Galbeta(1->4)GIcNAc-R
CMP + NeuNAcalpha(2->6)Galbeta(l->4)GlcNAc-R
-
Substrates: -
Products: -
Products: -
?
CMP-N-acetyl-beta-neuraminate + beta-D-galactosyl-R
CMP + N-acetyl-alpha-neuraminyl-(2->6)-beta-D-galactosyl-R
-
Substrates: -
Products: -
Products: -
?
CMP-N-acetyl-beta-neuraminate + beta-D-galactosyl-R
CMP + N-acetyl-alpha-neuraminyl-(2->6)-beta-D-galactosyl-R
Substrates: -
Products: -
Products: -
?
CMP-N-acetyl-beta-neuraminate + beta-D-galactosyl-R
CMP + N-acetyl-alpha-neuraminyl-(2->6)-beta-D-galactosyl-R
-
Substrates: -
Products: -
Products: -
?
CMP-N-acetyl-beta-neuraminate + beta-D-galactosyl-R
CMP + N-acetyl-alpha-neuraminyl-(2->6)-beta-D-galactosyl-R
Substrates: -
Products: -
Products: -
?
CMP-N-acetylneuraminate + beta-D-galactosyl-(1->4)-N-acetyl-beta-D-glucosamine
CMP + alpha-N-acetylneuraminyl-(2->6)-beta-D-galactosyl-(1->4)-N-acetyl-beta-D-glucosamine
-
Substrates: -
Products: -
Products: -
?
CMP-N-acetylneuraminate + beta-D-galactosyl-(1->4)-N-acetyl-beta-D-glucosamine
CMP + alpha-N-acetylneuraminyl-(2->6)-beta-D-galactosyl-(1->4)-N-acetyl-beta-D-glucosamine
Substrates: -
Products: -
Products: -
?
CMP-N-acetylneuraminate + beta-D-galactosyl-(1->4)-N-acetyl-beta-D-glucosamine
CMP + alpha-N-acetylneuraminyl-(2->6)-beta-D-galactosyl-(1->4)-N-acetyl-beta-D-glucosamine
-
Substrates: -
Products: -
Products: -
?
CMP-N-acetylneuraminate + beta-D-galactosyl-(1->4)-N-acetyl-beta-D-glucosamine
CMP + alpha-N-acetylneuraminyl-(2->6)-beta-D-galactosyl-(1->4)-N-acetyl-beta-D-glucosamine
Substrates: -
Products: -
Products: -
?
CMP-N-acetylneuraminate + beta-D-galactosyl-(1->4)-N-acetyl-beta-D-glucosamine
CMP + alpha-N-acetylneuraminyl-(2->6)-beta-D-galactosyl-(1->4)-N-acetyl-beta-D-glucosamine
-
Substrates: -
Products: -
Products: -
?
CMP-N-acetylneuraminate + beta-D-galactosyl-(1->4)-N-acetyl-beta-D-glucosamine
CMP + alpha-N-acetylneuraminyl-(2->6)-beta-D-galactosyl-(1->4)-N-acetyl-beta-D-glucosamine
Substrates: -
Products: -
Products: -
?
CMP-N-acetylneuraminate + beta-D-galactosyl-(1->4)-N-acetyl-beta-D-glucosamine
CMP + alpha-N-acetylneuraminyl-(2->6)-beta-D-galactosyl-(1->4)-N-acetyl-beta-D-glucosamine
Substrates: -
Products: -
Products: -
?
CMP-N-acetylneuraminate + beta-D-galactosyl-(1->4)-N-acetyl-beta-D-glucosamine
CMP + alpha-N-acetylneuraminyl-(2->6)-beta-D-galactosyl-(1->4)-N-acetyl-beta-D-glucosamine
Substrates: -
Products: -
Products: -
?
CMP-N-acetylneuraminate + beta-D-galactosyl-(1->4)-N-acetyl-beta-D-glucosamine
CMP + alpha-N-acetylneuraminyl-(2->6)-beta-D-galactosyl-(1->4)-N-acetyl-beta-D-glucosamine
Substrates: -
Products: -
Products: -
?
CMP-N-acetylneuraminate + beta-D-galactosyl-(1->4)-N-acetyl-beta-D-glucosamine
CMP + alpha-N-acetylneuraminyl-(2->6)-beta-D-galactosyl-(1->4)-N-acetyl-beta-D-glucosamine
Substrates: -
Products: -
Products: -
?
CMP-N-acetylneuraminate + beta-D-galactosyl-1,4-N-acetyl-beta-D-glucosaminyl-R
CMP + alpha-N-acetylneuraminyl-2,6-beta-D-galactosyl-1,4-N-acetyl-beta-D-glucosaminyl-R
-
Substrates: one of a group of glycosyltransferases which act to assemble the carbohydrate units of thyroglobulin
Products: -
Products: -
?
CMP-N-acetylneuraminate + beta-D-galactosyl-1,4-N-acetyl-beta-D-glucosaminyl-R
CMP + alpha-N-acetylneuraminyl-2,6-beta-D-galactosyl-1,4-N-acetyl-beta-D-glucosaminyl-R
-
Substrates: R: glycoprotein or glycopeptide
Products: -
Products: -
?
CMP-N-acetylneuraminate + beta-D-galactosyl-1,4-N-acetyl-beta-D-glucosaminyl-R
CMP + alpha-N-acetylneuraminyl-2,6-beta-D-galactosyl-1,4-N-acetyl-beta-D-glucosaminyl-R
-
Substrates: final step in synthesis of serum-type glycoproteins
Products: -
Products: -
?
CMP-N-acetylneuraminate + beta-D-galactosyl-1,4-N-acetyl-beta-D-glucosaminyl-R
CMP + alpha-N-acetylneuraminyl-2,6-beta-D-galactosyl-1,4-N-acetyl-beta-D-glucosaminyl-R
-
Substrates: final step in synthesis of serum-type glycoproteins
Products: -
Products: -
?
CMP-N-acetylneuraminate + beta-D-galactosyl-1,4-N-acetyl-beta-D-glucosaminyl-R
CMP + alpha-N-acetylneuraminyl-2,6-beta-D-galactosyl-1,4-N-acetyl-beta-D-glucosaminyl-R
-
Substrates: final step in synthesis of serum-type glycoproteins
Products: -
Products: -
?
CMP-N-acetylneuraminate + beta-D-galactosyl-1,4-N-acetyl-beta-D-glucosaminyl-R
CMP + alpha-N-acetylneuraminyl-2,6-beta-D-galactosyl-1,4-N-acetyl-beta-D-glucosaminyl-R
-
Substrates: R: glycoprotein or glycopeptide
Products: -
Products: -
?
CMP-N-acetylneuraminate + beta-D-galactosyl-1,4-N-acetyl-beta-D-glucosaminyl-R
CMP + alpha-N-acetylneuraminyl-2,6-beta-D-galactosyl-1,4-N-acetyl-beta-D-glucosaminyl-R
-
Substrates: regulation of enzyme expression
Products: -
Products: -
?
CMP-N-acetylneuraminate + tumor necrosis factor receptor 1
CMP + alpha2,6-sialyated tumor necrosis factor receptor 1
Substrates: -
Products: -
Products: -
?
CMP-N-acetylneuraminate + tumor necrosis factor receptor 1
CMP + alpha2,6-sialyated tumor necrosis factor receptor 1
Substrates: -
Products: -
Products: -
?
additional information
?
-
-
Substrates: soluble ST6Gal I produced by BACE1 plays, at least in part, a role in the sialylation of soluble glycoproteins
Products: -
Products: -
?
additional information
?
-
Substrates: radiation exposure is found to increase the sialylation of glycoproteins such as integrin beta1 by inducing the expression of ST6Gal I, and increased protein sialylation contributed to cellular radiation resistance
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme is responsible for the synthesis of 6'-sialylolifosaccharides in milk
Products: -
Products: -
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additional information
?
-
-
Substrates: ST6Gal I sialyltransferase knock-out mouse lacks the main enzyme necessary for the attachment of alpha2,6 sialic acid to N-linked glycoproteins on the cell surface. Even in the absence of detectable alpha2,6 sialic acid in the mouse respiratory tract, human influenza viruses can still infect these mice and grow to similar titers in the lung and trachea as compared to wild-type animals. The presence of a major alpha2,6 sialic acid on N-linked glycoproteins is not essential for human influenza virus infection in mice
Products: -
Products: -
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additional information
?
-
-
Substrates: addition of alpha2,6-linked sialic acid to the Gal1,4GlcNAc sequence, the preferred ligand for galectin-1, inhibits recognition of this saccharide ligand by galectin-1. The enzyme sialylates N-glycans on CD45, a receptor tyrosine phosphatase that is a T cell receptor for galectin-1. ST6Gal I expression abrogates the reduction in CD45 tyrosine phosphatase activity that results from galectin1 binding. Sialylation of CD45 by the ST6Gal I also prevents galectin-1-induced clustering of CD45 on the T cell surface, an initial step in galectin-1 cell death. Regulation of glycoprotein sialylation may control susceptibility to cell death at specific points during T cell development and peripheral activation
Products: -
Products: -
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additional information
?
-
-
Substrates: the enzyme functions in Golgi vesicles to terminally sialylate the N-linked oligosaccharides of glycoproteins
Products: -
Products: -
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
MgCl2
NaCl
-
alpha2,6-sialyltransferase activity is increased approximately 40% in the presence of 300-800 mM
additional information
additional information
-
a metal ion is not required for the activity
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
5'-deoxy-5'-([[(3-phenoxyphenyl)(phosphono)methoxy]carbonyl]amino)cytidine
-
5'-deoxy-5'-[4-[(3-phenoxyphenyl)(phosphono)methyl]-1H-1,2,3-triazol-1-yl]cytidine
-
5'-O-[hydroxy[(2R)-2-(3-phenoxyphenyl)-2-phosphonoethyl]phosphoryl]cytidine
-
Aflatoxins
-
aflatoxins B1, B2a, G1, slightly by aflatoxins B2 and G2, inhibition is probably due to membrane disruption through binding of the aflatoxins and change in enzyme conformation
cycloheximide
-
reduces the enzyme expression 3fold in normal hepatocytes and 16 to 17fold in Zaidela ascitic hepatoma, but not in cells isolated from the tumor and cultured for 48 h
endo F
-
inactivation due to deglycosylation of the enzyme, best in methanol or ethanol, less efficient than glycanase
-
glycanase
-
inactivation due to deglycosylation of the enzyme, best in methanol or ethanol
-
long chain fatty acids
-
oleic acid, stearic acid, less efficient: palmitic acid, lauric acid, capric acid, caprylic acid or caproic acid, no inhibition by linoleic acid or linolenic acid
CDP
-
at a concentration of 1 mM inhibits both sialidase and trans-sialidase activities of DELTA15Pd2,6ST
CTP
-
at a concentration of 1 mM inhibits both sialidase and trans-sialidase activities of DELTA15Pd2,6ST
CTP
-
also decreases the stimulation by the natural cytosolic rat colon factor
additional information
-
no inhibition by linoleic acid or linolenic acid
-
additional information
-
inhibitory capacity of several synthetic trisaccharides
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
CMP
-
cytidine 5'-monophosphate, the product of sialyltransferase reactions, is not required by the trans-sialidase activity of the enzyme but enhances the trans-sialidase activity modestly as a non-essential activator. CMP can enhance the efficiency of the alpha2,6-sialidase activity of DELTA15Pd2,6ST in a dose-dependent manner
natural factor from rat colon
-
stimulation is decreased by CTP, no activation at 0.75 mM CTP
-
natural factor from rat colon
-
specific, 4fold stimulation by decreasing the Km value for the substrates and increasing Vmax, present in the cytosol, temperature dependent, protease sensitive, independent of metal ions or detergent, unaffceted by monosaccharides
-
natural factor from rat colon
-
may also be present in rat brain and kidney
-
additional information
-
the enzyme is induced by phorbol 12-myristate 13-acetate via a PKC/ERK/CREB-dependent pathway in K562 human leukemia cells, the induction is inhibited by Gö6976, a specific inhibitor of PKC, and U0126, an inhibitor of the extracellular signal-regulated kinase, but not by wortmannin, overview
-
additional information
in the sialyltransferase activity assay, FLAG-tagged ST6Gal1 has the highest expression level, which is 1.8- or 4.1fold higher than that of Strep- or His-tagged ST6Gal1, respectively
-
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1.1
(2S,3S,4R,5R,6R)-5-Acetylamino-4-hydroxy-6-methoxy-3-((2S,3R,4S,5R,6R)-3,4,5-trihydroxy-6-hydroxymethyl-tetrahydro-pyran-2-yloxy)-tetrahydro-pyran-2-carboxylic acid methyl ester
-
-
2.4
(2S,3S,4R,5R,6R)-5-Acetylamino-4-hydroxy-6-methoxy-3-((2S,3R,4S,5R,6R)-3,4,5-trihydroxy-6-hydroxymethyl-tetrahydro-pyran-2-yloxy)-tetrahydro-pyran-2-carboxylic acid methylamide
-
-
2.8
5-(5-dimethylaminonaphthalene-1-sulfonyl-2-(2-aminoethoxy))ethyl beta-lactose
-
0.92
5-(5-dimethylaminonaphthalene-1-sulfonyl-2-(2-aminoethoxy))ethyl beta-N-acetyllactosamine
-
0.078
asialo-ceruloplasmin
-
expressed as concentration of acceptor sites
-
0.3
CMP-Neu5Ac
-
alpha2,6-sialyltransferase activity of the truncated recombinant enzyme
0.086
cytidine-5'-yl-5-(acetamido)-9-(3-[4-chloro-1,2,3-oxadiazol-3-ium-5-olate]benzamido)-3,5,9-trideoxy-beta-D-glycero-D-galacto-non-2-ulopyranosid-2''-yl phosphate
pH and temperature not specified in the publication
0.385
cytidine-5'-yl-5-(acetamido)-9-azido-3,5,9-trideoxy-beta-D-glycero-D-galacto-non-2-ulopyranosid-2''-yl phosphate
pH and temperature not specified in the publication
3.3
Formic acid (2R,3R,4S,5R,6R)-2-((2R,3R,4R,5R,6R)-3-acetylamino-5-hydroxy-2-methoxy-6-methylaminomethyl-tetrahydro-pyran-4-yloxy)-4,5-dihydroxy-6-hydroxymethyl-tetrahydro-pyran-3-yl ester
-
pH 6.5, 37°C
1.4
Galbeta(1-4)GlcNAc
-
non-reducing terminus of asialofetuin glycans
0.7
Methanesulfonic acid (2R,3S,4R,5R,6R)-5-acetylamino-4-hydroxy-6-methoxy-3-((2S,3R,4S,5R,6R)-3,4,5-trihydroxy-6-hydroxymethyl-tetrahydro-pyran-2-yloxy)-tetrahydro-pyran-2-ylmethyl ester
-
-
11.6
N-((1R,3R,5R,6R,7S,8R,13R,15R,16R,17S)-6,7,17-Trihydroxy-5-hydroxymethyl-15-methoxy-2,4,9,11,14-pentaoxa-tricyclo[11.3.1.03,8]heptadec-16-yl)-acetamide
-
pH 6.5, 37°C
1
N-((1R,3R,5R,6R,7S,8R,14R,16R,17R,18R)-6,7,18-trihydroxy-5-hydroxymethyl-16-methoxy-11-oxo-2,4,9,15-tetraoxa-12-aza-tricyclo[12.3.1.03,8]octadec-17-yl)-acetamide
-
pH 6.5, 37°C
1.1
N-((1R,3R,5R,6R,7S,8R,14R,16R,17R,18S)-6,7,18-Trihydroxy-5-hydroxymethyl-16-methoxy-2,4,9,12,15-pentaoxa-tricyclo[12.3.1.03,8]octadec-17-yl)-acetamide
-
pH 6.5, 37°C
0.8
N-[(2R,3R,4R,5S,6R)-4-Hydroxy-6-(methanesulfonylamino-methyl)-2-methoxy-5-((2S,3R,4S,5R,6R)-3,4,5-trihydroxy-6-hydroxymethyl-tetrahydro-pyran-2-yloxy)-tetrahydro-pyran-3-yl]-acetamide
-
-
3.1
N-[(2R,3R,4R,5S,6R)-5-((2S,3R,4S,5R,6R)-4,5-Dihydroxy-6-hydroxymethyl-3-methoxy-tetrahydro-pyran-2-yloxy)-6-formylaminomethyl-4-hydroxy-2-methoxy-tetrahydro-pyran-3-yl]-acetamide
-
-
1.4
N-[(2R,3R,4R,5S,6R)-6-(Acetylamino-methyl)-4-hydroxy-2-methoxy-5-((2S,3R,4S,5R,6R)-3,4,5-trihydroxy-6-hydroxymethyl-tetrahydro-pyran-2-yloxy)-tetrahydro-pyran-3-yl]-acetamide
-
-
5.8
N-[(2R,3R,4R,5S,6R)-6-Aminomethyl-4-hydroxy-2-methoxy-5-((2S,3R,4S,5R,6R)-3,4,5-trihydroxy-6-hydroxymethyl-tetrahydro-pyran-2-yloxy)-tetrahydro-pyran-3-yl]-acetamide
-
-
53
Neu5Acalpha-4-nitrophenyl
-
alpha2,6-trans-sialidase activity of DELTA15Pd2,6ST
3.5
pyridylamine-type 2H
recombinant enzyme, in 50 mM MES-NaOH buffer (pH 6.0), 1 mM MnCl2, at 37°C
0.9
pyridylaminyl-lacto-N-neotetraose
recombinant enzyme, in 50 mM MES-NaOH buffer (pH 6.0), 1 mM MnCl2, at 37°C
0.6
4-methylumbelliferyl beta-D-lactoside
-
pH 8.5, 37°C, enzyme form DELTA112Pd2,6ST(N)
0.8
4-methylumbelliferyl beta-D-lactoside
-
pH 8.5, 37°C, enzyme form DELTA15Pd2,6ST(N)
0.23
asialo-alpha1-acid glycoprotein
-
with stimulation by the natural cytosolic crat colon factor
-
0.53
asialo-alpha1-acid glycoprotein
-
without stimulation by the natural cytosolic crat colon factor
-
0.0064
asialo-fetuin
-
expressed as concentration of terminal galactosyl residues
-
1
beta-D-galactosyl-(1->4)-N-acetyl-beta-D-glucosamine
mutant enzyme F208A, at pH 6.5 and 37°C
1.1
beta-D-galactosyl-(1->4)-N-acetyl-beta-D-glucosamine
mutant enzyme K355A, at pH 6.5 and 37°C
1.4
beta-D-galactosyl-(1->4)-N-acetyl-beta-D-glucosamine
recombinant wild type enzyme from HEK-293 cells, at pH 6.5 and 37°C
1.8
beta-D-galactosyl-(1->4)-N-acetyl-beta-D-glucosamine
recombinant wild type enzyme from 293-F cells, at pH 6.5 and 37°C
1.8
beta-D-galactosyl-(1->4)-N-acetyl-beta-D-glucosamine
mutant enzyme Y119F, at pH 6.5 and 37°C
1.8
beta-D-galactosyl-(1->4)-N-acetyl-beta-D-glucosamine
mutant enzyme Q354A, at pH 6.5 and 37°C
2.6
beta-D-galactosyl-(1->4)-N-acetyl-beta-D-glucosamine
mutant enzyme Q232A, at pH 6.5 and 37°C
3.5
beta-D-galactosyl-(1->4)-N-acetyl-beta-D-glucosamine
mutant enzyme Y272A, at pH 6.5 and 37°C
6.5
beta-D-galactosyl-(1->4)-N-acetyl-beta-D-glucosamine
mutant enzyme D271A, at pH 6.5 and 37°C
0.119
CMP-N-acetyl-beta-neuraminate
pH and temperature not specified in the publication
0.078
CMP-N-acetylneuraminate
mutant enzyme Y119F, at pH 6.5 and 37°C
0.092
CMP-N-acetylneuraminate
recombinant wild type enzyme from 293-F cells, at pH 6.5 and 37°C
0.093
CMP-N-acetylneuraminate
recombinant wild type enzyme from HEK-293 cells, at pH 6.5 and 37°C
0.095
CMP-N-acetylneuraminate
mutant enzyme K355A, at pH 6.5 and 37°C
0.1
CMP-N-acetylneuraminate
apparent value, recombinant enzyme, using pyridylamine-type 2H as cosubstrate, in 50 mM MES-NaOH buffer (pH 6.0), 1 mM MnCl2, at 37°C
0.11
CMP-N-acetylneuraminate
apparent value, recombinant enzyme, using pyridylaminyl-lacto-N-neotetraose as cosubstrate, in 50 mM MES-NaOH buffer (pH 6.0), 1 mM MnCl2, at 37°C
0.133
CMP-N-acetylneuraminate
mutant enzyme Q232A, at pH 6.5 and 37°C
0.14
CMP-N-acetylneuraminate
-
with stimulation by the natural cytosolic crat colon factor
0.22
CMP-N-acetylneuraminate
mutant enzyme Y272A, at pH 6.5 and 37°C
0.24
CMP-N-acetylneuraminate
-
without stimulation by the natural cytosolic crat colon factor
0.365
CMP-N-acetylneuraminate
mutant enzyme D271A, at pH 6.5 and 37°C
0.9
CMP-N-acetylneuraminate
-
pH 8.5, 37°C, enzyme form DELTA15Pd2,6ST(N)
0.9
CMP-N-acetylneuraminate
-
pH 8.5, 37°C, enzyme form DELTA112Pd2,6ST(N)
2.27
CMP-N-acetylneuraminate
-
mutant enzyme L433T, at pH 8.0 and 22°C
3.37
CMP-N-acetylneuraminate
-
mutant enzyme I411T/L433T, at pH 8.0 and 22°C
6.06
CMP-N-acetylneuraminate
-
mutant enzyme I411T, at pH 8.0 and 22°C
8.15
CMP-N-acetylneuraminate
-
mutant enzyme L433S, at pH 8.0 and 22°C
10.7
CMP-N-acetylneuraminate
-
mutant enzyme I411T/L433S, at pH 8.0 and 22°C
35.7
Galbeta(1,4)-GlcNAcbeta-4-nitrophenyl
-
mutant enzyme N284Q, at pH 6.0 and 37°C
40.2
Galbeta(1,4)-GlcNAcbeta-4-nitrophenyl
-
wild type enzyme, at pH 6.0 and 37°C
52.8
Galbeta(1,4)-GlcNAcbeta-4-nitrophenyl
-
mutant enzyme N284A, at pH 6.0 and 37°C
3.6
lactose
-
pH 5.0, 37°C, cosubstrate: cytidine-5'-monophospho-sialic acid
17.2
lactose
-
alpha2,6-sialyltransferase activity of the truncated recombinant enzyme
2
N-acetyllactosamine
-
pH 5.0, 37°C, cosubstrate: CMP-9''-phenylacetamido-Neu5Ac
4.3
N-acetyllactosamine
-
pH 5.0, 37°C, cosubstrate: cytidine-5'-monophospho-sialic acid
5.2
N-acetyllactosamine
-
pH 5.0, 37°C, cosubstrate: CMP-9''-phenylhexanamido-Neu5Ac
6.8
N-acetyllactosamine
-
pH 5.0, 37°C, cosubstrate: CMP-9''-benzamido-Neu5Ac
10
N-acetyllactosamine
-
pH 5.0, 37°C, cosubstrate: CMP-9''-phenylpropionamido-Neu5Ac
15.4
N-acetyllactosamine
-
alpha2,6-sialyltransferase activity of the truncated recombinant enzyme
additional information
additional information
-
several recombinant truncated mutants
-
additional information
additional information
-
kinetics, several synthetic trisaccharides used as substrates
-
additional information
additional information
-
kinetics, several synthetic trisaccharides used as substrates
-
additional information
additional information
-
Km-values for synthetic CMP-N-acetylneuraminate analogues
-
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.087
5-(5-dimethylaminonaphthalene-1-sulfonyl-2-(2-aminoethoxy))ethyl beta-lactose
-
1.13
5-(5-dimethylaminonaphthalene-1-sulfonyl-2-(2-aminoethoxy))ethyl beta-N-acetyllactosamine
-
0.183
CMP-N-acetyl-beta-neuraminate
pH and temperature not specified in the publication
0.0167
cytidine-5'-yl-5-(acetamido)-9-(3-[4-chloro-1,2,3-oxadiazol-3-ium-5-olate]benzamido)-3,5,9-trideoxy-beta-D-glycero-D-galacto-non-2-ulopyranosid-2''-yl phosphate
pH and temperature not specified in the publication
0.3
cytidine-5'-yl-5-(acetamido)-9-azido-3,5,9-trideoxy-beta-D-glycero-D-galacto-non-2-ulopyranosid-2''-yl phosphate
pH and temperature not specified in the publication
0.883
Neu5Acalpha-4-nitrophenyl
-
alpha2,6-trans-sialidase activity of DELTA15Pd2,6ST
1.1
4-methylumbelliferyl beta-D-lactoside
-
pH 8.5, 37°C, enzyme form DELTA112Pd2,6ST(N)
2.3
4-methylumbelliferyl beta-D-lactoside
-
pH 8.5, 37°C, enzyme form DELTA15Pd2,6ST(N)
0.07
beta-D-galactosyl-(1->4)-N-acetyl-beta-D-glucosamine
mutant enzyme Y272A, at pH 6.5 and 37°C
0.09
beta-D-galactosyl-(1->4)-N-acetyl-beta-D-glucosamine
mutant enzyme D271A, at pH 6.5 and 37°C
0.14
beta-D-galactosyl-(1->4)-N-acetyl-beta-D-glucosamine
mutant enzyme Q232A, at pH 6.5 and 37°C
0.31
beta-D-galactosyl-(1->4)-N-acetyl-beta-D-glucosamine
mutant enzyme Y119F, at pH 6.5 and 37°C
0.35
beta-D-galactosyl-(1->4)-N-acetyl-beta-D-glucosamine
recombinant wild type enzyme from HEK-293 cells, at pH 6.5 and 37°C
0.39
beta-D-galactosyl-(1->4)-N-acetyl-beta-D-glucosamine
mutant enzyme K355A, at pH 6.5 and 37°C
0.43
beta-D-galactosyl-(1->4)-N-acetyl-beta-D-glucosamine
mutant enzyme F208A, at pH 6.5 and 37°C
0.64
beta-D-galactosyl-(1->4)-N-acetyl-beta-D-glucosamine
mutant enzyme Q354A, at pH 6.5 and 37°C
0.67
beta-D-galactosyl-(1->4)-N-acetyl-beta-D-glucosamine
recombinant wild type enzyme from 293-F cells, at pH 6.5 and 37°C
0.05
CMP-N-acetylneuraminate
mutant enzyme D271A, at pH 6.5 and 37°C
0.05
CMP-N-acetylneuraminate
mutant enzyme Y272A, at pH 6.5 and 37°C
0.19
CMP-N-acetylneuraminate
mutant enzyme F208A, at pH 6.5 and 37°C
0.39
CMP-N-acetylneuraminate
mutant enzyme Y119F, at pH 6.5 and 37°C
0.42
CMP-N-acetylneuraminate
mutant enzyme Q354A, at pH 6.5 and 37°C
0.49
CMP-N-acetylneuraminate
recombinant wild type enzyme from HEK-293 cells, at pH 6.5 and 37°C
0.59
CMP-N-acetylneuraminate
recombinant wild type enzyme from 293-F cells, at pH 6.5 and 37°C
0.69
CMP-N-acetylneuraminate
mutant enzyme K355A, at pH 6.5 and 37°C
1.4
CMP-N-acetylneuraminate
-
pH 8.5, 37°C, enzyme form DELTA112Pd2,6ST(N)
2.7
CMP-N-acetylneuraminate
-
pH 8.5, 37°C, enzyme form DELTA15Pd2,6ST(N)
10.7
CMP-N-acetylneuraminate
-
mutant enzyme L433T, at pH 8.0 and 22°C
10.9
CMP-N-acetylneuraminate
-
mutant enzyme I411T, at pH 8.0 and 22°C
16.9
CMP-N-acetylneuraminate
-
mutant enzyme I411T/L433S, at pH 8.0 and 22°C
18.8
CMP-N-acetylneuraminate
-
mutant enzyme I411T/L433T, at pH 8.0 and 22°C
20.3
CMP-N-acetylneuraminate
-
mutant enzyme L433S, at pH 8.0 and 22°C
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.031
5-(5-dimethylaminonaphthalene-1-sulfonyl-2-(2-aminoethoxy))ethyl beta-lactose
-
1.23
5-(5-dimethylaminonaphthalene-1-sulfonyl-2-(2-aminoethoxy))ethyl beta-N-acetyllactosamine
-
1.53
CMP-N-acetyl-beta-neuraminate
pH and temperature not specified in the publication
1.93
cytidine-5'-yl-5-(acetamido)-9-(3-[4-chloro-1,2,3-oxadiazol-3-ium-5-olate]benzamido)-3,5,9-trideoxy-beta-D-glycero-D-galacto-non-2-ulopyranosid-2''-yl phosphate
pH and temperature not specified in the publication
0.78
cytidine-5'-yl-5-(acetamido)-9-azido-3,5,9-trideoxy-beta-D-glycero-D-galacto-non-2-ulopyranosid-2''-yl phosphate
pH and temperature not specified in the publication
0.016
Neu5Acalpha-4-nitrophenyl
-
alpha2,6-trans-sialidase activity of DELTA15Pd2,6ST
0.01
beta-D-galactosyl-(1->4)-N-acetyl-beta-D-glucosamine
mutant enzyme D271A, at pH 6.5 and 37°C
0.02
beta-D-galactosyl-(1->4)-N-acetyl-beta-D-glucosamine
mutant enzyme Y272A, at pH 6.5 and 37°C
0.05
beta-D-galactosyl-(1->4)-N-acetyl-beta-D-glucosamine
mutant enzyme Q232A, at pH 6.5 and 37°C
0.17
beta-D-galactosyl-(1->4)-N-acetyl-beta-D-glucosamine
mutant enzyme Y119F, at pH 6.5 and 37°C
0.25
beta-D-galactosyl-(1->4)-N-acetyl-beta-D-glucosamine
recombinant wild type enzyme from HEK-293 cells, at pH 6.5 and 37°C
0.36
beta-D-galactosyl-(1->4)-N-acetyl-beta-D-glucosamine
mutant enzyme Q354A, at pH 6.5 and 37°C
0.36
beta-D-galactosyl-(1->4)-N-acetyl-beta-D-glucosamine
mutant enzyme K355A, at pH 6.5 and 37°C
0.37
beta-D-galactosyl-(1->4)-N-acetyl-beta-D-glucosamine
recombinant wild type enzyme from 293-F cells, at pH 6.5 and 37°C
0.44
beta-D-galactosyl-(1->4)-N-acetyl-beta-D-glucosamine
mutant enzyme F208A, at pH 6.5 and 37°C
0.13
CMP-N-acetylneuraminate
mutant enzyme D271A, at pH 6.5 and 37°C
0.23
CMP-N-acetylneuraminate
mutant enzyme Y272A, at pH 6.5 and 37°C
0.47
CMP-N-acetylneuraminate
mutant enzyme F208A, at pH 6.5 and 37°C
1.58
CMP-N-acetylneuraminate
-
mutant enzyme I411T/L433S, at pH 8.0 and 22°C
1.8
CMP-N-acetylneuraminate
-
mutant enzyme I411T, at pH 8.0 and 22°C
2.61
CMP-N-acetylneuraminate
-
mutant enzyme L433S, at pH 8.0 and 22°C
4.17
CMP-N-acetylneuraminate
mutant enzyme Q354A, at pH 6.5 and 37°C
4.7
CMP-N-acetylneuraminate
-
mutant enzyme L433T, at pH 8.0 and 22°C
5.27
CMP-N-acetylneuraminate
recombinant wild type enzyme from HEK-293 cells, at pH 6.5 and 37°C
5.6
CMP-N-acetylneuraminate
-
mutant enzyme I411T/L433T, at pH 8.0 and 22°C
6.45
CMP-N-acetylneuraminate
recombinant wild type enzyme from 293-F cells, at pH 6.5 and 37°C
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.79
CMP-4-O-[4-carboxy-2,2,6,6-tetramethylpiperidinine-1-oxyl]
pH 6.5, 37°C
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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5.5
82.9
-
alpha2,6-sialyltransferase activity of the 15.2fold purified truncated recombinant enzyme
additional information
5.5
-
crude extract, alpha2,6-sialyltransferase activity of the truncated recombinant enzyme
additional information
-
assay method development, biosensor-based method using immobilized Sambucus nigra agglutinin
additional information
-
assay method development, biosensor-based method using immobilized Sambucus nigra agglutinin
additional information
-
activity of stimulated and unstimulated enzyme with different substrates
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5 - 6
-
pH 5: alpha2,6-sialyltransferase activity of the truncated recombinant enzyme, pH 6: neuraminidase activity of the truncated recombinant enzyme
5.8
-
alpha2,6-sialidase and alpha2,6-trans-sialidase activities of DELTA15Pd2,6ST in MES buffer
6 - 6.5
6.4 - 7.2
-
broad, optimal buffer concentration: 0.05-0.15 M, decreasing activity above 0.15 M
6.5
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5 - 9.7
-
about 65% of maximal activity at pH 5 and about half-maximal activity at pH 9.7
7.5 - 10
-
pH-profile of truncated enzyme forms DELTA15Pd2,6ST(N) and DELTA112Pd2,6ST(N). Similar to the DELTA15Pd2,6ST(N), the shorter DELTA112Pd2,6ST(N) is active in a wide pH range of 7.5-10.0
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30
35
-
alpha2,6-sialyltransferase activity and neuraminidase activity of the truncated recombinant enzyme
37
37
-
assay at
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
ST6GAL2, fragment; i.e. Silurana tropicalis, western clawed frog
SwissProt
brenda
-
637257, 637259, 637273, 637276, 637285, 637291, 637292, 637295, 637296, 637297, 675938, 686984, 687646
-
-
brenda
ST6GAL1; i.e. Takifugu rubripes, Japanese pufferfish
SwissProt
brenda
ST6GAL2, fragment; i.e. Takifugu rubripes, Japanese pufferfish
SwissProt
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
level of serum ST6Gal I in patients with chronic active hepatitis is significantly increased compared to that in patients with chronic persistent hepatitis. Serum level of ST6Gal I in hepatitis C patients is correlated with the activity of hepatic inflammation, but not with liver fibrosis
brenda
-
expressed during embryonic development in a tissue- and stage-specific fashion, with elevated expression in a subset of cells within the central nervous system
brenda
-
high activity in cells grown in tissue culture or adherent to extracellular matrices, low activity in cells not adherent nor grown in tissue culture
brenda
-
BACE1 affects the alpha2,6-sialylation of proteins secreted from Hep-3B cells. Following BACE1 overexpression in Hep3B cells, the alpha2,6-sialylation of soluble secreted glycoproteins is significantly increased, whereas that of cell-surface glycoproteins remains unchanged
brenda
-
a leukemia cell line, the enzyme is expressed during the induction of megakaryocytic differentiation
brenda
additional information
-
cultured cells isolated from the tumor behave as normal hepatocytes
brenda
-
no enzyme activity in Zaidela ascitic hepatoma, but 3.6fold reduced mRNA content of a larger transcript size compared to normal liver cells
brenda
-
ST6GalI protein level is negligibly decreased in moderate drinkers but decreases by 30% in heavy alcohol drinkers compared to non-drinkers. The appearance of asialoconjugates in alcoholics is possibly due to the down-regulation of ST6GalI gene expression
brenda
-
-
636803, 637267, 637269, 637270, 637271, 637283, 637284, 637285, 637288, 637291, 637293, 637294, 637295, 637297, 658008, 658279, 685963
brenda
both mRNA expression and enzyme activity of ST6Gal I do not show a significant difference in the placental tissues of the women with preeclampsia and without preeclampsia. ST6Gal I is not involved in the pathogenesis of the preeclampsia
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
exogenous and endogenous ST6Gal I in the perinuclear Golgi of Hep3B-ST6Gal I and control Hep3B cells
-
brenda
additional information
has a short cytosolic region of 11 amino acids (M1-G11)
brenda
-
isoform Stcys is found in both the endoplasmic reticulum and in Golgi
brenda
-
membrane-bound at the luminal side, trans compartment
brenda
-
the STtyr isoform is transiently localized in the Golgi and is ultimately cleaved and secreted, whereas the STcys isoform is stably localized in the Golgi and is not cleaved and secreted. Cytosolic tail and transmembrane region of the ST6Gal I both play roles in Golgi localization
brenda
the enzyme is a Golgi type II transmembrane glycosyltransferase
brenda
the enzyme is a Golgi type II transmembrane glycosyltransferase
brenda
the enzyme is a Golgi type II transmembrane glycosyltransferase
brenda
the enzyme is a Golgi type II transmembrane glycosyltransferase
brenda
the enzyme is a Golgi type II transmembrane glycosyltransferase
brenda
the enzyme is a Golgi type II transmembrane glycosyltransferase
brenda
the enzyme is a Golgi type II transmembrane glycosyltransferase
brenda
the enzyme is a Golgi type II transmembrane glycosyltransferase
brenda
the enzyme is a Golgi type II transmembrane glycosyltransferase
brenda
the enzyme is a Golgi type II transmembrane glycosyltransferase
brenda
the enzyme is a Golgi type II transmembrane glycosyltransferase
brenda
the enzyme is a Golgi type II transmembrane glycosyltransferase
brenda
the enzyme is a Golgi type II transmembrane glycosyltransferase
brenda
the enzyme is a Golgi type II transmembrane glycosyltransferase
brenda
-
in medial-trans regions. Isoform STtyr is restricted to Golgi in most cells
-
brenda
-
in medial-trans regions. Isoform Stcys is found in both the endoplasmic reticulum and in Golgi
-
brenda
is a type II membrane-bound protein with a short cytosolic region of 11 amino acids (M1-G11), a single transmembrane region of 19 amino acids (M12-F30) and a luminal domain of 465 amino acids (T31-A495)
brenda
-
-
brenda
additional information
-
deletion of the transmembrane fragment results in loss of acceptor preference
-
brenda
additional information
oxidative stress changes the intracellular localizations of ST6Gal I and BACE1, more disperse localizations
-
brenda
additional information
-
oxidative stress changes the intracellular localizations of ST6Gal I and BACE1, more disperse localizations
-
brenda
additional information
-
enzyme is not catalytically active in the endoplasmic reticulum and only achieves full activity when it locates itself to the trans compartment of the Golgi system
-
brenda
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
metabolism
the enzyme is responsible for the biosynthesis of alpha2,6-linked sialic acid in N-linked glycans
physiological function
malfunction
enzyme down-regulation limits monocyte/macrophage lifespan by sensitizing cells to apoptosis via tumor necrosis factor receptor I hyposialylation
malfunction
enzyme down-regulation limits monocyte/macrophage lifespan by sensitizing cells to apoptosis via tumor necrosis factor receptor I hyposialylation
malfunction
B cells of mice lacking the hepatocyte specific enzyme promoter have reduced sialylation of cell surface CD22 and CD45 and produce less immunoglobulin G upon stimulation
malfunction
enzyme knockdown is sufficient to inhibit pancreatic cancer metastasis in pancreatic ductal adenocarcinoma
physiological function
recombinant ST6Gal1 can be used as a key enzyme for the synthesis of an artificial sialoglycopolymer for potentially blocking influenza virus infection
physiological function
-
DELTA15Pd2,6ST-catalyzed trans-sialidase reaction follows a ping-pong bi-bi reaction mechanism. DELTA15Pd2,6ST also has alpha2,6-sialidase activity
physiological function
-
shows both alpha2,6-sialyltransferase and alpha2,6-linkage-specific neuraminidase activity. Sialyltransferase activity of pLST-DELTAN is much higher than that of pLST-FL, and reaches 1477 U/l culture broth
physiological function
alpha2,6-sialylation mediated by ST6Gal II can contribute to organism's response to infections
physiological function
-
reduced sialylation of serum IgA1 may result from decreased expression of ST6GALNAC2
physiological function
-
enzyme overexpression in an U-373MG stable transfectant leads to elevated expression of GM2alpha and GM3 gangliosides and and decreased expression of GM1b, Gb3, and Gb4, marked inhibition of in vitro invasivity, modified cellular adhesion to fibronectin and laminin, increased adhesion-mediated protein tyrosine-phosphorylationof HSPA8, and inhibition of tumor growth in vivo
physiological function
the enzyme is responsible for alpha2,6-sialylated blood group type 2H antigen biosynthesis in human colon cancer cells
physiological function
circulatory enzyme, mostly of hepatic origin, limits myelopoiesis by a mechanism independent of hepatic sialylation of serum glycoproteins
physiological function
the enzyme regulates macrophage tumor necrosis factor alpha-induced apoptosis via alpha2-6 sialylation of the tumor necrosis factor receptor I death receptor. The enzyme inhibits phorbol-12-myristate-13-acetate-induced suppression of cell growth
physiological function
the enzyme regulates macrophage tumor necrosis factor alpha-induced apoptosis via alpha2-6 sialylation of the tumor necrosis factor receptor I death receptor. The enzyme inhibits phorbol-12-myristate-13-acetate-induced suppression of cell growth
physiological function
alpha2,6 sialylation mediated by the enzyme is required for the activation of Pax7, limits the fusion of C2C12 myoblasts, and allows the upkeep of satellite cells
physiological function
the enzyme is essential to the development of a robust and tolerant humoral immunity. Extracellular enzyme enhances B cell IgG production and increases blood IgG titers. Sialylation of B cells by extracellular enzyme boosts expression of immunoglobulin M, immunoglobulin D, and CD86, proliferation, and immunoglobulin G production in vitro. In vivo, elevation of blood enzyme enhances B cell development and systemic IgG in a CD22-dependent manner
physiological function
enzyme overexpression in differentiating 3T3-L1 cells inhibits adipogenesis with increased phosphorylation of focal adhesion kinase. The enzyme has an inhibitory role in adipogenesis through integrin-beta1 activation
physiological function
in the hallmarks of cancer, the enzyme plays a role in resisting cell death, inducing angiogenesis, evading growth suppressors, activating invasion and metastasis, avoiding immune destruction, enabling replicative immortality, sustained proliferative signalling, tumor promoting inflammations, deregulating cellular energetics, and genome instability and mutation
physiological function
-
the enzyme inhibits the colorectal cancer metastasis by stabilizing intercellular adhesion molecule-1 via sialylation
physiological function
the enzyme plays a fundamental role in growth, migration, and invasion of prostate cancer cells. Enzyme overexpression rescues the activation of the Hippo/YAP signaling pathway in prostate cancer cells
physiological function
the enzyme regulates the invasiveness of pancreatic ductal adenocarcinomas in a fructose-responsive manner
physiological function
-
the physiological function of the enzyme is almost certainly the synthesis of the NeuNAcalpha(2->6)Galbeta(l->4)GlcNAc-antennae of complex N-glycosyl oligosaccharides
physiological function
-
shows both alpha2,6-sialyltransferase and alpha2,6-linkage-specific neuraminidase activity. Sialyltransferase activity of pLST-DELTAN is much higher than that of pLST-FL, and reaches 1477 U/l culture broth
-
Show AA Sequence and Transmembrane Helices (2688 entries)
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
40000
41500
-
1 * 41500, low molecular weight form, SDS-PAGE under non-reducing conditions
42900
-
low molecular weight form, sedimentation equilibrium centrifugation, two enzyme forms differing in molecular weight when submitted to gel filtration, the smaller one is probably a degradation product of the larger one
45000
50000
53500
-
1 * 53500, high molecular weight form, SDS-PAGE under non-reducing conditions
55000
57000
x * 57000, the enzyme shows two bands at 55000 and 57000 Da, SDS-PAGE
57900
-
high molecular weight form, sedimentation equilibrium centrifugation, two enzyme forms differing in molecular weight when submitted to gel filtration, the smaller one is probably a degradation product of the larger one
80000
-
high molecular weight form, gel filtration, two enzyme forms differing in molecular weight when submitted to gel filtration, the smaller one is probably a degradation product of the larger one
45000
-
low molecular weight form, gel filtration, two enzyme forms differing in molecular weight when submitted to gel filtration, the smaller one is probably a degradation product of the larger one
55000
x * 55000, the enzyme shows two bands at 55000 and 57000 Da, SDS-PAGE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
homodimer
monomer
oligomer
-
STcys oligomerization is a secondary event resulting from its concentration in the Golgi via mechanisms independently mediated by its cytosolic tail and transmembrane region
additional information
?
-
x * 88300, fused to maltose-binding protein, calculated from amino acid sequence
monomer
-
1 * 44000, low molecular weight form, SDS-PAGE under reducing conditions
monomer
-
1 * 53500, high molecular weight form, SDS-PAGE under non-reducing conditions
monomer
-
1 * 41500, low molecular weight form, SDS-PAGE under non-reducing conditions
monomer
-
1 * 56000, high molecular weight form, SDS-PAGE under reducing conditions
additional information
the enzymes contain four conserved peptide motifs: L/large, S/small, motif III, and motif VS/very small
additional information
the enzymes contain four conserved peptide motifs: L/large, S/small, motif III, and motif VS/very small
additional information
the enzymes contain four conserved peptide motifs: L/large, S/small, motif III, and motif VS/very small
additional information
the enzymes contain four conserved peptide motifs: L/large, S/small, motif III, and motif VS/very small
additional information
the enzymes contain four conserved peptide motifs: L/large, S/small, motif III, and motif VS/very small
additional information
the enzymes contain four conserved peptide motifs: L/large, S/small, motif III, and motif VS/very small
additional information
the enzymes contain four conserved peptide motifs: L/large, S/small, motif III, and motif VS/very small
additional information
the enzymes contain four conserved peptide motifs: L/large, S/small, motif III, and motif VS/very small
additional information
the enzymes contain four conserved peptide motifs: L/large, S/small, motif III, and motif VS/very small
additional information
the enzymes contain four conserved peptide motifs: L/large, S/small, motif III, and motif VS/very small
additional information
the enzymes contain four conserved peptide motifs: L/large, S/small, motif III, and motif VS/very small
additional information
the enzymes contain four conserved peptide motifs: L/large, S/small, motif III, and motif VS/very small
additional information
-
the enzymes contain four conserved peptide motifs: L/large, S/small, motif III, and motif VS/very small
additional information
the enzymes contain four conserved peptide motifs: L/large, S/small, motif III, and motif VS/very small
additional information
-
the enzymes contain four conserved peptide motifs: L/large, S/small, motif III, and motif VS/very small
additional information
the enzymes contain four conserved peptide motifs: L/large, S/small, motif III, and motif VS/very small
additional information
the enzymes contain four conserved peptide motifs: L/large, S/small, motif III, and motif VS/very small
additional information
the enzymes contain four conserved peptide motifs: L/large, S/small, motif III, and motif VS/very small
additional information
the enzymes contain four conserved peptide motifs: L/large, S/small, motif III, and motif VS/very small
additional information
the enzymes contain four conserved peptide motifs: L/large, S/small, motif III, and motif VS/very small
additional information
the enzymes contain four conserved peptide motifs: L/large, S/small, motif III, and motif VS/very small
additional information
the enzymes contain four conserved peptide motifs: L/large, S/small, motif III, and motif VS/very small
additional information
the enzymes contain four conserved peptide motifs: L/large, S/small, motif III, and motif VS/very small
additional information
the enzymes contain four conserved peptide motifs: L/large, S/small, motif III, and motif VS/very small
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
glycoprotein
sialoprotein
-
recombinant Drosophila SiaT expressed in cultured insect cells possesses in vivo and in vitro autosialylation activity toward beta-linked GalNAc termini of its own N-linked glycans
additional information
-
deglycosylation of the enzyme is much more efficient in presence of methanol or ethanol
glycoprotein
-
contains at least 2 N-linked carbohydate chains of the complex type
glycoprotein
-
catalytic activity of the enzyme depends on the presence of oligosaccharide chains
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
sitting drop vapor diffusion, method truncated enzyme DELTA89 in complex with CMP using 0.1 M HEPES-NaOH pH 7.0, 20% (w/v) PEG 550 MME, 0.01 MCaCl2, 0.01 MMgCl2, or in complex with cytidine and phosphate using 0.1 M MES-NaOH pH 5.8, 20% (w/v) PEG 2000 MME, 0.01 M CaCl2, 0.01 M MgCl2
hanging-drop vapour-diffusion method at 20°C. The crystal belongs to space group P3(1)2(1) or P3(2)2(1), with unit-cell parameters a = b = 90.29, c = 204.33 A. X-ray diffraction data are collected to 2.5 A resolution
-
single crystals are grown by the hanging-drop vapor diffusion method at 20°C. Crystal structure of DELTA16psp26ST, the N-terminal truncated form of alpha2,6-sialyltransferase from Photobacterium sp. JT-ISH-224, complexed with a donor productCMPand an acceptor substrate lactose
microbatch method, using 100 mM Tris, pH 9, 40% (w/v) PEG 1000, and 100 mM lithium bromide
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
C139A
the mutant has almost the same activity (98%) and specificity as those of native enzyme
C139S
the mutant has almost the same activity (94%) and specificity as those of native enzyme
I411T/L433T
-
the mutant exhibits 5fold enhancement of the enzyme's specific activity compared with the wild type enzyme
L433S
-
the mutant exhibits 3fold enhancement of the enzyme's specific activity compared with the wild type enzyme
L433T
-
the mutant exhibits 3fold enhancement of the enzyme's specific activity compared with the wild type enzyme
D219A
site-directed mutagenesis, mutant of the conserved sialyl-motif contained by all members of the sialyltransferase family, 10.8fold increased Km for CMP-NeuAc, only slightly altered Km for the acceptor substrate
D271A
the mutant shows strongly reduced activity compared to the wild type enzyme
F208A
the mutant shows strongly reduced activity compared to the wild type enzyme
G221A
site-directed mutagenesis, mutant of the conserved sialyl-motif contained by all members of the sialyltransferase family, 1.6fold increased Km for CMP-NeuAc, only slightly altered Km for the acceptor substrate
K223A
site-directed mutagenesis, mutant of the conserved sialyl-motif contained by all members of the sialyltransferase family, 6.6fold increased Km for CMP-NeuAc, only slightly altered Km for the acceptor substrate
K355A
the mutant shows increased activity compared to the wild type enzyme
L190A
site-directed mutagenesis, mutant of the conserved sialyl-motif contained by all members of the sialyltransferase family, 11.9fold increased Km for CMP-NeuAc, only slightly altered Km for the acceptor substrate
Q232A
the mutant shows strongly reduced activity compared to the wild type enzyme
Q354A
the mutant shows reduced activity compared to the wild type enzyme
T224A
site-directed mutagenesis, mutant of the conserved sialyl-motif contained by all members of the sialyltransferase family, 1.3fold increased Km for CMP-NeuAc, only slightly altered Km for the acceptor substrate
T225A
site-directed mutagenesis, mutant of the conserved sialyl-motif contained by all members of the sialyltransferase family, 3.2fold increased Km for CMP-NeuAc, only slightly altered Km for the acceptor substrate
V184A
site-directed mutagenesis, mutant of the conserved sialyl-motif contained by all members of the sialyltransferase family, 6.8fold increased Km for CMP-NeuAc, only slightly altered Km for the acceptor substrate
V220A
site-directed mutagenesis, mutant of the conserved sialyl-motif contained by all members of the sialyltransferase family, 6.0fold increased Km for CMP-NeuAc, only slightly altered Km for the acceptor substrate
Y119F
the mutant shows reduced activity compared to the wild type enzyme
Y272A
the mutant shows strongly reduced activity compared to the wild type enzyme
additional information
additional information
-
construction of a chimeric enzyme with the N-terminal membrane portion of the rat core 2 beta1,6-GlcNAc-transferase, amino acid residues 1-52, and the residues 1-70 of the human alpha2,6-sialyltransferase, also FLAG-tagged, functional expression in CHO-K1 cells, broader acceptor substrate specificity than the wild-type
additional information
the DELTA108 mutant enzyme shows only sialyl transferase activity with specificity for mono-sialylation and a Km value for 6'-sialyl-N-acetyl-D-lactosamine of 84 mM while the DELTA89 mutant show a Km value for 6'-sialyl-N-acetyl-D-lactosamine of 8.3 mM
additional information
-
the truncated enzyme DELTA108 is active as alpha2,6-sialyltransferase and CMP-N-acetylneuraminate hydrolase
additional information
-
cloned as N- and C-His-tagged fusion proteins with different lengths (16-497 aa or 113-497 aa). Expression and activity assays indicate that the N-terminal 112 amino acid residues of the protein are not required for its alpha2,6-sialyltransferase activity. Among four truncated forms tested, N-His-tagged ELTA15Pd2,6ST(N) containing 16-497 amino acid residues has the highest expression level. Similar to the DELTA15Pd2,6ST(N), the shorter DELTA112Pd2,6ST(N) is active in a wide pH range of 7.5-10.0
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0 - 30
-
the enzyme is stable below 30°C for 1 h but shows significantly decreased activities at higher temperatures
20
purified enzyme is stable below 20°C but is rapidly inactivated at temperatures above 20°C
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
fractionation on Ultrogel AcA34 decreases activity, bovine serum albumin restores
-
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ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, in 50% glycerol, 35 mM cacodylate, pH 6, 0.45 M NaCl, 0.08% Triton CF-54, at least 1 year
-
-20°C, pure enzyme in 50% (v/v) glycerol containing 12 mM cacodylate buffer pH 5.3, at least 2 months, no loss of activity
-
0-4C, partially purified enzyme preparation, 2-4 weeks
4°C, partially purified enzyme preparation in 20% glycerol, v/v, at least 1 week
-
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CDP-ethanolamine-Sepharose column chromatography, ammonium sulfate precipitation, SP-50-Sephadex gel filtration, and Sephadex G-150 gel filtration
-
CDP-hexanolamine-agarose affinity chromatography
FLAG-tagged recombinant ST6Gal1 purified by precipitation with ammonium sulphate followed by affinity chromatography, with a recovery yield of 64%, 159fold
homogenized, centrifuged, resuspended in 140 mM-cacodylate/HCl buffer pH 6.8
-
homogenized, centrifuged, resuspended in 25 mM-cacodylate buffer pH 6.5 containing 0.15% Triton X-100, 75 mM NaCl and 10 mM MnCl2
N-terminal truncated form, by gel filtration, 15.2fold, with a yield of 53.2%
-
Ni-NTA column chromatography
partial
S-Sepharose column chromatography, heparin Sepharose column chromatography, and Superdex 75 gel filtration
homogenized, centrifuged, resuspended in 25 mM-cacodylate buffer pH 6.5 containing 0.15% Triton X-100, 75 mM NaCl and 10 mM MnCl2
-
homogenized, centrifuged, resuspended in 25 mM-cacodylate buffer pH 6.5 containing 0.15% Triton X-100, 75 mM NaCl and 10 mM MnCl2
-
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
a CHO clone displaying a high rat alpha2,6-ST activity co-transfected with dicistronic mRNA expression vectors pEDdc-alpha-hTSH and pEAdc-beta-hTSH in a ratio of 1:5
-
a full-length Drosophila SiaT protein with a C-terminal HA tag is transiently expressed in Drosophila S2 cells. A fraction of SiaT-HA protein expressed in S2 cell culture is secreted into the cell medium in soluble form
-
cloned as N- and C- His-tagged fusion proteins with different lengths (16-497 aa or 113-497 aa). Expression and activity assays indicate that the N-terminal 112 amino acid residues of the protein are not required for its alpha2,6-sialyltransferase activity but affect the solubility of the recombinant protein expressed in Escherichia coli
-
DNA and amino acid sequence analysis, detailed phylogenetic analysis of the ST6GalNAc family and the four subfamilies, sialyltransferases show a common genetic origin, by successive duplications of an ancestral gene, followed by divergent evolution, overview
DNA sequence determination, expression of various truncated forms lacking the transmembrane fragment as FLAG-tagged proteins, the chimeric mutant, and the membrane-bound enzyme form in CHO-K1 cells
-
DNA sequence determination, functional overexpression of full length cDNA and fragment of residues 113-1227, the latter fused to staphylococcal protein A, in COS-1 cells
-
enzyme expression analysis in Zaidela ascitic hepatoma cell lines and normal liver cells
-
expressed in CHO cells
expressed in COS-7 cells
expressed in Escherichia coli BL21 cells
expressed in Escherichia coli DH10B cells
expression cassettes of the full-length form in pLST-FL and of the truncated form (N-terminal Lys2 to Ala15 deletion) in pLST-DELTAN expressed in Escherichia coli
-
expression in Pichia pastoris, entry in the secretory pathway, i.e. excretion of the soluble enzyme to the medium, by usage of the N-terminal signal sequence of Saccharomyces cerevisiae alpha-factor, no hyperglycosylation
-
expression of the ST6Gal I enzyme in a galectin-1-sensitive murine T cell line
-
high level functional expression in Spodoptera frugiperda Sf9 insect cells via baculovirus infection using a vector that fuses the enzyme to the mouse IgM signal peptide and the IgG binding domain of the Staphylococcus aureus protein A at the N-terminus for secretion of the recombinant protein into the culture medium
-
overexpression of ST6Gal I in SW480 colon cancer cells that initially show a low level of ST6Gal I expression increases the sialylation of integrin beta1 and also increases the stability of the protein
ST6Gal I FLAG-pcDNA construct transiently transfected into COS-7 cells
ST6Gal1 cloned as N-terminal His-, Strep- and FLAG-tagged fusion proteins. FLAG-tagged recombinant ST6Gal1 expressed in fifth instar silkworm larval hemolymph using recombinant both cysteine protease- and chitinase-deficient Bombyx mori nucleopolyhedrovirus (BmNPV-CP--Chi-) bacmid
the putative mature form of JT-ISH-224 alpha2,6-sialyltransferase is overproduced in Escherichia coli
-
the truncated DELTA89 and DELTA108 variants of the recombinant human enzyme are expressed in human embryonic kidney cells
two pFlag-bST6Gal II vector constructions separately transfected in COS-1 cells for expression of either membrane-bound or soluble active forms of ST6Gal II
DNA and amino acid sequence analysis, detailed phylogenetic analysis of the ST6GalNAc family and the four subfamilies, sialyltransferases show a common genetic origin, by successive duplications of an ancestral gene, followed by divergent evolution, overview
DNA and amino acid sequence analysis, detailed phylogenetic analysis of the ST6GalNAc family and the four subfamilies, sialyltransferases show a common genetic origin, by successive duplications of an ancestral gene, followed by divergent evolution, overview
DNA and amino acid sequence analysis, detailed phylogenetic analysis of the ST6GalNAc family and the four subfamilies, sialyltransferases show a common genetic origin, by successive duplications of an ancestral gene, followed by divergent evolution, overview
DNA and amino acid sequence analysis, detailed phylogenetic analysis of the ST6GalNAc family and the four subfamilies, sialyltransferases show a common genetic origin, by successive duplications of an ancestral gene, followed by divergent evolution, overview
DNA and amino acid sequence analysis, detailed phylogenetic analysis of the ST6GalNAc family and the four subfamilies, sialyltransferases show a common genetic origin, by successive duplications of an ancestral gene, followed by divergent evolution, overview
DNA and amino acid sequence analysis, detailed phylogenetic analysis of the ST6GalNAc family and the four subfamilies, sialyltransferases show a common genetic origin, by successive duplications of an ancestral gene, followed by divergent evolution, overview
DNA and amino acid sequence analysis, detailed phylogenetic analysis of the ST6GalNAc family and the four subfamilies, sialyltransferases show a common genetic origin, by successive duplications of an ancestral gene, followed by divergent evolution, overview
DNA and amino acid sequence analysis, detailed phylogenetic analysis of the ST6GalNAc family and the four subfamilies, sialyltransferases show a common genetic origin, by successive duplications of an ancestral gene, followed by divergent evolution, overview
DNA and amino acid sequence analysis, detailed phylogenetic analysis of the ST6GalNAc family and the four subfamilies, sialyltransferases show a common genetic origin, by successive duplications of an ancestral gene, followed by divergent evolution, overview
DNA and amino acid sequence analysis, detailed phylogenetic analysis of the ST6GalNAc family and the four subfamilies, sialyltransferases show a common genetic origin, by successive duplications of an ancestral gene, followed by divergent evolution, overview
DNA and amino acid sequence analysis, detailed phylogenetic analysis of the ST6GalNAc family and the four subfamilies, sialyltransferases show a common genetic origin, by successive duplications of an ancestral gene, followed by divergent evolution, overview
DNA and amino acid sequence analysis, detailed phylogenetic analysis of the ST6GalNAc family and the four subfamilies, sialyltransferases show a common genetic origin, by successive duplications of an ancestral gene, followed by divergent evolution, overview
DNA and amino acid sequence analysis, detailed phylogenetic analysis of the ST6GalNAc family and the four subfamilies, sialyltransferases show a common genetic origin, by successive duplications of an ancestral gene, followed by divergent evolution, overview
DNA and amino acid sequence analysis, detailed phylogenetic analysis of the ST6GalNAc family and the four subfamilies, sialyltransferases show a common genetic origin, by successive duplications of an ancestral gene, followed by divergent evolution, overview
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
alginate oligosaccharide inhibits the expressions of the enzyme both in mRNA levels and protein levels
alpha2,6-ST activity in B lymphocytes is correlated positively with the level of alpha2,6-sialic acid in serum IgA1 in patients and controls
-
carbon tetrachloride administration significantly increases the level of plasma ST6Gal I as evidenced from significant increases in plasma aspartate aminotransferase (AST) and alanine aminotransferase (ALT) as hepatitis markers
expression of ST6GALNAC2 in B peripheral lymphocytes is significantly lower in patients with IgA nephropathy than that in normal controls
-
level of plasma ST6Gal I is increased in two different types of liver injury models: in zone 1 hepatocyte-injured rats, the level of plasma ST6Gal I is increased together with acute phase reactions. Meanwhile, in zone 3 hepatocyte-injured rats, ST6Gal I secretion is most likely triggered by oxidative stress
low level of enzyme 1 mRNA is observed in high microsatellite instability patients with colorectal cancer
prostaglandin F2alpha treatment for 72 h enhances the expression of enzyme mRNA
ST6Gal II gene is upregulated in cells stimulated by interleukin-6, whereas interleukin-1 and TNFalpha treatments have no effect on the expression of ST6Gal II. Inflammatory response induced by interleukin-6 treatment provokes an overexpression of ST6Gal II at 24 h and 48 h of treatment, its expression level in the treated cells is 2.5- and 5.6fold higher than in the control, respectively
the enzyme expression is increased in cancer of colon, breast, cervix, choriocarcinomas, acute myeloid leukemias, liver, and brain
-
the enzyme is upregulated in numerous types of cancer (including cervical, colon, gastric, glioma, leukemia, liver, melanoma, pancreatic, prostate, breast and ovarian cancer)
the expression level of the enzyme is increased in hepatocellular carcinoma tissues. Caveolin-1 upregulates the enyzme expression
-
carbon tetrachloride administration significantly increases the level of plasma ST6Gal I as evidenced from significant increases in plasma aspartate aminotransferase (AST) and alanine aminotransferase (ALT) as hepatitis markers
-
carbon tetrachloride administration significantly increases the level of plasma ST6Gal I as evidenced from significant increases in plasma aspartate aminotransferase (AST) and alanine aminotransferase (ALT) as hepatitis markers
-
-
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
biotechnology
-
recombinant enzyme may be used for in vitro synthesis of oligosaccharides
medicine
synthesis
medicine
protein sialylation might be a target to overcome radioresistance in radiation therapie
medicine
-
two kinds of sandwich enzyme-linked immunosorbent assay (ELISA) systems are very useful tools for measuring plasma ST6Gal I, which represents a potential biomarker for diagnosing hepatic diseases
medicine
-
two kinds of sandwich enzyme-linked immunosorbent assay (ELISA) systems are very useful tools for measuring plasma ST6Gal I, which represents a potential biomarker for diagnosing hepatic diseases
medicine
-
two kinds of sandwich enzyme-linked immunosorbent assay (ELISA) systems are very useful tools for measuring plasma ST6Gal I, which represents a potential biomarker for diagnosing hepatic diseases
medicine
the enzyme is associated with reduced recurrence-free intervals and a poorer overall survival in ovarian, prostate and pancreatic cancer
medicine
patients with pancreatic ductal adenocarcinoma expressing higher enzyme levels present poorer prognosis compared to other groups
medicine
-
increased enzyme expression in hepatocellular carcinoma tissues correlates with poor prognosis
medicine
-
two kinds of sandwich enzyme-linked immunosorbent assay (ELISA) systems are very useful tools for measuring plasma ST6Gal I, which represents a potential biomarker for diagnosing hepatic diseases
-
synthesis
-
recombinant enzyme may be used for in vitro synthesis of oligosaccharides
synthesis
-
enzyme can be exploited as biocatalyst in the synthesis of interesting non-natural compounds, especially in view of chemical, regiospecific sialylation, chemo-enzymatic synthesis of modified carbohydrate ligands, and their suitability as probes for studying molecular recognition phenomena
synthesis
-
enzyme can be exploited as biocatalyst in the synthesis of interesting non-natural compounds, especially in view of chemical, regiospecific sialylation, chemo-enzymatic synthesis of modified carbohydrate ligands, and their suitability as probes for studying molecular recognition phenomena
synthesis
-
because this enzyme is most active at basic pH, sialyltransferase obtained from Photobacterium leiognathi JT-SHIZ-145 is a promising tool for the efficient production of sialosides and the modification of glycoconjugates
synthesis
-
the Photobacterium sialyltransferase can be used in the synthesis of sialoside analogues having a large substituent at the 9-position of Neu5Ac
synthesis
-
application of the alpha2,6-trans-sialidase activity of DELTA15Pd2,6ST in the synthesis of sialosides
synthesis
-
the enzyme may be a powerful tool for the synthesis of sialosides and the modification of sialyl-glycoconjugates
synthesis
-
because this enzyme is most active at basic pH, sialyltransferase obtained from Photobacterium leiognathi JT-SHIZ-145 is a promising tool for the efficient production of sialosides and the modification of glycoconjugates
-
synthesis
-
the enzyme may be a powerful tool for the synthesis of sialosides and the modification of sialyl-glycoconjugates
-
EXTERNAL LINKS (specific for EC-Number 2.4.3.1)
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Release 2026.1 (March 2026)
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