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Information on EC 2.4.99.1 - beta-galactoside alpha-(2,6)-sialyltransferase and Organism(s) Rattus norvegicus and UniProt Accession Q701R3

for references in articles please use BRENDA:EC2.4.99.1
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EC Tree
IUBMB Comments
The enzyme acts on the terminal non-reducing beta-D-galactosyl residue of the oligosaccharide moiety of glycoproteins and glycolipids.
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Select one or more organisms in this record:
This record set is specific for:
Rattus norvegicus
UNIPROT: Q701R3
Word Map
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
The taxonomic range for the selected organisms is: Rattus norvegicus
Synonyms
(alpha-N-acetyl-neuraminyl-2,3-beta-galactosyl-1,3)-N-acetylgalactosaminide alpha2,6-sialyltransferase 5, 2,6ST, 6STase, alpha 2,6-sialyltransferase, alpha 2,6-ST, alpha(2,6)-sialyltransferase, alpha(2,6)-ST, alpha-(2->6)-sialyltransferase, alpha-2,6-sialyltransferase, alpha2,6 sialyltransferase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6STase
248
-
alpha 2,6-sialyltransferase
248
-
alpha 2,6-ST
-
-
-
-
alpha-(2->6)-sialyltransferase
248
-
alpha-2,6-sialyltransferase
248
-
alpha2,6-sialyltransferase
alpha2,6-sialyltransferase ST6Gal I
248
-
alpha2,6-ST
248
-
alpha2-6 sialyltransferase
-
-
-
-
antigens, CD75
-
-
-
-
B-cell antigen CD75
-
-
-
-
beta-galactoside alpha2,6-sialyltransferase
CMP-acetylneuraminate-galactosylglycoprotein sialyltransferase
-
-
-
-
CMP-acetylneuraminate-glycoprotein sialyltransferase
-
-
-
-
CMP-acetylneuraminate-lactosylceramide-sialyltransferase
-
-
-
-
CMP-N-acetylneuraminic acid-glycoprotein sialyltransferase
-
-
-
-
CMP-N-acetylneuraminic acid:lactosylceramide sialyltransferase
-
-
-
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CMP-sialic acid:lactosylceramide sialyltransferase
-
-
-
-
cytidine monophosphoacetylneuraminate-galactosylglycoprotein sialyltransferase
-
-
-
-
cytidine monophosphoacetylneuraminate-lactosylceramide sialyltransferase
-
-
-
-
Galbeta1,4-GlcNAc alpha2,6 sialyltransferase
248
-
GM3-synthase
-
-
-
-
R-2,6-sialyltransferase
248
-
sialotransferase
-
-
-
-
sialyltransferase
-
-
-
-
sialyltransferase, cytidine monophosphoacetylneuraminate-galactosylglycoprotein
-
-
-
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sialyltransferase, cytidine monophosphoacetylneuraminate-lactosylceramide
-
-
-
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ST6Gal
267544, 281126
-
ST6Gal I
ST6Gal-I
248
-
ST6Gal1
267544
-
additional information
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
CMP-N-acetyl-beta-neuraminate + beta-D-galactosyl-R = CMP + N-acetyl-alpha-neuraminyl-(2->6)-beta-D-galactosyl-R
show the reaction diagram
Val220 participates in binding the common cytidine moiety in substrate CMP-NeuAc and inhibitor CDP
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
glycosyl group transfer
-
-
-
-
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.
CAS REGISTRY NUMBER
COMMENTARY hide
55071-95-9
-
9075-81-4
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
CMP-9''-benzamido-Neu5Ac + N-acetyllactosamine
?
show the reaction diagram
-
-
-
-
?
CMP-9''-phenylacetamido-Neu5Ac + N-acetyllactosamine
?
show the reaction diagram
-
-
-
-
?
CMP-9''-phenylhexanamido-Neu5Ac + N-acetyllactosamine
?
show the reaction diagram
-
-
-
-
?
CMP-9''-phenylpropionamido-Neu5Ac + N-acetyllactosamine
?
show the reaction diagram
-
-
-
-
?
CMP-9-acetamido-N-acetylneuraminate + asialo-alpha1-acid glycoprotein
?
show the reaction diagram
-
-
-
-
?
CMP-9-amino-N-acetylneuraminate + asialo-alpha1-acid glycoprotein
?
show the reaction diagram
-
-
-
-
?
CMP-9-azido-N-acetylneuraminate + asialo-alpha1-acid glycoprotein
?
show the reaction diagram
-
-
-
-
?
CMP-9-benzamido-N-acetylneuraminate + asialo-alpha1-acid glycoprotein
?
show the reaction diagram
-
-
-
-
?
CMP-9-hexanoylamido-N-acetylneuraminate + asialo-alpha1-acid glycoprotein
?
show the reaction diagram
-
-
-
-
?
CMP-9-O-acetyl-N-acetylneuraminate + asialo-alpha1-acid glycoprotein
?
show the reaction diagram
-
comparable or even higher transfer rates than with CMP-N-acetylneuraminate
-
-
?
CMP-9-O-acetyl-N-acetylneuraminate + asialo-alpha1-acid glycoprotein
CMP + ?
show the reaction diagram
-
-
-
-
?
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 + ?
show the reaction diagram
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 + ?
show the reaction diagram
-
0.2% of the activity with Galbeta(1-3)GlcNAcbeta-O-Me
-
-
?
CMP-N-acetylneuraminate + (Gal-3-O-Me)beta(1-3)(GlcNAc-6-O-Me)beta-O-Me
CMP + ?
show the reaction diagram
-
50% of the activity with Galbeta(1-3)GlcNAcbeta-O-Me
-
-
?
CMP-N-acetylneuraminate + (Gal-3-O-Me)beta(1-3)GlcNAcbeta-O-Me
CMP + ?
show the reaction diagram
-
80% of the activity with Galbeta(1-3)GlcNAcbeta-O-Me
-
-
?
CMP-N-acetylneuraminate + 5-(5-dimethylaminonaphthalene-1-sulfonyl-2-(2-aminoethoxy))ethyl beta-lactose
CMP + ?
show the reaction diagram
-
-
-
-
?
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
show the reaction diagram
-
-
-
-
?
CMP-N-acetylneuraminate + asialo-agalacto-prothrombin
CMP + agalacto-prothrombin
show the reaction diagram
-
-
-
-
?
CMP-N-acetylneuraminate + asialo-apoceruloplasmin
CMP + apoceruloplasmin
show the reaction diagram
-
best substrate
-
-
?
CMP-N-acetylneuraminate + asialo-ceruloplasmin
CMP + ceruloplasmin
show the reaction diagram
-
-
-
-
?
CMP-N-acetylneuraminate + asialo-chorionic gonadotropin
CMP + chorionic gonadotropin
show the reaction diagram
-
acceptor protein from human source
-
-
?
CMP-N-acetylneuraminate + asialo-fetuin
CMP + fetuin
show the reaction diagram
CMP-N-acetylneuraminate + asialo-fibrinogen
CMP + fibrinogen
show the reaction diagram
-
-
-
-
?
CMP-N-acetylneuraminate + asialo-orosomucoid
CMP + orosomucoid
show the reaction diagram
CMP-N-acetylneuraminate + asialo-prothrombin
CMP + prothrombin
show the reaction diagram
-
-
-
-
?
CMP-N-acetylneuraminate + asialo-thyroglobulin
CMP + thyroglobulin
show the reaction diagram
-
-
-
-
?
CMP-N-acetylneuraminate + asialo-transferrin
CMP + transferrin
show the reaction diagram
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
show the reaction diagram
-
-
-
-
?
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
show the reaction diagram
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
show the reaction diagram
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
show the reaction diagram
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 + ?
show the reaction diagram
-
as active as Galbeta(1-3)GlcNAcbeta-O-Me
-
-
?
CMP-N-acetylneuraminate + Galbeta(1-3)(GlcNAc-6-O-Me)beta-O-Me
CMP + ?
show the reaction diagram
-
80% of the activity with Galbeta(1-3)GlcNAcbeta-O-Me
-
-
?
CMP-N-acetylneuraminate + Galbeta(1-3)GlcNAcbeta-O-Me
CMP + NeuAcalpha(2-6)Galbeta(1-3)GlcNAcbeta-O-Me
show the reaction diagram
-
-
-
-
?
CMP-N-acetylneuraminate + lacto-N-neotetraose
?
show the reaction diagram
-
-
-
-
?
CMP-N-acetylneuraminate + lactose
CMP + 6'-sialyllactose
show the reaction diagram
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 + ?
show the reaction diagram
-
90% of the activity with Galbeta(1-3)GlcNAcbeta-O-Me
-
-
?
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 + ?
show the reaction diagram
-
as active as Galbeta(1-3)GlcNAcbeta-O-Me
-
-
?
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 + ?
show the reaction diagram
-
110% of the activity with Galbeta(1-3)GlcNAcbeta-O-Me
-
-
?
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 + ?
show the reaction diagram
-
130% of the activity with Galbeta(1-3)GlcNAcbeta-O-Me
-
-
?
CMP-N-acetylneuraminate + N-acetyllactosamine
?
show the reaction diagram
-
-
-
-
?
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 + ?
show the reaction diagram
-
70% of the activity with Galbeta(1-3)GlcNAcbeta-O-Me
-
-
?
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 + ?
show the reaction diagram
-
as active as Galbeta(1-3)GlcNAcbeta-O-Me
-
-
?
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 + ?
show the reaction diagram
-
60% of the activity with Galbeta(1-3)GlcNAcbeta-O-Me
-
-
?
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 + ?
show the reaction diagram
-
50% of the activity with Galbeta(1-3)GlcNAcbeta-O-Me
-
-
?
CMP-N-aminoacetylneuraminate + asialo-alpha1-acid glycoprotein
?
show the reaction diagram
-
-
-
-
?
CMP-N-formylneuraminate + asialo-alpha1-acid glycoprotein
?
show the reaction diagram
-
-
-
-
?
CMP-N-glycolylneuraminate + asialo-alpha1-acid glycoprotein
?
show the reaction diagram
-
comparable or even higher transfer rates than with CMP-N-acetylneuraminate
-
-
?
cytidine 5'-monophosphate 3-(axial)-fluoro-N-acetylneuraminic acid + alpha-lactose
?
show the reaction diagram
-
[15N]Phe-labeled ST6Gal-I with a 15fold excess of CMP-3FNeuAc
-
-
?
cytidine 5'-monophosphate 4-O-(4-carboxy-2,2,6,6-tetramethylpiperidine-1-oxyl) + alpha-N-acetyllactosamine
?
show the reaction diagram
-
-
-
-
?
cytidine-5'-monophospho-sialic acid + N-acetyllactosamine
?
show the reaction diagram
-
-
-
-
?
N-acetyllactosamine 4-O-(4-carboxy-2,2,6,6-tetramethylpiperidine-1-oxyl)
?
show the reaction diagram
-
[15N]Phe-labeled ST6Gal-I with a 20fold excess of N-acetyllactosamine 4-O-(4-carboxy-2,2,6,6-tetramethylpiperidine-1-oxyl)
-
-
?
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
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
show the reaction diagram
-
-
-
-
?
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
show the reaction diagram
additional information
?
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
MgCl2
-
slight stimulation at 5 mM
additional information
-
no metal ion requirement
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
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
CMP
-
is an efficient competitive inhibitor
CMP-4-O-[2,2,6,6-tetramethylpiperidine-1-oxyl]
-
-
CMP-4-O-[4-carboxy-2,2,6,6-tetramethylpiperidinine-1-oxyl]
-
-
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
deoxycholate
-
9fold stimulation at 0.25%, inactivation at 0.5%
endo F
-
inactivation due to deglycosylation of the enzyme, best in methanol or ethanol, less efficient than glycanase
-
Endogenous acidic peptide
-
heat-stable, amino acid composition
-
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
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
deoxycholate
-
9fold stimulation at 0.25%, inhibition at 0.5%
EDTA
-
activation
natural factor from rat colon
-
may also be present in rat brain and kidney; partially purified; 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; stimulation is decreased by CTP, no activation at 0.75 mM CTP
-
Triton CF-54/Tween 80
-
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
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
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
-
-
11.2
(Gal-3-O-Me)beta(1-3)(GlcNAc-6-O-Me)beta-O-Me
4.1
(Gal-3-O-Me)beta(1-3)GlcNAcbeta-O-Me
-
-
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
-
-
0.14 - 0.53
asialo-alpha1-acid glycoprotein
-
0.078
asialo-ceruloplasmin
-
expressed as concentration of acceptor sites
-
0.21
asialo-transferrin
-
-
-
1 - 6.5
beta-D-galactosyl-(1->4)-N-acetyl-beta-D-glucosamine
0.051
CMP-9''-benzamido-Neu5Ac
-
pH 5.0, 37°C
0.05
CMP-9''-phenylacetamido-Neu5Ac
-
pH 5.0, 37°C
0.098
CMP-9''-phenylhexanamido-Neu5Ac
-
pH 5.0, 37°C
0.165
CMP-9''-phenylpropionamido-Neu5Ac
-
pH 5.0, 37°C
0.12
CMP-9-acetamido-N-acetylneuraminate
-
-
0.72
CMP-9-amino-N-acetylneuraminate
-
-
0.03
CMP-9-benzamido-N-acetylneuraminate
-
-
0.0053 - 0.4
CMP-N-acetylneuraminate
0.12
cytidine-5'-monophospho-sialic acid
-
pH 5.0, 37°C
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
4.3
Galbeta(1-3)(GlcNAc-6-O-Me)beta-O-Me
-
-
1.7
Galbeta(1-3)GlcNAcbeta-O-Me
1.67
lacto-N-neotetraose
-
-
129
lactose
-
-
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
1.62 - 10
N-acetyllactosamine
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
-
-
additional information
additional information
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
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
-
-
0.07 - 0.67
beta-D-galactosyl-(1->4)-N-acetyl-beta-D-glucosamine
0.05 - 0.69
CMP-N-acetylneuraminate
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
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
-
-
0.01 - 0.44
beta-D-galactosyl-(1->4)-N-acetyl-beta-D-glucosamine
0.13 - 7.3
CMP-N-acetylneuraminate
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0047 - 0.016
CDP
4.07
CMP-4-O-[2,2,6,6-tetramethylpiperidine-1-oxyl]
-
pH 6.5, 37°C
0.79
CMP-4-O-[4-carboxy-2,2,6,6-tetramethylpiperidinine-1-oxyl]
-
pH 6.5, 37°C
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
8.7
CMP-4-O-[2,2,6,6-tetramethylpiperidine-1-oxyl]
Rattus norvegicus
-
pH 6.5, 37°C
1.7
CMP-4-O-[4-carboxy-2,2,6,6-tetramethylpiperidinine-1-oxyl]
Rattus norvegicus
-
pH 6.5, 37°C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.00000022
-
hepatocyte
0.00083
-
partially purified enzyme
0.016
-
crude enzyme
2.6
-
159fold purified enzyme
8.2
-
purified enzyme
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6 - 6.5
-
2-(N-morpholino)ethane sulfonic acid buffer
6.8
-
assay at
7.5
-
Tris-HCl buffer
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5 - 9.7
-
about 65% of maximal activity at pH 5 and about half-maximal activity at pH 9.7
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.3
-
isoelectric focusing
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
ST6GAL2, fragment
SwissProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
cultured cells isolated from the tumor behave as normal hepatocytes; no enzyme activity in Zaidela ascitic hepatoma, but 3.6fold reduced mRNA content of a larger transcript size compared to normal liver cells
Manually annotated by BRENDA team
-
from heart and abdominal aorta
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
the enzyme is a Golgi type II transmembrane glycosyltransferase
Manually annotated by BRENDA team
-
; isoform Stcys is found in both the endoplasmic reticulum and in Golgi
Manually annotated by BRENDA team
the enzyme is a Golgi type II transmembrane glycosyltransferase
Manually annotated by BRENDA team
-
in medial-trans regions. Isoform Stcys is found in both the endoplasmic reticulum and in Golgi; in medial-trans regions. Isoform STtyr is restricted to Golgi in most cells
-
Manually annotated by BRENDA team
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
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
-
recombinant ST6Gal1 can be used as a key enzyme for the synthesis of an artificial sialoglycopolymer for potentially blocking influenza virus infection
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
Sequence
SIAT2_RAT
525
1
59917
Swiss-Prot
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
40000
-
1 * 40000, SDS-PAGE
40500
-
1 * 40500, SDS-PAGE under reducing conditions
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
glycoprotein
-
catalytic activity of the enzyme depends on the presence of oligosaccharide chains; contains at least 2 N-linked carbohydate chains of the complex type
additional information
-
deglycosylation of the enzyme is much more efficient in presence of methanol or ethanol
CRYSTALLIZATION/commentary
ORGANISM
UNIPROT
LITERATURE
microbatch method, using 100 mM Tris, pH 9, 40% (w/v) PEG 1000, and 100 mM lithium bromide
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C350A/C361A
-
inactive
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
H367A
-
inactive
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
N230A
-
inactive
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
Y366A
-
inactive
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5 - 9
-
purified enzyme is relatively stable over a wide range of pH
702879
5.3
-
and below, storage stability decreases with t1/2: about 3 months
637270
6
-
full stability for at least 1 year
637270
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
20
-
purified enzyme is stable below 20°C but is rapidly inactivated at temperatures above 20°C
67
-
30 s, 90% loss of activity
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
high NaCl concentrations stabilize during storage
-
ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Methanol
-
stable at 10%, 37°C
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
-
3°C, microsomal fraction, 2 weeks
-
PURIFICATION/commentary
ORGANISM
UNIPROT
LITERATURE
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
-
further purification of commercial rat liver enzyme
-
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
-
isoform STcys; isoform STtyr
-
Ni-NTA column chromatography and Superdex-75 gel filtration
-
soluble ST6Gal I-FLAG purified from conditioned media on affinity gel
-
CLONED/commentary
ORGANISM
UNIPROT
LITERATURE
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
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
-
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
enzyme expression analysis in Zaidela ascitic hepatoma cell lines and normal liver cells
-
expressed in HEK-293 and 293-F cells
-
expression in COS cells
-
expression of the ST6Gal I enzyme in a galectin-1-sensitive murine T cell line
-
expression of wild-type and mutants in COS-1 cells
-
isoform STcys expressed in CHO cells or in HeLa cells; isoform STtyr expressed in CHO cells or in HeLa cells
-
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
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
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
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
-
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
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Higa, H.H.; Paulson, J.C.
Sialylation of glycoprotein oligosaccharides with N-acetyl-, N-glycolyl-, and N-O-diacetylneuraminic acids
J. Biol. Chem.
260
8838-8849
1985
Bos taurus, Rattus norvegicus
Manually annotated by BRENDA team
Gross, H.J.; Rose, U.; Krause, J.M.; Paulson, J.C.; Schmid, K.; Feeney, R.E.; Brossmer, R.
Transfer of synthetic sialic acid analogues to N- and O-linked glycoprotein glycans using four different mammalian sialyltransferases
Biochemistry
28
7386-7392
1989
Rattus norvegicus
Manually annotated by BRENDA team
Albarracin, I.; Lassaga, F.E.; Caputto, R.
Purification and characterization of an endogenous inhibitor of the sialyltransferase CMP-N-acetylneuraminate: lactosylceramide alpha 2,6-N-acetylneuraminyltransferase (EC 2.4.99.-)
Biochem. J.
254
559-565
1988
Gallus gallus, Rattus norvegicus
Manually annotated by BRENDA team
Freischutz, B.; Saito, M.; Rahmann, H.; Yu, R.K.
Activities of five different sialyltransferases in fish and rat brains
J. Neurochem.
62
1965-1973
1994
Oreochromis mossambicus, Rattus norvegicus, Rattus norvegicus Sprague-Dawley
Manually annotated by BRENDA team
Hickman, J.; Ashwell, G.; Morell, A.G.; Van den Hamer, C.J.A.; Scheinberg, I.H.
Physical and chemical studies on ceruloplasmin. 8. Preparation of N-acetylneuraminic acid-1-14C-labeled ceruloplasmin
J. Biol. Chem.
245
759-766
1970
Rattus norvegicus, Rattus norvegicus Sprague-Dawley
Manually annotated by BRENDA team
Weinstein, J.; de Souza-e-Silva, U.; Paulson, J.C.
Sialylation of glycoprotein oligosaccharides N-linked to asparagine. Enzymatic characterization of a Gal beta 1-3(4)GlcNAc alpha 2-3 sialyltransferase and a Gal beta 1-4GlcNAc alpha 2-6 sialyltransferase from rat liver
J. Biol. Chem.
257
13845-13853
1982
Rattus norvegicus
Manually annotated by BRENDA team
Weinstein, J.; de Souza-e-Silva, U.; Paulson, J.C.
Purification of a Gal beta 1-4GlcNAc alpha 2-6 sialyltransferase and a Gal beta 1-3(4)GlcNAc alpha 2-3 sialyltransferase to homogeneity from rat liver
J. Biol. Chem.
257
13835-13844
1982
Rattus norvegicus
Manually annotated by BRENDA team
Bernacki, R.J.; Gurtoo, H.L.
Differential inhibition of rat liver sialyltransferase(s) by various aflatoxins and their metabolites
Res. Commun. Chem. Pathol. Pharmacol.
10
681-692
1975
Rattus norvegicus
Manually annotated by BRENDA team
Fast, D.G.; Jamieson, J.C.; McCaffrey, G.
The role of the carbohydrate chains of Gal beta-1,4-GlcNAc alpha 2,6-sialyltransferase for enzyme activity
Biochim. Biophys. Acta
1202
325-330
1993
Rattus norvegicus
Manually annotated by BRENDA team
Jain, N.; Sudhakar, C.; Das, M.R.
Regulation of expression of beta-galactoside alpha 2,6-sialyltransferase in a rat tumor, Zajdela ascitic hepatoma
FEBS Lett.
317
147-151
1993
Rattus norvegicus
Manually annotated by BRENDA team
Van Dorst, J.A.L.M.; Tikkanen, J.M.; Krezdorn, C.H.; Streiff, M.B.; Berger, E.G.; Van Kuik, J.A.; Kamerling, J.P.; Vliegenthart, J.F.G.
Exploring the substrate specificities of alpha-2,6- and alpha-2,3-sialyltransferases using synthetic acceptor analogs
Eur. J. Biochem.
242
674-681
1996
Homo sapiens, Rattus norvegicus
Manually annotated by BRENDA team
Datta, A.K.; Paulson, J.C.
The sialyltransferase 'sialylmotif' participates in binding the donor substrate CMP-NeuAc
J. Biol. Chem.
270
1497-1500
1995
Rattus norvegicus (P13721)
Manually annotated by BRENDA team
Nagpurkar, A.; Hunt, D.; Mookerjea, S.
Specific stimulation of alpha 2-6 sialyltransferase activity by a novel cytosolic factor from rat colon
Int. J. Biochem. Cell Biol.
28
1337-1348
1996
Rattus norvegicus, Rattus norvegicus Sprague-Dawley
Manually annotated by BRENDA team
Nakamura, M.; Tsunoda, A.; Yanagisawa, K.; Furukawa, Y.; Kikuchi, J.; Iwase, S.; Sakai, T.; Larson, G.; Saito, M.
CMP-NeuAc:Galbeta1->4GlcNAc alpha2->6sialyltransferase catalyzes NeuAc transfer to glycolipids
J. Lipid Res.
38
1795-1806
1997
Homo sapiens, Rattus norvegicus
Manually annotated by BRENDA team
Dufner, G.; Schworer, R.; Muller, B.; Schmidt, R.R.
Base- and sugar-modified cytidine monophosphate N-acetylneuraminic acid (CMP-Neu5Ac) analogues - synthesis and studies with alpha(2-6)-sialyltransferase from rat liver
Eur. J. Org. Chem.
8
1467-1482
2000
Rattus norvegicus
-
Manually annotated by BRENDA team
Halliday, J.A.W.; Franks, A.H.; Ramsdale, T.E.; Martin, R.; Palant, E.
A rapid, semi-automated method for detection of Galbeta1-4GlcNAc alpha2,6-sialyltransferase (EC 2.4.99.1) activity using the lectin Sambucus nigra agglutinin
Glycobiology
11
557-564
2001
Homo sapiens, Rattus norvegicus
Manually annotated by BRENDA team
Gross, H.J.; Brossmer, R.
Enzymic transfer of sialic acids modified at C-5 employing four different sialyltransferases
Glycoconjugate J.
12
739-746
1995
Homo sapiens, Rattus norvegicus
Manually annotated by BRENDA team
Kim, H.G.; Yang, S.M.; Lee, Y.C.; Do, S.I.; Chung, I.S.; Yang, J.M.
High-level expression of human glycosyltransferases in insect cells as biochemically active form
Biochem. Biophys. Res. Commun.
305
488-493
2003
Homo sapiens, Rattus norvegicus
Manually annotated by BRENDA team
Galan, M.C.; Venot, A.P.; Boons, G.J.
Glycosyltransferase activity can be modulated by small conformational changes of acceptor substrates
Biochemistry
42
8522-8529
2003
Rattus norvegicus
Manually annotated by BRENDA team
Galan, M.C.; Dodson, C.S.; Venot, A.P.; Boons, G.J.
Glycosyltransferase activity can be selectively modulated by chemical modifications of acceptor substrates
Bioorg. Med. Chem. Lett.
14
2205-2208
2004
Rattus norvegicus
Manually annotated by BRENDA team
Chen, T.L.; Chen, C.; Bergeron, N.Q.; Close, B.E.; Bohrer, T.J.; Vertel, B.M.; Colley, K.J.
The two rat alpha 2,6-sialyltransferase (ST6Gal I) isoforms: evaluation of catalytic activity and intra-Golgi localization
Glycobiology
13
109-117
2003
Rattus norvegicus
Manually annotated by BRENDA team
Amano, M.; Galvan, M.; He, J.; Baum, L.G.
The ST6Gal I sialyltransferase selectively modifies N-glycans on CD45 to negatively regulate galectin-1-induced CD45 clustering, phosphatase modulation, and T cell death
J. Biol. Chem.
278
7469-7475
2003
Rattus norvegicus
Manually annotated by BRENDA team
Fenteany, F.H.; Colley, K.J.
Multiple signals are required for alpha2,6-sialyltransferase (ST6Gal I) oligomerization and Golgi localization
J. Biol. Chem.
280
5423-5429
2005
Rattus norvegicus
Manually annotated by BRENDA team
Harduin-Lepers, A.; Mollicone, R.; Delannoy, P.; Oriol, R.
The animal sialyltransferases and sialyltransferase-related genes: a phylogenetic approach
Glycobiology
15
805-817
2005
Anopheles gambiae (Q683N9), Bos taurus (A5D7T4), Bos taurus (O18974), Danio rerio (Q6KB61), Danio rerio (Q701R2), Drosophila melanogaster (Q9GU23), Drosophila pseudoobscura (Q683P0), Drosophila yakuba (Q683P1), Gallus gallus (Q701R0), Gallus gallus (Q92182), Homo sapiens, Homo sapiens (P15907), Homo sapiens (Q96JF0), Mus musculus, Mus musculus (Q64685), Oryzias latipes (Q5K027), Oryzias latipes (Q5K028), Pan troglodytes (Q701R4), Pan troglodytes (Q701R5), Rattus norvegicus (P13721), Rattus norvegicus (Q701R3), Takifugu rubripes (Q5QQ37), Takifugu rubripes (Q6KB62), Xenopus tropicalis (Q701R1)
Manually annotated by BRENDA team
Kajihara, Y.; Kamitani, T.; Sato, R.; Kamei, N.; Miyazaki, T.; Okamoto, R.; Sakakibara, T.; Tsuji, T.; Yamamoto, T.
Synthesis of CMP-9-modified-sialic acids as donor substrate analogues for mammalian and bacterial sialyltransferases
Carbohydr. Res.
342
1680-1688
2007
Photobacterium sp., Rattus norvegicus
Manually annotated by BRENDA team
Liu, S.; Venot, A.; Meng, L.; Tian, F.; Moremen, K.W.; Boons, G.; Prestegard, J.H.
Spin-labeled analogs of CMP-NeuAc as NMR probes of the alpha -2,6-sialyltransferase ST6Gal I
Chem. Biol.
14
409-418
2007
Rattus norvegicus (P13721)
Manually annotated by BRENDA team
Futakawa, S.; Kitazume, S.; Oka, R.; Ogawa, K.; Hagiwara, Y.; Kinoshita, A.; Miyashita, K.; Hashimoto, Y.
Development of sandwich enzyme-linked immunosorbent assay systems for plasma beta-galactoside alpha2,6-sialyltransferase, a possible hepatic disease biomarker
Anal. Chim. Acta
631
116-120
2009
Homo sapiens, Mus musculus, Mus musculus C57BL/6, Rattus norvegicus
Manually annotated by BRENDA team
Liu, S.; Meng, L.; Moremen, K.W.; Prestegard, J.H.
Nuclear magnetic resonance structural characterization of substrates bound to the alpha-2,6-sialyltransferase, ST6Gal-I
Biochemistry
48
11211-11219
2009
Rattus norvegicus
Manually annotated by BRENDA team
Ogata, M.; Nakajima, M.; Kato, T.; Obara, T.; Yagi, H.; Kato, K.; Usui, T.; Park, E.Y.
Synthesis of sialoglycopolypeptide for potentially blocking influenza virus infection using a rat alpha2,6-sialyltransferase expressed in BmNPV bacmid-injected silkworm larvae
BMC Biotechnol.
9
54
2009
Rattus norvegicus (P13721)
Manually annotated by BRENDA team
Kitazume, S.; Oka, R.; Ogawa, K.; Futakawa, S.; Hagiwara, Y.; Takikawa, H.; Kato, M.; Kasahara, A.; Miyoshi, E.; Taniguchi, N.; Hashimoto, Y.
Molecular insights into beta-galactoside alpha2,6-sialyltransferase secretion in vivo
Glycobiology
19
479-487
2009
Homo sapiens, Homo sapiens (P15907), Rattus norvegicus (P13721)
Manually annotated by BRENDA team
Damiani, R.; Oliveira, J.E.; Vorauer-Uhl, K.; Peroni, C.N.; Vianna, E.G.; Bartolini, P.; Ribela, M.T.
Stable expression of a human-like sialylated recombinant thyrotropin in a Chinese hamster ovary cell line expressing alpha2,6-sialyltransferase
Protein Expr. Purif.
67
7-14
2009
Rattus norvegicus
Manually annotated by BRENDA team
Meng, L.; Forouhar, F.; Thieker, D.; Gao, Z.; Ramiah, A.; Moniz, H.; Xiang, Y.; Seetharaman, J.; Milaninia, S.; Su, M.; Bridger, R.; Veillon, L.; Azadi, P.; Kornhaber, G.; Wells, L.; Montelione, G.T.; Woods, R.J.; Tong, L.; Moremen, K.W.
Enzymatic basis for N-glycan sialylation: structure of rat alpha2,6-sialyltransferase (ST6GAL1) reveals conserved and unique features for glycan sialylation
J. Biol. Chem.
288
34680-34698
2013
Rattus norvegicus (P13721)
Manually annotated by BRENDA team
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