Information on EC 2.4.99.4 - beta-galactoside alpha-2,3-sialyltransferase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
2.4.99.4
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RECOMMENDED NAME
GeneOntology No.
beta-galactoside alpha-2,3-sialyltransferase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
CMP-N-acetylneuraminate + beta-D-galactosyl-(1->3)-N-acetyl-alpha-D-galactosaminyl-R = CMP + alpha-N-acetylneuraminyl-(2->3)-beta-D-galactosyl-(1->3)-N-acetyl-alpha-D-galactosaminyl-R
show the reaction diagram
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
glycosyl group transfer
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
ganglio-series glycosphingolipids biosynthesis
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globo-series glycosphingolipids biosynthesis
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Glycosaminoglycan biosynthesis - keratan sulfate
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Glycosphingolipid biosynthesis - ganglio series
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Glycosphingolipid biosynthesis - globo and isoglobo series
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Glycosphingolipid biosynthesis - lacto and neolacto series
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Metabolic pathways
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mucin core 1 and core 2 O-glycosylation
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Mucin type O-glycan biosynthesis
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SYSTEMATIC NAME
IUBMB Comments
CMP-N-acetylneuraminate:beta-D-galactoside alpha-(2->3)-N-acetylneuraminyl-transferase
The acceptor is Galbeta1,3GalNAc-R, where R is H, a threonine or serine residue in a glycoprotein, or a glycolipid. Lactose can also act as acceptor. May be identical with EC 2.4.99.2 monosialoganglioside sialyltransferase.
CAS REGISTRY NUMBER
COMMENTARY hide
71124-51-1
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
isoform ST3GAL I/II
UniProt
Manually annotated by BRENDA team
ST3Gal I
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Manually annotated by BRENDA team
non-typeable, genes lic3A and lic3B
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Manually annotated by BRENDA team
C57BL/6 mice
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
strain JT-ISH-467
UniProt
Manually annotated by BRENDA team
strain JT-ISH-467
UniProt
Manually annotated by BRENDA team
strain JT-ISH-224, isolated from the gut of japanese barracuda
UniProt
Manually annotated by BRENDA team
isoform ST3GAL II
UniProt
Manually annotated by BRENDA team
strain JT-FAJ-16
UniProt
Manually annotated by BRENDA team
strain JT-FAJ-16
UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
metabolism
the production of ganglioside GD1a and sialyl paragloboside in castration-resistant prostate cancer cells is indirectly controlled by nuclear factor-kappaB, mainly by RelB, through the transcriptional regulation of isoform ST3Gal I; the production of ganglioside GD1a and sialyl paragloboside in castration-resistant prostate cancer cells is indirectly controlled by nuclear factor-kappaB, mainly by RelB, through the transcriptional regulation of isoform ST3Gal II; the production of ganglioside GD1a and sialyl paragloboside in castration-resistant prostate cancer cells is indirectly controlled by nuclear factor-kappaB, mainly by RelB, through the transcriptional regulation of isoform ST3Gal VI
physiological function
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
CMP + Galbeta(1->3)GalNAcbeta(1->3)Galalpha-O-Me
CMP-N-acetylneuraminate + NeuAcalpha(2->3)Galbeta(1->3)GalNAcbeta(1->3)Galalpha-O-Me
show the reaction diagram
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r
CMP + NeuAcalpha2,3Galbeta1,3GalNAcalpha-O-glycan
CMP-5-N-acetylneuraminate + Galbeta1,3GalNAcalpha-O-glycan
show the reaction diagram
CMP-5-N-acetylneuraminate + 2-O-MeGalbeta1,3GlcNAc
?
show the reaction diagram
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an efficient acceptor for alpha2,3(N)ST
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?
CMP-5-N-acetylneuraminate + 3-FGalbeta1,4GlcNAcbeta1,6(Galbeta1,3)GalNAcalpha-O-Bn
?
show the reaction diagram
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?
CMP-5-N-acetylneuraminate + 3-O-MeGalbeta1,4GlcNAcbeta1,6(Galbeta1,3)GalNAcalpha-O-Bn
?
show the reaction diagram
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?
CMP-5-N-acetylneuraminate + 4-FGalbeta1,4GlcNAcbeta1,6(Galbeta1,3)GalNAcalpha-O-Bn
?
show the reaction diagram
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?
CMP-5-N-acetylneuraminate + 4-O-MeGalbeta1,4GlcNAc
?
show the reaction diagram
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an efficient acceptor for alpha2,3(N)ST
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?
CMP-5-N-acetylneuraminate + 4-O-MeGalbeta1,4GlcNAcbeta1,6(Galbeta1,3)GalNAcalpha-O-Bn
?
show the reaction diagram
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?
CMP-5-N-acetylneuraminate + D-Fucbeta1,3GalNAcbeta1,3-Gal-alpha-O-Me
?
show the reaction diagram
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an efficient acceptor for alpha2,3(O)ST
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?
CMP-5-N-acetylneuraminate + Galbeta1,3GalNAcbeta1,3Galalpha-O-Me
?
show the reaction diagram
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i.e. Globo, an efficient acceptor for both alpha2,3(N)ST and alpha2,3(O)ST, structures containing sialyl, fucosyl, sulfo, methyl, or fluoro substituents
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?
CMP-5-N-acetylneuraminate + Galbeta1,4GlcNAcbeta1,6(3-FGalbeta1,3)GalNAcalpha-O-Bn
?
show the reaction diagram
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?
CMP-5-N-acetylneuraminate + Galbeta1,4GlcNAcbeta1,6(3-O-MeGalbeta1,3)GalNAcalpha-O-Bn
?
show the reaction diagram
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?
CMP-5-N-acetylneuraminate + Galbeta1,4GlcNAcbeta1,6(4-O-MeGalbeta1,3)GalNAcalpha-O-Bn
?
show the reaction diagram
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best substrate
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?
CMP-5-N-acetylneuraminate + Galbeta1,4GlcNAcbeta1,6(Galbeta1,3)GalNAcalpha-O-Bn
?
show the reaction diagram
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a mucin core 2 tetrasaccharide, structures containing sialyl, fucosyl, sulfo, methyl, or fluoro substituents
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?
CMP-N-acetyl-beta-neuraminate + Galbeta(1,3)(4-deoxy)GalNAcalphaOBn
?
show the reaction diagram
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effective acceptor for isoform ST3Gal-I
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CMP-N-acetyl-beta-neuraminate + Galbeta(1,3)GlcNAcbeta(1,3)lac-beta-4-nitrophenyl
?
show the reaction diagram
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less than 1% activity compared to Galbeta(1,3)(4-deoxy)GalNAcalphaOBn
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?
CMP-N-acetyl-beta-neuraminate + Galbeta(1,3)GlcNAcbeta(1,6)GalNAc-OBn
?
show the reaction diagram
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about 50% activity compared to Galbeta(1,3)(4-deoxy)GalNAcalphaOBn
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?
CMP-N-acetylneuraminate + 1D-chiro-inositol
CMP + 1D-2-O-(alpha-sialosyl)-chiro-inositol
show the reaction diagram
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15% activity compared to lactose
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?
CMP-N-acetylneuraminate + 2-nitrophenyl-betaGal
CMP + ?
show the reaction diagram
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?
CMP-N-acetylneuraminate + 3-(4-tetradecyl-1H-1,2,3-triazol-1-yl)propyl 4-O-beta-D-galactopyranosyl-beta-D-glucopyranoside
CMP + 3-(4-tetradecyl-1H-1,2,3-triazol-1-yl)propyl alpha-N-acetylneuraminyl-(2->3)-beta-D-galactosyl-(1->4)-beta-D-glucoside
show the reaction diagram
CMP-N-acetylneuraminate + 3-(4-tetradecyl-1H-1,2,3-triazol-1-yl)propyl beta-D-galactopyranoside
CMP + 3-(4-tetradecyl-1H-1,2,3-triazol-1-yl)propyl alpha-N-acetylneuraminyl-(2->3)-beta-D-galactopyranoside
show the reaction diagram
CMP-N-acetylneuraminate + 3-(4-tetradecyl-1H-1,2,3-triazol-1-yl)propyl beta-D-galactosyl-(1->4)-beta-D-glucoside
CMP + 3-(4-tetradecyl-1H-1,2,3-triazol-1-yl)propyl alpha-N-acetylneuraminyl-(2->3)-beta-D-galactosyl-(1->4)-beta-D-glucoside
show the reaction diagram
CMP-N-acetylneuraminate + 3-deoxy-Galbeta1-3GalNAcalpha-benzyl
?
show the reaction diagram
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?
CMP-N-acetylneuraminate + 4-deoxy-Galbeta1-3GalNAcalpha-benzyl
CMP + NeuAcalpha2-3(4-deoxy)-Galbeta1-3GalNAcalpha-benzyl
show the reaction diagram
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?
CMP-N-acetylneuraminate + 4-methylumbelliferyl 4-O-beta-D-galactopyranosyl-beta-D-glucopyranoside
CMP + 4-methylumbelliferyl alpha-N-acetylneuraminyl-(2->3)-beta-D-galactosyl-(1->4)-beta-D-glucoside
show the reaction diagram
CMP-N-acetylneuraminate + 4-methylumbelliferyl 4-O-beta-D-galactosyl-beta-D-glucoside
CMP + 4-methylumbelliferyl alpha-N-acetylneuraminyl-(2->3)-beta-D-galactosyl-(1->4)-beta-D-glucoside
show the reaction diagram
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best substrate, about 37% conversion
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CMP-N-acetylneuraminate + 4-methylumbelliferyl lactoside
CMP + ?
show the reaction diagram
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preferred acceptor
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?
CMP-N-acetylneuraminate + 4-methylumbelliferyl Lewisx
CMP + ?
show the reaction diagram
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?
CMP-N-acetylneuraminate + 6-deoxy-Galbeta1-3GalNAcalpha-benzyl
CMP + NeuAcalpha2-3(6-deoxy)-Galbeta1-3GalNAcalpha-benzyl
show the reaction diagram
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?
CMP-N-acetylneuraminate + Ala-Pro-(Galbeta1-3GalNAcalpha)-Ser-Ser-Ser
CMP + NeuAcalpha2-3(Galbeta1-3GalNAcalpha)-Ser-Ser-Ser
show the reaction diagram
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?
CMP-N-acetylneuraminate + Ala-Pro-(Galbeta1-3GalNAcalpha)-Thr-Ser-Ser
CMP + NeuAcalpha2-3(Galbeta1-3GalNAcalpha)-Thr-Ser-Ser
show the reaction diagram
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?
CMP-N-acetylneuraminate + alpha-D-Manp-(1->6)-D-Manp
CMP + alpha-D-mannopyranosyl-(1->6)-beta-D-mannopyranosyl (6R)-5-(acetylamino)-3,5-dideoxy-6-[(1R,2R)-1,2,3-trihydroxypropyl]-beta-L-threo-hex-2-ulopyranosidonic acid
show the reaction diagram
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26% yield
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?
CMP-N-acetylneuraminate + alpha-methyl-galactopyranoside
CMP + ?
show the reaction diagram
823% of the activity with acceptor Gal-beta-1,4-Glc
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?
CMP-N-acetylneuraminate + beta-D-galactosyl-(1->3)-N-acetyl-alpha-D-galactosaminyl-R
CMP + alpha-N-acetylneuraminyl-(2->3)-beta-D-galactosyl-(1->3)-N-acetyl-alpha-D-galactosaminyl-R
show the reaction diagram
CMP-N-acetylneuraminate + beta-D-galactosyl-(1->3)-N-acetyl-alpha-D-galactosaminyl-Ser/Thr
CMP + alpha-N-acetylneuraminyl-(2->3)-beta-D-galactosyl-(1->3)-N-acetyl-alpha-D-galactosaminyl-Ser/Thr
show the reaction diagram
CMP-N-acetylneuraminate + beta-D-galactosyl-(1->4)-alpha-D-glucosyl-R
CMP + alpha-N-acetylneuraminyl-(2->3)-beta-D-glucosyl-(1->4)-R
show the reaction diagram
CMP-N-acetylneuraminate + beta-D-galactosyl-1,3-N-acetyl-alpha-D-galactosaminyl-R
?
show the reaction diagram
CMP-N-acetylneuraminate + beta-D-galactosyl-1,3-N-acetyl-alpha-D-galactosaminyl-R
CMP + alpha-N-acetylneuraminyl-2,3-beta-D-galactosyl-1,3-N-acetyl-alpha-D-galactosaminyl-R
show the reaction diagram
CMP-N-acetylneuraminate + beta-D-galactosyl-1,4-N-acetyl-beta-D-glucosamine
CMP + alpha-N-acetylneuraminyl-2,3-beta-D-galactosyl-1,4-N-acetyl-beta-D-glucosamine
show the reaction diagram
CMP-N-acetylneuraminate + beta-D-galactosyl-O-R
CMP + alpha-N-acetylneuraminyl-2,3-beta-D-galactosyl-O-R
show the reaction diagram
CMP-N-acetylneuraminate + beta-methyl-galactopyranoside
CMP + ?
show the reaction diagram
343% of the activity with acceptor Gal-beta-1,4-Glc
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?
CMP-N-acetylneuraminate + D-mannose
CMP + beta-D-mannopyranosyl (6R)-5-(acetylamino)-3,5-dideoxy-6-[(1R,2R)-1,2,3-trihydroxypropyl]-beta-L-threo-hex-2-ulopyranosidonic acid
show the reaction diagram
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18% yield
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?
CMP-N-acetylneuraminate + epi-inositol
CMP + 1L-3-O-(alpha-sialosyl)-epi-inositol
show the reaction diagram
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18% activity compared to lactose
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?
CMP-N-acetylneuraminate + Fucalpha1,2-Galbeta1,4-Glc
CMP + ?
show the reaction diagram
52% of the activity with acceptor Gal-beta-1,4-Glc
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?
CMP-N-acetylneuraminate + fucosylated Lewisx
CMP + ?
show the reaction diagram
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?
CMP-N-acetylneuraminate + Gal-beta-1,3-GlcNAc-beta-OMe
CMP + ?
show the reaction diagram
CMP-N-acetylneuraminate + Gal-beta-1,4-Glc
CMP + ?
show the reaction diagram
CMP-N-acetylneuraminate + Gal-beta-1,4-GlcNAc
CMP + ?
show the reaction diagram
CMP-N-acetylneuraminate + Galalpha-1,3-Galalpha-OMe
CMP + ?
show the reaction diagram
528% of the activity with acceptor Gal-beta-1,4-Glc
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?
CMP-N-acetylneuraminate + Galalpha1-4Galbeta1-4Glc-pyridylamine
CMP + ?
show the reaction diagram
CMP-N-acetylneuraminate + Galbeta(1-3)GalNAcOBzl
CMP + NeuAcalpha(2-3)Galbeta(1-3)GalNAcOBzl
show the reaction diagram
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-
-
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?
CMP-N-acetylneuraminate + Galbeta1,3-Galbeta-OMe
CMP + ?
show the reaction diagram
331% of the activity with acceptor Gal-beta-1,4-Glc
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?
CMP-N-acetylneuraminate + Galbeta1-3(2-deoxy)Galalpha-benzyl
CMP + NeuAcalpha2-3Galbeta1-3(2-deoxy)Galalpha-benzyl
show the reaction diagram
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?
CMP-N-acetylneuraminate + Galbeta1-3(4-deoxy)GalNAcalpha-benzyl
CMP + NeuAcalpha2-3Galbeta1-3(4-deoxy)GalNAcalpha-benzyl
show the reaction diagram
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?
CMP-N-acetylneuraminate + Galbeta1-3(6-deoxy)GalNAcalpha-benzyl
CMP + NeuAcalpha2-3Galbeta1-3(6-deoxy)GalNAcalpha-benzyl
show the reaction diagram
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?
CMP-N-acetylneuraminate + Galbeta1-3(6-O-Me)GalNAcalpha-benzyl
CMP + NeuAcalpha2-4Galbeta1-3(6-O-Me)GalNAcalpha-benzyl
show the reaction diagram
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-
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?
CMP-N-acetylneuraminate + Galbeta1-3(6-sulfo)GalNAcalpha-O-allyl
CMP + NeuAcalpha2-4Galbeta1-3(6-sulfo)GalNAcalpha-O-allyl
show the reaction diagram
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?
CMP-N-acetylneuraminate + Galbeta1-3(Fucalpha1-4)GlcNAcbeta1-3Galbeta1-4Glc-pyridylamine
CMP + ?
show the reaction diagram
CMP-N-acetylneuraminate + Galbeta1-3(NeuAcalpha2,6)GalNAcalpha-O-benzyl
CMP + NeuAcalpha2-4Galbeta1-3(NeuAcalpha2,6)GalNAcalpha-O-benzyl
show the reaction diagram
CMP-N-acetylneuraminate + Galbeta1-3GalNAc
CMP + NeuAcalpha2-3Galbeta1-3GalNAc
show the reaction diagram
CMP-N-acetylneuraminate + Galbeta1-3GalNAcalpha-8-methoxycarbonyl-octyl
CMP + NeuAcalpha2-3Galbeta1-3GalNAcalpha-8-methoxycarbonyl-octyl
show the reaction diagram
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-
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?
CMP-N-acetylneuraminate + Galbeta1-3GalNAcalpha-antifreeze glycoprotein
CMP + NeuAcalpha2-3Galbeta1-3GalNAcalpha-antifreeze glycoprotein
show the reaction diagram
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?
CMP-N-acetylneuraminate + Galbeta1-3GalNAcalpha-O-allyl
CMP + NeuAcalpha2-4Galbeta1-3GalNAcalpha-O-allyl
show the reaction diagram
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-
-
-
?
CMP-N-acetylneuraminate + Galbeta1-3GalNAcalpha-O-benzyl
CMP + NeuAcalpha2-4Galbeta1-3GalNAcalpha-O-benzyl
show the reaction diagram
CMP-N-acetylneuraminate + Galbeta1-3GalNAcalpha-o-nitrophenyl
CMP + NeuAcalpha2-3Galbeta1-3GalNAcalpha-o-nitrophenyl
show the reaction diagram
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-
-
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?
CMP-N-acetylneuraminate + Galbeta1-3GalNAcalpha-p-nitrophenyl
CMP + NeuAcalpha2-3Galbeta1-3GalNAcalpha-p-nitrophenyl
show the reaction diagram
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-
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?
CMP-N-acetylneuraminate + Galbeta1-3GalNAcalpha-phenyl
CMP + NeuAcalpha2-3Galbeta1-3GalNAcalpha-phenyl
show the reaction diagram
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-
-
-
?
CMP-N-acetylneuraminate + Galbeta1-3GalNAcalpha-Ser
CMP + NeuAcalpha2-3Galbeta1-3GalNAcalpha-Ser
show the reaction diagram
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-
-
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?
CMP-N-acetylneuraminate + Galbeta1-3GalNAcalpha-Thr(NAc)OMe
CMP + ?
show the reaction diagram
CMP-N-acetylneuraminate + Galbeta1-3GalNAcbeta1-4Galbeta1-4Glc-pyridylamine
CMP + ?
show the reaction diagram
CMP-N-acetylneuraminate + Galbeta1-3GalNAcbeta1-4[Neu5Acalpha2-3]Galalpha1-4Glcbeta1
CMP + ?
show the reaction diagram
CMP-N-acetylneuraminate + Galbeta1-3GlcNAc
CMP + NeuAcalpha2-3Galbeta1-3GlcNAc
show the reaction diagram
CMP-N-acetylneuraminate + Galbeta1-3GlcNAcbeta-CH2-CH2-N3
CMP + ?
show the reaction diagram
CMP-N-acetylneuraminate + Galbeta1-3GlcNAcbeta1-3Galbeta1-4Glc
CMP + NeuAcalpha2-3Galbeta1-3GlcNAcbeta1-3Galbeta1-4Glc
show the reaction diagram
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weak, i.e. lactotetraose
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?
CMP-N-acetylneuraminate + Galbeta1-3GlcNAcbeta1-3Galbeta1-4Glc-pyridylamine
CMP + ?
show the reaction diagram
CMP-N-acetylneuraminate + Galbeta1-3[6-O-(4,4-azo)pentyl]GalNAcalpha-benzyl
CMP + neuAcalpha2-3Galbeta1-3[6-O-(4,4-azo)pentyl]GalNAcalpha-benzyl
show the reaction diagram
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-
-
-
?
CMP-N-acetylneuraminate + Galbeta1-4(Fucalpha1-3)GlcNAcbeta1-3Galbeta1-4Glc-pyridylamine
CMP + ?
show the reaction diagram
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-
-
?
CMP-N-acetylneuraminate + Galbeta1-4Glc
CMP + NeuAcalpha2-3Galbeta1-4Glc
show the reaction diagram
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weak acceptor
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?
CMP-N-acetylneuraminate + Galbeta1-4GlcNAc
CMP + NeuAcalpha2-3Galbeta1-4GlcNAc
show the reaction diagram
CMP-N-acetylneuraminate + Galbeta1-4GlcNAcbeta1-3Galbeta1-4Glc-pyridylamine
CMP + ?
show the reaction diagram
-
-
-
?
CMP-N-acetylneuraminate + Galbeta1-6GlcNAc
CMP + NeuAcalpha2-3Galbeta1-6GlcNAc
show the reaction diagram
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weak acceptor for enzyme B
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?
CMP-N-acetylneuraminate + GalNAcalpha1-3GalNAcbeta1-3Galalpha1-4Galbeta1-4Glc-pyridylamine
CMP + ?
show the reaction diagram
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-
-
?
CMP-N-acetylneuraminate + GalNAcbeta1-4Galbeta1-4Glc-pyridylamine
CMP + ?
show the reaction diagram
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-
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?
CMP-N-acetylneuraminate + GlcNAcbeta1-6(D-Fucbeta1-3)GalNAcalpha-benzyl
CMP + NeuAcalpha2-3 GlcNAcbeta1-6(D-Fucbeta1-3)GalNAcalpha-benzyl
show the reaction diagram
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-
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?
CMP-N-acetylneuraminate + GlcNAcbeta1-6(Galbeta1-3)GalNAcalpha-benzyl
CMP + NeuAcalpha2-3 GlcNAcbeta1-6(Galbeta1-3)GalNAcalpha-benzyl
show the reaction diagram
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-
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?
CMP-N-acetylneuraminate + GlcNAcbeta1-6(GlcNAcbeta1-6Galbeta1-3)GalNAcalpha-benzyl
CMP + NeuAcalpha2-3GlcNAcbeta1-6(GlcNAcbeta1-6Galbeta1-3)GalNAcalpha-benzyl
show the reaction diagram
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-
-
-
?
CMP-N-acetylneuraminate + LacNAcbeta-Pro-triazole-C14
CMP + ?
show the reaction diagram
CMP-N-acetylneuraminate + lactose
?
show the reaction diagram
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100% activity
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-
?
CMP-N-acetylneuraminate + lactose
CMP + 3'-siallyllactose
show the reaction diagram
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-
-
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?
CMP-N-acetylneuraminate + lactose
CMP + 3'-sialyllactose
show the reaction diagram
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-
-
?
CMP-N-acetylneuraminate + lactose
CMP + ?
show the reaction diagram
-
-
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?
CMP-N-acetylneuraminate + lactose
CMP + NeuAcalpha(2->3)Galbeta(1->4)Glc
show the reaction diagram
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-
-
-
?
CMP-N-acetylneuraminate + methyl 2-([4-[(3-[[3-O-(beta-D-galactopyranosyl)-beta-D-glucopyranosyl]oxy]propyl)amino]-4-oxobutanoyl]amino)benzoate
CMP + 3-[(4-[[2-(methoxycarbonyl)phenyl]amino]-4-oxobutanoyl)amino]propyl alpha-N-acetylneuraminyl-(2->3)-beta-D-galactopyranosyl-(1->4)-beta-D-glucopyranoside
show the reaction diagram
CMP-N-acetylneuraminate + methyl 2-([4-[(3-[[4-O-(beta-D-galactopyranosyl)-beta-D-glucopyranosyl]oxy]propyl)amino]-4-oxobutanoyl]amino)benzoate
CMP + 3-[(4-[[2-(methoxycarbonyl)phenyl]amino]-4-oxobutanoyl)amino]propyl alpha-N-acetylneuraminyl-(2->3)-beta-D-galactopyranosyl-(1->4)-beta-D-glucopyranoside
show the reaction diagram
CMP-N-acetylneuraminate + methyl 2-([4-[(3-[[4-O-(beta-D-galactopyranosyl)-beta-D-N-acetylglucosaminopyranosyl]oxy]propyl)amino]-4-oxobutanoyl]amino)benzoate
CMP + 3-[(4-[[2-(methoxycarbonyl)phenyl]amino]-4-oxobutanoyl)amino]propyl alpha-N-acetylneuraminyl-(2->3)-beta-D-galactopyranosyl-(1->4)-beta-D-N-acetylglucosaminopyranoside
show the reaction diagram
34.4% conversion after 10 min incubation, 73.9% conversion after 4 h incubation
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-
?
CMP-N-acetylneuraminate + methyl-alpha-D-galactopyranoside
CMP + ?
show the reaction diagram
CMP-N-acetylneuraminate + methyl-alpha-D-glucopyranoside
CMP + ?
show the reaction diagram
CMP-N-acetylneuraminate + methyl-alpha-L-fucopyranoside
CMP + ?
show the reaction diagram
49% of the activity with Gal-beta-1,4-Glc
-
-
?
CMP-N-acetylneuraminate + methyl-beta-D-galactopyranoside
CMP + ?
show the reaction diagram
CMP-N-acetylneuraminate + methyl-beta-D-glucopyranoside
CMP + ?
show the reaction diagram
CMP-N-acetylneuraminate + methyl-beta-D-mannopyranoside
CMP + ?
show the reaction diagram
CMP-N-acetylneuraminate + methyl-beta-L-fucopyranoside
CMP + ?
show the reaction diagram
42% of the activity with Gal-beta-1,4-Glc
-
-
?
CMP-N-acetylneuraminate + methyl-D-galactopyranosyl-beta-1,3-N-acetylglucosamine
CMP + ?
show the reaction diagram
124% of the activity with lactose
-
-
?
CMP-N-acetylneuraminate + muco-inositol
?
show the reaction diagram
-
1.7% activity compared to lactose
-
-
?
CMP-N-acetylneuraminate + myo-inositol
?
show the reaction diagram
-
4.5% activity compared to lactose
-
-
?
CMP-N-acetylneuraminate + N-acetyl-D-galactosamine
CMP + ?
show the reaction diagram
CMP-N-acetylneuraminate + N-acetyl-D-glucosamine
CMP + ?
show the reaction diagram
40% of the activity with Gal-beta-1,4-Glc
-
-
?
CMP-N-acetylneuraminate + N-acetyl-lactosamine
CMP + ?
show the reaction diagram
-
-
-
?
CMP-N-acetylneuraminate + N-acetylgalactosamine
CMP + ?
show the reaction diagram
58% of the activity with lactose
-
-
?
CMP-N-acetylneuraminate + N-acetylglucosamine
CMP + ?
show the reaction diagram
55% of the activity with lactose
-
-
?
CMP-N-acetylneuraminate + N-acetyllactosamine
CMP + ?
show the reaction diagram
127% of the activity with lactose
-
-
?
CMP-Neu5Ac + Galbeta-1,4-Glc-6-(5-fluorescein-carboxamido)-hexanoic acid succinimidyl ester
?
show the reaction diagram
-
-
-
-
?
CMP-NeuAc + Galbeta(1-3)GalNAc-O-octyl
CMP + NeuAcalpha(2-3)Galbeta(1-3)GalNAc-O-octyl
show the reaction diagram
-
-
-
-
?
CMP-NeuAc + Galbeta(1-3)[Galbeta(1-3)NeuAcalpha(2-6)]GalNAc-O-octyl
CMP + NeuAcalpha(2-3)Galbeta(1-3)[Galbeta(1-3)NeuAcalpha(2-6)]GalNAc-O-octyl
show the reaction diagram
-
-
-
-
?
CMP-NeuAc + Galbeta(1-3)[NeuAcalpha(2-6)]GalNAc-O-octyl
CMP + NeuAcalpha(2-3)Galbeta(1-3)[NeuAcalpha(2-6)]GalNAc-O-octyl
show the reaction diagram
-
-
-
-
?
UMP + CMP-5-N-acetylneuraminate
UMP-5-N-acetylneuraminate + CMP
show the reaction diagram
additional information
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
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->3)-N-acetyl-alpha-D-galactosaminyl-R
CMP + alpha-N-acetylneuraminyl-(2->3)-beta-D-galactosyl-(1->3)-N-acetyl-alpha-D-galactosaminyl-R
show the reaction diagram
CMP-N-acetylneuraminate + beta-D-galactosyl-(1->4)-alpha-D-glucosyl-R
CMP + alpha-N-acetylneuraminyl-(2->3)-beta-D-glucosyl-(1->4)-R
show the reaction diagram
CMP-N-acetylneuraminate + beta-D-galactosyl-1,3-N-acetyl-alpha-D-galactosaminyl-R
?
show the reaction diagram
CMP-N-acetylneuraminate + beta-D-galactosyl-O-R
CMP + alpha-N-acetylneuraminyl-2,3-beta-D-galactosyl-O-R
show the reaction diagram
-
-
-
-
?
CMP-N-acetylneuraminate + fucosylated Lewisx
CMP + ?
show the reaction diagram
-
-
-
-
?
additional information
?
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Mg2+
-
about 220% activity at 10 mM
additional information
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2alpha-hydroxystachybotrylactone
-
IC50: 0.1684 mg/ml
3-deoxy-Galbeta1-3GalNAcalpha-benzyl
-
-
3-O-sulfoGalbeta1,4GlcNAcbeta1,6(Galbeta1,3)GalNAcalpha-O-benzyl
-
inhibitory to reverse sialylation, producing CMP-5-N-acetylneuraminate
5'-CDP
-
inhibitory to direct sialylation, using CMP-5-N-acetylneuraminate as a substrate, not inhibitory to reverse sialylation, producing CMP-5-N-acetylneuraminate
asialofetuin
-
inhibits reaction with asialoGM1 and Galbeta1-3GalNAc as acceptor
-
asialoGM1
-
inhibits reaction with Galbeta1-3GalNAc, asialofetuin or GM1 as acceptor
beta-D-galactosyl-1,3-N-acetylgalactosylamide
-
with porcine submaxillary asialomucin as substrate
CDP
-
less effective than CTP
Galbeta1-3(6-deoxy)GalNAcalpha-benzyl
-
-
Galbeta1-3GalNAc
-
inhibits reaction with asialoGM1 as acceptor
GM1
-
inhibits reaction with asialoGM1
lysophosphatidylglycerol
-
enzyme forms A and B
lysophosphatidylserine
-
enzyme form A
N-bromosuccinimide
strong inhibitor, complete inhibition at 3 mM
N-ethylmaleimide
-
octylglucoside
-
irreversible, at higher concentrations
Sodium citrate
-
inhibitory to direct sialylation, using CMP-5-N-acetylneuraminate as a substrate, not inhibitory to reverse sialylation, producing CMP-5-N-acetylneuraminate
stachybotrydial
-
IC50: 0.0067 mg/ml
stachybotrylactone
-
IC50: 0.0302 mg/ml
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
lysophosphatidylcholine
-
activation, enzyme form A, not B
phospholipid/octylglucoside liposomes
-
incorporation into phospholipid/octylglucoside liposomes activates enzyme form A
-
Triton X-100
additional information
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
4.1
3-(4-tetradecyl-1H-1,2,3-triazol-1-yl)propyl 4-O-beta-D-galactopyranosyl-beta-D-glucopyranoside
-
in Tris-HCl buffer (200 mM, pH 8.0), at 37°C
0.4 - 0.5
4-deoxy-Galbeta1-3GalNAcalpha-benzyl
1.2
4-methyl-2-oxo-2H-chromen-7-yl 4-O-beta-D-galactopyranosyl-beta-D-glucopyranoside
-
in Tris-HCl buffer (200 mM, pH 8.0), at 37°C
0.54 - 1.4
4-methylumbelliferyl 4-O-beta-D-galactosyl-beta-D-glucoside
3.3
4-methylumbelliferyl-Lewisx
-
in Tris-HCl buffer (200 mM, pH 8.0), at 37°C
0.4 - 3.4
6-deoxy-Galbeta1-3GalNAcalpha-benzyl
0.18
alpha-methyl-galactopyranoside
pH 5.0, 30°C
0.37 - 0.46
asialo-GM1
0.049 - 0.52
asialofetuin
-
0.56 - 1.25
asialoGM1
0.32 - 0.37
beta-D-galactosyl-1,3-N-acetylgalactosylamide
0.2
beta-methyl-galactopyranoside
pH 5.0, 30°C
0.00434 - 4.09
CMP-N-acetylneuraminate
0.14 - 1.7
Gal-beta-1,4-Glc
0.11 - 0.5
Galbeta1,3GalNAc
1.3 - 2.7
Galbeta1-3(2-deoxy)Galalpha-benzyl
0.4 - 1.3
Galbeta1-3(4-deoxy)GalNAcalpha-benzyl
1.3 - 1.6
Galbeta1-3(6-deoxy)GalNAcalpha-benzyl
0.105
Galbeta1-3(6-sulfo)GalNAcalpha-O-allyl
-
-
0.42
Galbeta1-3(NeuAcalpha2,6)GalNAcalpha-O-benzyl
-
-
0.05 - 0.45
Galbeta1-3GalNAc
0.35 - 0.39
Galbeta1-3GalNAc-Thr antifreeze glycoprotein
-
0.03 - 0.4
Galbeta1-3GalNAcalpha-benzyl
0.2
Galbeta1-3GalNACalpha-O-allyl
-
-
-
0.05
Galbeta1-3GalNAcalpha-O-allyl/acrylamide copolymer
-
-
-
0.018 - 0.023
Galbeta1-3GalNAcalpha-O-benzyl
4.7 - 85
Galbeta1-3GlcNAc
15 - 27
Galbeta1-3GlcNAcbeta1-3Galbeta1-4Glc
0.5
Galbeta1-3[6-O-(4,4-azo)pentyl]GalNAcalpha-benzyl
-
enzyme from acute myeloid leukemia
130 - 180
Galbeta1-4Glc
42
Galbeta1-4GlcNAc
-
enzyme form B
29
Galbeta1-6GlcNAc
-
enzyme form A
0.15 - 1
GD1b
0.45 - 1.67
GM1
1.64 - 5
lactose
14
methyl 2-([4-[(3-[[3-O-(beta-D-galactopyranosyl)-beta-D-glucopyranosyl]oxy]propyl)amino]-4-oxobutanoyl]amino)benzoate
at 37°C in Tris-HCl (200 mM, pH 7.5)
4.9 - 28
methyl 2-([4-[(3-[[4-O-(beta-D-galactopyranosyl)-beta-D-glucopyranosyl]oxy]propyl)amino]-4-oxobutanoyl]amino)benzoate
0.54
methyl-alpha-D-galactopyranoside
-
pH 6.0, 25°C
1.3
methyl-beta-D-galactopyranoside
-
pH 6.0, 25°C
2.5
N-acetyl-lactosamine
-
pH 6.0, 25°C
additional information
additional information
-
influence of liposome incorporation on the Km-value
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.2
3-(4-tetradecyl-1H-1,2,3-triazol-1-yl)propyl 4-O-beta-D-galactopyranosyl-beta-D-glucopyranoside
Pasteurella multocida
-
in Tris-HCl buffer (200 mM, pH 8.0), at 37°C
0.53
4-methyl-2-oxo-2H-chromen-7-yl 4-O-beta-D-galactopyranosyl-beta-D-glucopyranoside
myxoma virus
-
in Tris-HCl buffer (200 mM, pH 8.0), at 37°C
2 - 47
4-methylumbelliferyl 4-O-beta-D-galactosyl-beta-D-glucoside
0.55
4-methylumbelliferyl-Lewisx
myxoma virus
-
in Tris-HCl buffer (200 mM, pH 8.0), at 37°C
0.078 - 44.6
CMP-N-acetylneuraminate
53.2 - 89.7
lactose
0.25
methyl 2-([4-[(3-[[3-O-(beta-D-galactopyranosyl)-beta-D-glucopyranosyl]oxy]propyl)amino]-4-oxobutanoyl]amino)benzoate
Pasteurella multocida
Q9CLP3
at 37°C in Tris-HCl (200 mM, pH 7.5)
0.132 - 0.75
methyl 2-([4-[(3-[[4-O-(beta-D-galactopyranosyl)-beta-D-glucopyranosyl]oxy]propyl)amino]-4-oxobutanoyl]amino)benzoate
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.048
3-(4-tetradecyl-1H-1,2,3-triazol-1-yl)propyl 4-O-beta-D-galactopyranosyl-beta-D-glucopyranoside
Pasteurella multocida
-
in Tris-HCl buffer (200 mM, pH 8.0), at 37°C
42278
0.47
4-methyl-2-oxo-2H-chromen-7-yl 4-O-beta-D-galactopyranosyl-beta-D-glucopyranoside
myxoma virus
-
in Tris-HCl buffer (200 mM, pH 8.0), at 37°C
28942
28 - 39
4-methylumbelliferyl 4-O-beta-D-galactosyl-beta-D-glucoside
8959
0.025
4-methylumbelliferyl-Lewisx
myxoma virus
-
in Tris-HCl buffer (200 mM, pH 8.0), at 37°C
28943
0.068 - 140
CMP-N-acetylneuraminate
180
0.74 - 5.6
lactose
114
0.017
methyl 2-([4-[(3-[[3-O-(beta-D-galactopyranosyl)-beta-D-glucopyranosyl]oxy]propyl)amino]-4-oxobutanoyl]amino)benzoate
Pasteurella multocida
Q9CLP3
at 37°C in Tris-HCl (200 mM, pH 7.5)
42279
0.005 - 0.15
methyl 2-([4-[(3-[[4-O-(beta-D-galactopyranosyl)-beta-D-glucopyranosyl]oxy]propyl)amino]-4-oxobutanoyl]amino)benzoate
19691
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.8 - 3.1
3-deoxy-Galbeta1-3GalNAcalpha-benzyl
0.07 - 0.08
asialofetuin
-
0.11 - 1.29
asialoGM1
0.011
ATP
-
-
0.015
CMP
-
-
0.00015 - 0.001
CTP
0.15
Galbeta1-3GalNAc
-
reaction with asialoGM1 as acceptor, enzyme form ST3GalA.1
0.51
GM1
-
reaction with asialoGM1 as acceptor, enzyme form ST3GalA.2
0.0038
GTP
-
-
0.0007
UTP
-
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.006
-
recombinant Lic3B, alpha-2,8-sialyltransferase activity
0.1
-
recombinant Lic3B, alpha-2,3-sialyltransferase activity
0.116
-
wild type enzyme, at pH 7.5 and 37°C
0.241
-
recombinant Lic3A, alpha-2,3-sialyltransferase activity
0.457
-
pH 6.0, 25°C
10.6
-
-
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.5 - 6.5
-
-
5.5 - 8.5
-
-
6 - 6.5
-
-
6.5 - 9
activity decreases dramatically when pH is below 6.0 or reaches 10.0
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4.5 - 7.5
-
pH 4.5: about 20% of maximal activity, pH 7.5: about 55% of maximal activity
4.5 - 10
-
when methyl 2-([4-[(3-[[4-O-(beta-D-galactopyranosyl)-beta-D-glucopyranosyl]oxy]propyl)amino]-4-oxobutanoyl]amino)benzoate is used as the acceptor, the pH of the buffer in the range of 4.5-9.0 does not change the alpha2-3-sialyltransferase activity of the enzyme significantly. In comparison, when 3-(4-tetradecyl-1H-1,2,3-triazol-1-yl)propyl 4-O-beta-D-galactopyranosyl-beta-D-glucopyranoside is used as the acceptor, the optimal pH range is 5.0-8.0 and the alpha2-3-sialyltransferase activity of the enzyme decreases modestly at pH 4.5 and 9.0. Low activity is found at pH 10.0 and no significant activity is found at pH 4.0
4.8 - 6.4
-
reverse sialylation, producing CMP-5-N-acetylneuraminate
5.2 - 7.2
-
direct sialylation, using CMP-5-N-acetylneuraminate as a substrate
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
enzyme activity is significantly increased in patients with chronic myelogenous leukemia and acute myeloid leukemia
Manually annotated by BRENDA team
-
type 2 mRNA, type 1 mRNA is not detected
Manually annotated by BRENDA team
-
type 2 mRNA, type 1 mRNA is not detected
Manually annotated by BRENDA team
-
recombinant alpha2,3(O)STand alpha2,3(N)ST
Manually annotated by BRENDA team
-
na-EAT cells are not adherent nor grow in tissue culture, aEAT cells are selected to grow in tissue culture and adhere to extracellular matrices
Manually annotated by BRENDA team
-
slightly expressed in hepatoma and highly expressed in the surrounding tissue
Manually annotated by BRENDA team
-
type 2 mRNA, type 1 mRNA is not detected
Manually annotated by BRENDA team
-
T-lymphocytes, Epstein-Barr virus immortalized B-lymphocytes
Manually annotated by BRENDA team
-
high expression
Manually annotated by BRENDA team
-
type 1 and type 2 mRNA (differ only in 5'-untranslated region)
Manually annotated by BRENDA team
-
type 1 and type 2 mRNA (differ only in 5'-untranslated region)
Manually annotated by BRENDA team
-
type 1 and type 2 mRNA (differ only in 5'-untranslated region)
Manually annotated by BRENDA team
-
type 1 and type 2 mRNA (differ only in 5'-untranslated region)
Manually annotated by BRENDA team
-
ST3GalI gene is strongly expressed, ST3GalII gene is weakly expressed
Manually annotated by BRENDA team
-
expresses little ST3Gal III protein
Manually annotated by BRENDA team
-
type 1 and type 2 mRNA (differ only in 5'-untranslated region)
Manually annotated by BRENDA team
-
type 1 and type 2 mRNA (differ only in 5'-untranslated region)
Manually annotated by BRENDA team
-
toxic and nontoxic
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
a Golgi type II transmembrane glycosyltransferase; a Golgi type II transmembrane glycosyltransferase
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
about 15% of total activity, presumably enzyme form B
-
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
33000
x * 33000, SDS-PAGE
43921
x * 43921, MALDI-TOF of truncated enzyme with N-terminal Lys2 to Cys22 deletion
43995
x * 44027, calculated, x * 43995, MALDI-TOF, x * 40000, SDS-PAGE
44000
-
enzyme form B, sucrose density gradient centrifugation
44027
x * 44027, calculated, x * 43995, MALDI-TOF, x * 40000, SDS-PAGE
45026
-
x * 40000, SDS-PAGE, x * 45026, MALDI-TOF
72000
-
x * 72000, recombinant enzyme fused with N-terminal maltose binding protein, SDS-PAGE
72500
-
x * 72500, recombinant enzyme fused with N-terminal maltose binding protein, calculated from amino acid sequence
75000
-
x * 75000, His-tagged and maltose-binding protein-fused recombinant enzyme, SDS-PAGE
79500
-
x * 79500, His-tagged and maltose-binding protein-fused recombinant enzyme, calculated from amino acid sequence
220000
-
enzyme form A, gel filtration
additional information
-
enzyme form A and B are noninterconverting
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homotetramer
additional information
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
glycoprotein
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
purified dialyzed recombinant truncated enzyme DELTA24PmST1 alone or in a binary complex with CMP-N-acetylneuraminate, hanging drop vapor diffusion method, 0.003 ml of 10 mg/ml protein in 20 mM Tris-HCl buffer, pH 7.5, is mixed with 0.003 ml reservoir solution containing 26% PEG 3350, 100 mM HEPES, pH 7.5, 100 mM NaCl, and 0.4% Triton X-100, with or without 2 mM CMP-Neu5Ac, 2 weeks, X-ray diffraction structure determination and analysis at 1.65-2.0 A resolution
-
N-terminal truncated form of recombinant 2-24alpha2,3-sialyltransferase (DELTANpp23ST) in complex with CMP, by the hanging-drop vapor diffusion method at 20°C, to 2.0 A resolution. DELTANpp23ST consists of two separate Rossmann nucleotide-binding domains, domains 1 (39-224) and 2 (225-409) which form the glycosyltransferase-B structure. CMP is located in a deep cleft between domains 1 and 2. Crystal belongs to space group P1 with unit cell parameters a = 54.43 A, b = 57.83 A, c = 59.25 A, alphaa = 90.06°, beta = 106.76°, gamma = 103.20°. Broad substrate specificity may be attributed to the wider entrance of the acceptor substrate binding site
-
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6 - 6.5
-
maximal stability
636800
ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Acetone
-
in15%, 20%, and 25% of acetone, the enzyme retains its activities in an h but not after that
acetonitrile
-
in 10%, 15%, and 20% of acetonitrile, the enzyme retains its activities in an h but not after that
Ethanol
-
20% and 25% of ethanol, the enzyme retains its activities in an h but not after that
Methanol
-
in 25% of methanol, the enzyme retains its activities in an h but not after that
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, concentrated enzyme preparation in 50% v/v glycerol, stable for more than 6 months
-
the enzyme remains active after 3 months of storage in 10% (v/v) glycerol and 25 mM Tris-HCl (pH 7.5)
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
amylose column chromatography
-
chelating Sepharose column chromatography; HisTrap column chromatography
-
N-terminal truncated form of recombinant alpha2,3-sialyltransferase
-
Ni-NTA column chromatography
-
Ni2+-NTA column chromatography
Ni2+-NTA column chromatography, gel filtration
-
recombinant enzyme
recombinant fusion protein
-
recombinant maltose binding protein-fusion protein Lic3B from Escherichia coli by amylose resin affinity chromatography
-
recombinant N-terminally truncated enzyme DELTA24PmST1 from Escherichia coli strain BL21(DE3) by nickel affinity chromatography to homogeneity
-
recombinant truncated enzyme
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
a soluble form of hST3Gal II is expressed in COS-7 cells
-
commercial recombinant preparation
expressed COS-7 cells
expressed in CHO and HEK-293T cells; expressed in Escherichia coli BL21(DE3) cells
-
expressed in Escherichia coli AD202 cells
-
expressed in Escherichia coli BL21 (DE3) cells
-
expressed in Escherichia coli BL21(DE3) cells
expressed in Escherichia coli Origami B(DE3) cells as a fusion protein with an N-terminal maltose binding protein
-
expressed in Escherichia coli Tuner(DE3) cells
-
expression in CHO-K1 cells of truncated protein-A-His-tagged enzyme
expression in COS cells
-
expression in COS-1, Escherichia coli and Pichia pastoris. The recombinant protein expressed in COS-1 can catalyze the transfer of NeuAc from CMPNeuAc to asialo-fetuin. No activity is detected with a 32000 Da protein in Escherichia coli and both 32000 Da and 41000 Da proteins in Pichia pastoris
-
expression in COS-7 cell line of various constructs deleted in the N-terminal portion of the protein sequence. The souble forms of the protein consisting of amino acids 26-340, hST3-DELTA25, and amino acids 57-340, hST3-DELTA56, are efficiently secreted and active. Further deletion of the N-terminal region gives also rise to various polypeptides that are not active within the transfected cells and not secreted in the culture medium
-
expression in COS-7 cells
-
expression in COS-7 cells results in secretion of a catalytically active and soluble form of the enzyme into the medium, primary structure consists of a short NH2-terminal cytoplasmic domain, a signal-membrabe anchor domain, a proteolytically sensitive stem region, and a large COOH-terminal active domain
-
expression in Escherichia coli
expression in Escherichia coli, N-terminally truncated form
expression of full-length and truncated protein in Escherichia coli
-
expression of the N-terminally truncated enzyme DELTA24PmST1, lacking the first 24 amino acids of the membrane anchor, in Escherichia coli strain BL21(DE3)
-
full-length ST3Gal III DNA fragment subcloned into the pEF6/V5-His TOPO expression vector. SKOV-3 cells transfected with ST3Gal III-EF6
-
gene lic3B and lic3A, expression as maltose binding protein-fusion proteins in Escherichia coli
-
His-tagged and maltose-binding protein-fused enzyme is expressed in Escherichia coli BL21(DE3) cells
-
N-terminal 2-24 truncated form of recombinant alpha2,3-sialyltransferase (DELTANpp23ST)
-
overexpression in baculovirus system
overexpression in Trichoplusia ni cells as fusion protein with the IgG-binding domain and secretion into culture medium
-
ST3Gal I expression analysis; ST3Gal III expression analysis
ST3Gal I, DNA and amino acid sequence determination and analysis, phylogenetic tree and analysis; ST3Gal II, DNA and amino acid sequence determination and analysis, phylogenetic tree and analysis
ST3GalI and ST3GalII, expression in COS-7 cells
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
RelB RNAi most effectively inhibits the expression of isoform ST3Gal I; RelB RNAi most effectively inhibits the expression of isoform ST3Gal II; the expression of isoform ST3Gal VI is most effectively inhibited by RelB RNAi
taxol treatment upregulates ST3Gal III expression and forces expression of ST3Gal III attenuated taxol induced apoptosis. Taxol induces the expression of ST3Gal III by a post-transcriptional mechanism in SKOV-3 ovarian cancer cells
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the expression of isoform ST3Gal II is mildly induced by phorbol-12-myristate-13-acetate; the expression of isoform ST3Gal I mildly induced by phorbol-12-myristate-13-acetate
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D97A/Y125Q
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inactive
D97A/Y125Q/K253Q
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inactive
F121D/I124D/Y125D/F126D
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inactive
F121D/Y125Q
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inactive
H85A
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the mutant has very low activity compared to the wild type enzyme
H85F
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the mutant has very low activity compared to the wild type enzyme
H85W
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inactive
H85Y
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the mutant has very low activity compared to the wild type enzyme
Y125Q
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the mutant is active but less thermostable than the wild type enzyme; the mutant is active but less thermostable than the wild type enzyme and shows an approximately 3fold reduction in steady-state kinetic parameters
Y125Q/K253Q
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inactive
H85A
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the mutant has very low activity compared to the wild type enzyme
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H85F
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the mutant has very low activity compared to the wild type enzyme
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H85W
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inactive
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H85Y
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the mutant has very low activity compared to the wild type enzyme
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Y125Q
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the mutant is active but less thermostable than the wild type enzyme
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W70F
the mutant shows 60% of wild type activity
W97F
the mutant shows 40% of wild type activity
T116S
the mutation results in a marked increase in alpha2,3-trans-sialidase side activity
E271F
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the mutation does not affect alpha2-3-sialyltransferase activity
E271F/R313Y
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the mutations do not affect alpha2-3-sialyltransferase activity
H112A
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the mutant shows 4% of wild type activity
I335A
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the mutant shows 43% of wild type activity
L357A
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the mutant shows 23% of wild type activity
L40A
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the mutant shows 77% of wild type activity
M144A
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the mutant shows 12% of wild type activity
N85A
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inactive
P312A
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the mutant shows 48% of wild type activity
P34A
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the mutant shows 61% of wild type activity
R313A
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the mutant shows 107% of wild type activity
R313H
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the mutant shows 108% activity compared to the wild type enzyme; the mutation improves the enzyme's activity by a factor of 1.5
R313H/T265S
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the mutations improve the enzyme's activity by a factor of 2.37
R313N
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the mutation improves the enzyme's activity by a factor of 2.3
R313N/T265S
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the mutations improve the enzyme's activity by a factor of 2.16
R313T
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the mutation improves the enzyme's activity by a factor of 1.3
S143A
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the mutant shows 39% of wild type activity
S336A
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the mutant shows 17% of wild type activity
T265A
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the mutant shows 48% of wild type activity
T265G
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the mutant shows 94% activity compared to the wild type enzyme
T265N
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the mutant shows 126% activity compared to the wild type enzyme
T265S
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the mutant shows 116% activity compared to the wild type enzyme
T267A
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the mutant shows 26% of wild type activity
T268A
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the mutant shows 102% of wild type activity
T269A
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the mutant shows 48% of wild type activity
V147A
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the mutant shows 49% of wild type activity
Y388A
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the mutant shows 30% of wild type activity
additional information
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
drug development
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ST3Gal III can serve as a therapeutic target of taxol therapy
medicine
synthesis