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Enzyme Nomenclature
Information on EC 2.4.99.4 - beta-galactoside alpha-2,3-sialyltransferase
for references in articles please use BRENDA:EC2.4.99.4
Word Map on EC 2.4.99.4
- 2.4.99.4
-
sialylation
- st6gal
-
st8sia
-
st6galnac
-
maackia
-
sialylmotifs
- medicine
-
2.4.99.1
- synthesis
- drug development
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The enzyme appears in viruses and cellular organisms
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EC NUMBER 
COMMENTARY 
2.4.99.4
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RECOMMENDED NAME
GeneOntology No.
beta-galactoside alpha-2,3-sialyltransferase
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REACTION
REACTION DIAGRAM
COMMENTARY
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
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-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
glycosyl group transfer
-
-
-
-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
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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.
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CAS REGISTRY NUMBER
COMMENTARY
71124-51-1
-
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
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
malfunction
enzyme-deficient mice display reduced leukocyte adhesion in trauma-stimulated cremaster muscle venules, reduced induction of leukocyte arrest in cremaster muscle venules after systemic injection of CXCR2 chemokines CXCL1 and CXCL8, reduced leukocyte extravasation into inflamed cremaster muscle tissue, and reduced leukocyte extravasation in the thioglycollate-induced peritonitis model
malfunction
loss of isoform ST3Gal-IV leads to reduced cellularity of secondary lymphatic tissue; P- and E-selectin-dependent leukocyte rolling is mildly reduced in St3gal6-null mice and more severely in double-deficient mice. Neutrophil recruitment into the inflamed peritoneal cavity and lymphocyte homing to secondary lymphoid organs are impaired in St3gal6-null mice and more severely in double-deficient mice. Loss of isoform ST3Gal-VI leads to reduced cellularity of secondary lymphatic tissue
physiological function
-
ST3Gal III overexpression inhibits Taxol-triggered caspase-8 activation. ST3Gal III upregulation produces cellular resistance to taxol and hence reduces the efficacy of taxol therapy
physiological function
the enzyme significantly influences chemokine-triggered firmleukocyte arrest. The enzyme mediates reduced E-selectin-dependent rolling and increased E-selectin-mediated rolling velocity in inflamed cremaster muscle venules
physiological function
isoform ST3Gal-VI has a critical role in E-, P-, and L-selectin ligand synthesis in vitro and in vivo, and the coordinated expression of ST3Gal-IV and ST3Gal-VI together contribute to most of the sialylation that is responsible for the synthesis and function of the selectin ligands. Isoform ST3Gal-VI participates in leukocyte rolling under dynamic flow conditions. ST3Gal VI contributes to leukocyte rolling during inflammation in vivo and regulate lymphocyte homing to lymph nodes and Peyer patches in vivo. Leukocyte recruitment into the inflamed peritoneal cavity depends on ST3Gal-VI; the coordinated expression of ST3Gal-IV and ST3Gal-VI together contribute to most of the sialylation that is responsible for the synthesis and function of the selectin ligands. Isoform ST3Gal-IV contributes to leukocyte rolling during inflammation in vivo and regulate lymphocyte homing to lymph nodes and Peyer patches in vivo. Leukocyte recruitment into the inflamed peritoneal cavity depends on ST3Gal-IV
physiological function
-
the enzyme modulates pancreatic cancer cell motility and adhesion in vitro and enhances its metastatic potential in vivo. Isoform ST3Gal III increases de novo expression of SLex by enzymatic competition, enhances pancreatic adenocarcinoma cells adhesion to rh-E-selectin, and increases tumour cell adhesion to HSE cells
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
CMP + Galbeta(1->3)GalNAcbeta(1->3)Galalpha-O-Me
CMP-N-acetylneuraminate + NeuAcalpha(2->3)Galbeta(1->3)GalNAcbeta(1->3)Galalpha-O-Me
-
-
-
r
CMP + NeuAcalpha2,3Galbeta1,3GalNAcalpha-O-glycan
CMP-5-N-acetylneuraminate + Galbeta1,3GalNAcalpha-O-glycan
CMP-5-N-acetylneuraminate + 2-O-MeGalbeta1,3GlcNAc
?
-
an efficient acceptor for alpha2,3(N)ST
-
-
?
CMP-5-N-acetylneuraminate + 3-FGalbeta1,4GlcNAcbeta1,6(Galbeta1,3)GalNAcalpha-O-Bn
?
-
-
-
-
?
CMP-5-N-acetylneuraminate + 3-O-MeGalbeta1,4GlcNAcbeta1,6(Galbeta1,3)GalNAcalpha-O-Bn
?
-
-
-
-
?
CMP-5-N-acetylneuraminate + 4-FGalbeta1,4GlcNAcbeta1,6(Galbeta1,3)GalNAcalpha-O-Bn
?
-
-
-
-
?
CMP-5-N-acetylneuraminate + 4-O-MeGalbeta1,4GlcNAc
?
-
an efficient acceptor for alpha2,3(N)ST
-
-
?
CMP-5-N-acetylneuraminate + 4-O-MeGalbeta1,4GlcNAcbeta1,6(Galbeta1,3)GalNAcalpha-O-Bn
?
-
-
-
-
?
CMP-5-N-acetylneuraminate + D-Fucbeta1,3GalNAcbeta1,3-Gal-alpha-O-Me
?
-
an efficient acceptor for alpha2,3(O)ST
-
-
?
CMP-5-N-acetylneuraminate + Galbeta1,3GalNAcbeta1,3Galalpha-O-Me
?
-
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
-
-
?
CMP-5-N-acetylneuraminate + Galbeta1,4GlcNAcbeta1,6(3-FGalbeta1,3)GalNAcalpha-O-Bn
?
-
-
-
-
?
CMP-5-N-acetylneuraminate + Galbeta1,4GlcNAcbeta1,6(3-O-MeGalbeta1,3)GalNAcalpha-O-Bn
?
-
-
-
-
?
CMP-5-N-acetylneuraminate + Galbeta1,4GlcNAcbeta1,6(4-O-MeGalbeta1,3)GalNAcalpha-O-Bn
?
-
best substrate
-
-
?
CMP-5-N-acetylneuraminate + Galbeta1,4GlcNAcbeta1,6(Galbeta1,3)GalNAcalpha-O-Bn
?
-
a mucin core 2 tetrasaccharide, structures containing sialyl, fucosyl, sulfo, methyl, or fluoro substituents
-
-
?
CMP-N-acetyl-beta-neuraminate + Galbeta(1,3)(4-deoxy)GalNAcalphaOBn
?
-
effective acceptor for isoform ST3Gal-I
-
-
-
CMP-N-acetyl-beta-neuraminate + Galbeta(1,3)GlcNAcbeta(1,3)lac-beta-4-nitrophenyl
?
-
less than 1% activity compared to Galbeta(1,3)(4-deoxy)GalNAcalphaOBn
-
-
?
CMP-N-acetyl-beta-neuraminate + Galbeta(1,3)GlcNAcbeta(1,6)GalNAc-OBn
?
-
about 50% activity compared to Galbeta(1,3)(4-deoxy)GalNAcalphaOBn
-
-
?
CMP-N-acetylneuraminate + 1D-chiro-inositol
CMP + 1D-2-O-(alpha-sialosyl)-chiro-inositol
-
15% activity compared to lactose
-
-
?
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
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
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
CMP-N-acetylneuraminate + 4-deoxy-Galbeta1-3GalNAcalpha-benzyl
CMP + NeuAcalpha2-3(4-deoxy)-Galbeta1-3GalNAcalpha-benzyl
-
-
-
-
?
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
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
-
best substrate, about 37% conversion
-
-
-
CMP-N-acetylneuraminate + 4-methylumbelliferyl lactoside
CMP + ?
-
preferred acceptor
-
-
?
CMP-N-acetylneuraminate + 6-deoxy-Galbeta1-3GalNAcalpha-benzyl
CMP + NeuAcalpha2-3(6-deoxy)-Galbeta1-3GalNAcalpha-benzyl
-
-
-
-
?
CMP-N-acetylneuraminate + Ala-Pro-(Galbeta1-3GalNAcalpha)-Ser-Ser-Ser
CMP + NeuAcalpha2-3(Galbeta1-3GalNAcalpha)-Ser-Ser-Ser
-
-
-
-
?
CMP-N-acetylneuraminate + Ala-Pro-(Galbeta1-3GalNAcalpha)-Thr-Ser-Ser
CMP + NeuAcalpha2-3(Galbeta1-3GalNAcalpha)-Thr-Ser-Ser
-
-
-
-
?
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
-
-
26% yield
-
?
CMP-N-acetylneuraminate + alpha-methyl-galactopyranoside
CMP + ?
823% of the activity with acceptor Gal-beta-1,4-Glc
-
-
?
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
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
CMP-N-acetylneuraminate + beta-D-galactosyl-(1->4)-alpha-D-glucosyl-R
CMP + alpha-N-acetylneuraminyl-(2->3)-beta-D-glucosyl-(1->4)-R
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
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
CMP-N-acetylneuraminate + beta-D-galactosyl-O-R
CMP + alpha-N-acetylneuraminyl-2,3-beta-D-galactosyl-O-R
CMP-N-acetylneuraminate + beta-methyl-galactopyranoside
CMP + ?
343% of the activity with acceptor Gal-beta-1,4-Glc
-
-
?
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
-
-
18% yield
-
?
CMP-N-acetylneuraminate + epi-inositol
CMP + 1L-3-O-(alpha-sialosyl)-epi-inositol
-
18% activity compared to lactose
-
-
?
CMP-N-acetylneuraminate + Fucalpha1,2-Galbeta1,4-Glc
CMP + ?
52% of the activity with acceptor Gal-beta-1,4-Glc
-
-
?
CMP-N-acetylneuraminate + Galalpha-1,3-Galalpha-OMe
CMP + ?
528% of the activity with acceptor Gal-beta-1,4-Glc
-
-
?
CMP-N-acetylneuraminate + Galbeta(1-3)GalNAcOBzl
CMP + NeuAcalpha(2-3)Galbeta(1-3)GalNAcOBzl
-
-
-
-
?
CMP-N-acetylneuraminate + Galbeta1,3-Galbeta-OMe
CMP + ?
331% of the activity with acceptor Gal-beta-1,4-Glc
-
-
?
CMP-N-acetylneuraminate + Galbeta1-3(2-deoxy)Galalpha-benzyl
CMP + NeuAcalpha2-3Galbeta1-3(2-deoxy)Galalpha-benzyl
-
-
-
-
?
CMP-N-acetylneuraminate + Galbeta1-3(4-deoxy)GalNAcalpha-benzyl
CMP + NeuAcalpha2-3Galbeta1-3(4-deoxy)GalNAcalpha-benzyl
-
-
-
-
?
CMP-N-acetylneuraminate + Galbeta1-3(6-deoxy)GalNAcalpha-benzyl
CMP + NeuAcalpha2-3Galbeta1-3(6-deoxy)GalNAcalpha-benzyl
-
-
-
-
?
CMP-N-acetylneuraminate + Galbeta1-3(6-O-Me)GalNAcalpha-benzyl
CMP + NeuAcalpha2-4Galbeta1-3(6-O-Me)GalNAcalpha-benzyl
-
-
-
-
?
CMP-N-acetylneuraminate + Galbeta1-3(6-sulfo)GalNAcalpha-O-allyl
CMP + NeuAcalpha2-4Galbeta1-3(6-sulfo)GalNAcalpha-O-allyl
-
-
-
-
?
CMP-N-acetylneuraminate + Galbeta1-3(Fucalpha1-4)GlcNAcbeta1-3Galbeta1-4Glc-pyridylamine
CMP + ?
CMP-N-acetylneuraminate + Galbeta1-3(NeuAcalpha2,6)GalNAcalpha-O-benzyl
CMP + NeuAcalpha2-4Galbeta1-3(NeuAcalpha2,6)GalNAcalpha-O-benzyl
CMP-N-acetylneuraminate + Galbeta1-3GalNAcalpha-8-methoxycarbonyl-octyl
CMP + NeuAcalpha2-3Galbeta1-3GalNAcalpha-8-methoxycarbonyl-octyl
-
-
-
-
?
CMP-N-acetylneuraminate + Galbeta1-3GalNAcalpha-antifreeze glycoprotein
CMP + NeuAcalpha2-3Galbeta1-3GalNAcalpha-antifreeze glycoprotein
-
-
-
-
?
CMP-N-acetylneuraminate + Galbeta1-3GalNAcalpha-O-allyl
CMP + NeuAcalpha2-4Galbeta1-3GalNAcalpha-O-allyl
-
-
-
-
?
CMP-N-acetylneuraminate + Galbeta1-3GalNAcalpha-O-benzyl
CMP + NeuAcalpha2-4Galbeta1-3GalNAcalpha-O-benzyl
CMP-N-acetylneuraminate + Galbeta1-3GalNAcalpha-o-nitrophenyl
CMP + NeuAcalpha2-3Galbeta1-3GalNAcalpha-o-nitrophenyl
-
-
-
-
?
CMP-N-acetylneuraminate + Galbeta1-3GalNAcalpha-p-nitrophenyl
CMP + NeuAcalpha2-3Galbeta1-3GalNAcalpha-p-nitrophenyl
-
-
-
-
?
CMP-N-acetylneuraminate + Galbeta1-3GalNAcalpha-phenyl
CMP + NeuAcalpha2-3Galbeta1-3GalNAcalpha-phenyl
-
-
-
-
?
CMP-N-acetylneuraminate + Galbeta1-3GalNAcalpha-Ser
CMP + NeuAcalpha2-3Galbeta1-3GalNAcalpha-Ser
-
-
-
-
?
CMP-N-acetylneuraminate + Galbeta1-3GalNAcbeta1-4[Neu5Acalpha2-3]Galalpha1-4Glcbeta1
CMP + ?
CMP-N-acetylneuraminate + Galbeta1-3GlcNAcbeta1-3Galbeta1-4Glc
CMP + NeuAcalpha2-3Galbeta1-3GlcNAcbeta1-3Galbeta1-4Glc
-
weak, i.e. lactotetraose
-
-
?
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
-
-
-
-
?
CMP-N-acetylneuraminate + Galbeta1-4(Fucalpha1-3)GlcNAcbeta1-3Galbeta1-4Glc-pyridylamine
CMP + ?
-
-
-
?
CMP-N-acetylneuraminate + Galbeta1-4Glc
CMP + NeuAcalpha2-3Galbeta1-4Glc
-
weak acceptor
-
-
?
CMP-N-acetylneuraminate + Galbeta1-4GlcNAcbeta1-3Galbeta1-4Glc-pyridylamine
CMP + ?
-
-
-
?
CMP-N-acetylneuraminate + Galbeta1-6GlcNAc
CMP + NeuAcalpha2-3Galbeta1-6GlcNAc
-
weak acceptor for enzyme B
-
-
?
CMP-N-acetylneuraminate + GalNAcalpha1-3GalNAcbeta1-3Galalpha1-4Galbeta1-4Glc-pyridylamine
CMP + ?
-
-
-
?
CMP-N-acetylneuraminate + GalNAcbeta1-4Galbeta1-4Glc-pyridylamine
CMP + ?
-
-
-
?
CMP-N-acetylneuraminate + GlcNAcbeta1-6(D-Fucbeta1-3)GalNAcalpha-benzyl
CMP + NeuAcalpha2-3 GlcNAcbeta1-6(D-Fucbeta1-3)GalNAcalpha-benzyl
-
-
-
-
?
CMP-N-acetylneuraminate + GlcNAcbeta1-6(Galbeta1-3)GalNAcalpha-benzyl
CMP + NeuAcalpha2-3 GlcNAcbeta1-6(Galbeta1-3)GalNAcalpha-benzyl
-
-
-
-
?
CMP-N-acetylneuraminate + GlcNAcbeta1-6(GlcNAcbeta1-6Galbeta1-3)GalNAcalpha-benzyl
CMP + NeuAcalpha2-3GlcNAcbeta1-6(GlcNAcbeta1-6Galbeta1-3)GalNAcalpha-benzyl
-
-
-
-
?
CMP-N-acetylneuraminate + lactose
CMP + NeuAcalpha(2->3)Galbeta(1->4)Glc
-
-
-
-
?
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
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
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
34.4% conversion after 10 min incubation, 73.9% conversion after 4 h incubation
-
-
?
CMP-N-acetylneuraminate + methyl-alpha-L-fucopyranoside
CMP + ?
49% of the activity with Gal-beta-1,4-Glc
-
-
?
CMP-N-acetylneuraminate + methyl-beta-L-fucopyranoside
CMP + ?
42% of the activity with Gal-beta-1,4-Glc
-
-
?
CMP-N-acetylneuraminate + methyl-D-galactopyranosyl-beta-1,3-N-acetylglucosamine
CMP + ?
124% of the activity with lactose
-
-
?
CMP-N-acetylneuraminate + muco-inositol
?
-
1.7% activity compared to lactose
-
-
?
CMP-N-acetylneuraminate + myo-inositol
?
-
4.5% activity compared to lactose
-
-
?
CMP-N-acetylneuraminate + N-acetyl-D-glucosamine
CMP + ?
40% of the activity with Gal-beta-1,4-Glc
-
-
?
CMP-N-acetylneuraminate + N-acetyl-lactosamine
CMP + ?
-
-
-
?
CMP-N-acetylneuraminate + N-acetylgalactosamine
CMP + ?
58% of the activity with lactose
-
-
?
CMP-N-acetylneuraminate + N-acetylglucosamine
CMP + ?
55% of the activity with lactose
-
-
?
CMP-N-acetylneuraminate + N-acetyllactosamine
CMP + ?
127% of the activity with lactose
-
-
?
CMP-Neu5Ac + Galbeta-1,4-Glc-6-(5-fluorescein-carboxamido)-hexanoic acid succinimidyl ester
?
-
-
-
-
?
CMP-NeuAc + Galbeta(1-3)GalNAc-O-octyl
CMP + NeuAcalpha(2-3)Galbeta(1-3)GalNAc-O-octyl
-
-
-
-
?
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
-
-
-
-
?
CMP-NeuAc + Galbeta(1-3)[NeuAcalpha(2-6)]GalNAc-O-octyl
CMP + NeuAcalpha(2-3)Galbeta(1-3)[NeuAcalpha(2-6)]GalNAc-O-octyl
-
-
-
-
?
CMP + NeuAcalpha2,3Galbeta1,3GalNAcalpha-O-glycan
CMP-5-N-acetylneuraminate + Galbeta1,3GalNAcalpha-O-glycan
-
-
-
-
r
CMP + NeuAcalpha2,3Galbeta1,3GalNAcalpha-O-glycan
CMP-5-N-acetylneuraminate + Galbeta1,3GalNAcalpha-O-glycan
-
-
-
-
r
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
-
100% activity
-
-
?
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
21.5% conversion after 10 min incubation, 57.8% conversion after 4 h incubation
-
-
?
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
-
100% activity
-
-
?
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
21.5% conversion after 10 min incubation, 57.8% conversion after 4 h incubation
-
-
?
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
-
25.5% activity compared to Lacbeta-Pro-triazole-C14
-
-
?
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
-
25.5% activity compared to Lacbeta-Pro-triazole-C14
-
-
?
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
29.5% conversion after 10 min incubation, 76.9% conversion after 4 h incubation
-
-
?
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
29.5% conversion after 10 min incubation, 76.9% conversion after 4 h incubation
-
-
?
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
29.9% conversion after 10 min incubation, 65.6% conversion after 4 h incubation
-
-
?
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
29.9% conversion after 10 min incubation, 65.6% conversion after 4 h incubation
-
-
?
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
-
-
-
-
?
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
-
-
-
?
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
-
-
-
?
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
-
-
-
?
CMP-N-acetylneuraminate + beta-D-galactosyl-(1->4)-alpha-D-glucosyl-R
CMP + alpha-N-acetylneuraminyl-(2->3)-beta-D-glucosyl-(1->4)-R
-
-
-
-
?
CMP-N-acetylneuraminate + beta-D-galactosyl-(1->4)-alpha-D-glucosyl-R
CMP + alpha-N-acetylneuraminyl-(2->3)-beta-D-glucosyl-(1->4)-R
-
-
-
-
?
CMP-N-acetylneuraminate + beta-D-galactosyl-1,3-N-acetyl-alpha-D-galactosaminyl-R
?
-
enzyme is involved in O-linked glycosylation pathway for synthesis of core 1 oligosaccharides
-
-
-
CMP-N-acetylneuraminate + beta-D-galactosyl-1,3-N-acetyl-alpha-D-galactosaminyl-R
?
-
enzyme activity is significantly increased in patients with chronic myelogenous leukemia and acute myeloid leukemia
-
-
-
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
-
-
-
?
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
-
acceptor: GD1b
-
-
-
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
-
acceptor: asialo-GM1
-
-
-
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
-
acceptor: asialo-bovine-submaxillary mucin, weak activity
-
-
-
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
-
acceptor: asialofetuin
-
-
-
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
-
acceptor: Gg4
-
-
-
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
-
acceptor: GM1
-
-
-
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
-
acceptor: GD1b
-
-
?
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
-
acceptor: GD1a
-
-
?
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
-
acceptor: asialo-GM1
-
-
?
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
-
acceptor: asialofetuin
-
-
?
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
-
acceptor: asialo-bovine submaxillary mucin
-
-
?
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
-
acceptor substrate preference for glycolipid than for O-linked oligosaccharides of glycoproteins
-
-
?
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
-
acceptors are glycosides, glycolipids, or glycoproteins containing Galbeta1-3GalNAc terminal sequence
-
-
?
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
-
acceptor: antifreeze glycoprotein
-
-
?
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
-
acceptor: GM1
-
-
?
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
-
acceptor: asialo-GM1
-
-
-
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
-
acceptor: asialo-GM1
-
-
?
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
-
acceptor: asialofetuin
-
-
?
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
-
exhibits transferase activity towards only the disaccharide moiety of Galbeta1,3GalNAc of glycoproteins and glycolipids: asialo-GM1, GD1a is formed from GM1 and GD1b is formed from GD1b
-
-
?
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
-
acceptor: GM1
-
-
?
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
-
acceptor glycoprotein
-
-
?
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
-
acceptor: Galbeta1-3GalNAcalpha-O-allyl/acrylamide copolymer
-
-
?
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
-
acceptor: antifreeze glycoprotein
-
-
?
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
-
acceptor: asialoglycoprotein
-
-
?
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
-
highest activity
-
-
?
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
-
highest activity
-
-
?
CMP-N-acetylneuraminate + beta-D-galactosyl-O-R
CMP + alpha-N-acetylneuraminyl-2,3-beta-D-galactosyl-O-R
-
-
-
-
?
CMP-N-acetylneuraminate + beta-D-galactosyl-O-R
CMP + alpha-N-acetylneuraminyl-2,3-beta-D-galactosyl-O-R
-
substrate binding structure and induced conformational changes, CMP only forms interactions with residues in the C-terminal domain, both Ser 143 and Tyr 388 form hydrogen bonds to a water molecule, which in turn hydrogen-bonds to the terminal phosphate oxygen of CMP, overview
-
-
?
CMP-N-acetylneuraminate + Gal-beta-1,3-GlcNAc-beta-OMe
CMP + ?
129% of the activity with Gal-beta-1,4-Glc
-
-
?
CMP-N-acetylneuraminate + Gal-beta-1,3-GlcNAc-beta-OMe
CMP + ?
129% of the activity with Gal-beta-1,4-Glc
-
-
?
CMP-N-acetylneuraminate + Gal-beta-1,3-GlcNAc-beta-OMe
CMP + ?
192% of the activity with acceptor Gal-beta-1,4-Glc
-
-
?
CMP-N-acetylneuraminate + Gal-beta-1,4-Glc
CMP + ?
-
-
-
?
CMP-N-acetylneuraminate + Gal-beta-1,4-Glc
CMP + ?
-
-
-
?
CMP-N-acetylneuraminate + Gal-beta-1,4-GlcNAc
CMP + ?
103% of the activity with Gal-beta-1,4-Glc
-
-
?
CMP-N-acetylneuraminate + Gal-beta-1,4-GlcNAc
CMP + ?
103% of the activity with Gal-beta-1,4-Glc
-
-
?
CMP-N-acetylneuraminate + Gal-beta-1,4-GlcNAc
CMP + ?
96% of the activity with acceptor Gal-beta-1,4-Glc
-
-
?
CMP-N-acetylneuraminate + Galalpha1-4Galbeta1-4Glc-pyridylamine
CMP + ?
-
-
-
?
CMP-N-acetylneuraminate + Galalpha1-4Galbeta1-4Glc-pyridylamine
CMP + ?
-
-
-
?
CMP-N-acetylneuraminate + Galbeta1-3(Fucalpha1-4)GlcNAcbeta1-3Galbeta1-4Glc-pyridylamine
CMP + ?
-
-
-
?
CMP-N-acetylneuraminate + Galbeta1-3(Fucalpha1-4)GlcNAcbeta1-3Galbeta1-4Glc-pyridylamine
CMP + ?
-
-
-
?
CMP-N-acetylneuraminate + Galbeta1-3(NeuAcalpha2,6)GalNAcalpha-O-benzyl
CMP + NeuAcalpha2-4Galbeta1-3(NeuAcalpha2,6)GalNAcalpha-O-benzyl
-
-
-
-
?
CMP-N-acetylneuraminate + Galbeta1-3(NeuAcalpha2,6)GalNAcalpha-O-benzyl
CMP + NeuAcalpha2-4Galbeta1-3(NeuAcalpha2,6)GalNAcalpha-O-benzyl
-
-
-
-
?
CMP-N-acetylneuraminate + Galbeta1-3GalNAc
CMP + NeuAcalpha2-3Galbeta1-3GalNAc
-
-
-
-
?
CMP-N-acetylneuraminate + Galbeta1-3GalNAc
CMP + NeuAcalpha2-3Galbeta1-3GalNAc
-
-
-
-
-
CMP-N-acetylneuraminate + Galbeta1-3GalNAc
CMP + NeuAcalpha2-3Galbeta1-3GalNAc
-
-
-
-
?
CMP-N-acetylneuraminate + Galbeta1-3GalNAc
CMP + NeuAcalpha2-3Galbeta1-3GalNAc
-
-
-
-
-
CMP-N-acetylneuraminate + Galbeta1-3GalNAc
CMP + NeuAcalpha2-3Galbeta1-3GalNAc
-
-
-
-
?
CMP-N-acetylneuraminate + Galbeta1-3GalNAc
CMP + NeuAcalpha2-3Galbeta1-3GalNAc
-
best acceptor for enzyme ST3Gal I and ST3Gal II
-
-
?
CMP-N-acetylneuraminate + Galbeta1-3GalNAc
CMP + NeuAcalpha2-3Galbeta1-3GalNAc
-
-
-
-
?
CMP-N-acetylneuraminate + Galbeta1-3GalNAc
CMP + NeuAcalpha2-3Galbeta1-3GalNAc
-
best acceptor
-
-
?
CMP-N-acetylneuraminate + Galbeta1-3GalNAcalpha-O-benzyl
CMP + NeuAcalpha2-4Galbeta1-3GalNAcalpha-O-benzyl
-
-
-
-
?
CMP-N-acetylneuraminate + Galbeta1-3GalNAcalpha-O-benzyl
CMP + NeuAcalpha2-4Galbeta1-3GalNAcalpha-O-benzyl
-
-
-
?
CMP-N-acetylneuraminate + Galbeta1-3GalNAcalpha-O-benzyl
CMP + NeuAcalpha2-4Galbeta1-3GalNAcalpha-O-benzyl
-
-
-
-
?
CMP-N-acetylneuraminate + Galbeta1-3GalNAcalpha-O-benzyl
CMP + NeuAcalpha2-4Galbeta1-3GalNAcalpha-O-benzyl
-
-
-
-
?
CMP-N-acetylneuraminate + Galbeta1-3GalNAcalpha-Thr(NAc)OMe
CMP + ?
-
-
-
?
CMP-N-acetylneuraminate + Galbeta1-3GalNAcalpha-Thr(NAc)OMe
CMP + ?
-
-
-
?
CMP-N-acetylneuraminate + Galbeta1-3GalNAcbeta1-4Galbeta1-4Glc-pyridylamine
CMP + ?
-
-
-
?
CMP-N-acetylneuraminate + Galbeta1-3GalNAcbeta1-4Galbeta1-4Glc-pyridylamine
CMP + ?
-
-
-
?
CMP-N-acetylneuraminate + Galbeta1-3GalNAcbeta1-4[Neu5Acalpha2-3]Galalpha1-4Glcbeta1
CMP + ?
-
-
-
?
CMP-N-acetylneuraminate + Galbeta1-3GalNAcbeta1-4[Neu5Acalpha2-3]Galalpha1-4Glcbeta1
CMP + ?
best substrate tested
-
-
?
CMP-N-acetylneuraminate + Galbeta1-3GlcNAc
CMP + NeuAcalpha2-3Galbeta1-3GlcNAc
-
-
-
-
-
CMP-N-acetylneuraminate + Galbeta1-3GlcNAc
CMP + NeuAcalpha2-3Galbeta1-3GlcNAc
-
very low activity, enzyme ST3Gal I and ST3Gal II
-
-
-
CMP-N-acetylneuraminate + Galbeta1-3GlcNAc
CMP + NeuAcalpha2-3Galbeta1-3GlcNAc
-
weak acceptor
-
-
?
CMP-N-acetylneuraminate + Galbeta1-3GlcNAcbeta-CH2-CH2-N3
CMP + ?
-
-
-
?
CMP-N-acetylneuraminate + Galbeta1-3GlcNAcbeta-CH2-CH2-N3
CMP + ?
little activity
-
-
?
CMP-N-acetylneuraminate + Galbeta1-3GlcNAcbeta1-3Galbeta1-4Glc-pyridylamine
CMP + ?
-
-
-
?
CMP-N-acetylneuraminate + Galbeta1-3GlcNAcbeta1-3Galbeta1-4Glc-pyridylamine
CMP + ?
-
-
-
?
CMP-N-acetylneuraminate + Galbeta1-4GlcNAc
CMP + NeuAcalpha2-3Galbeta1-4GlcNAc
-
no activity
-
-
-
CMP-N-acetylneuraminate + Galbeta1-4GlcNAc
CMP + NeuAcalpha2-3Galbeta1-4GlcNAc
-
weak acceptor for enzyme B
-
-
?
CMP-N-acetylneuraminate + LacNAcbeta-Pro-triazole-C14
CMP + ?
-
51.2% activity compared to Lacbeta-Pro-triazole-C14
-
-
?
CMP-N-acetylneuraminate + LacNAcbeta-Pro-triazole-C14
CMP + ?
-
51.2% activity compared to Lacbeta-Pro-triazole-C14
-
-
?
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
-
-
-
?
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
-
-
-
?
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
-
-
-
-
?
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
preferred acceptor, 30.4% conversion after 10 min incubation, 64.8% conversion after 4 h incubation
-
-
?
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
-
-
-
-
?
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
preferred acceptor, 30.4% conversion after 10 min incubation, 64.8% conversion after 4 h incubation
-
-
?
CMP-N-acetylneuraminate + methyl-alpha-D-galactopyranoside
CMP + ?
452% of the activity with Gal-beta-1,4-Glc
-
-
?
CMP-N-acetylneuraminate + methyl-alpha-D-galactopyranoside
CMP + ?
452% of the activity with Gal-beta-1,4-Glc
-
-
?
CMP-N-acetylneuraminate + methyl-alpha-D-galactopyranoside
CMP + ?
135% of the activity with lactose
-
-
?
CMP-N-acetylneuraminate + methyl-alpha-D-glucopyranoside
CMP + ?
48% of the activity with Gal-beta-1,4-Glc
-
-
?
CMP-N-acetylneuraminate + methyl-alpha-D-glucopyranoside
CMP + ?
48% of the activity with Gal-beta-1,4-Glc
-
-
?
CMP-N-acetylneuraminate + methyl-alpha-D-glucopyranoside
CMP + ?
62% of the activity with lactose
-
-
?
CMP-N-acetylneuraminate + methyl-beta-D-galactopyranoside
CMP + ?
251% of the activity with Gal-beta-1,4-Glc
-
-
?
CMP-N-acetylneuraminate + methyl-beta-D-galactopyranoside
CMP + ?
114% of the activity with lactose
-
-
?
CMP-N-acetylneuraminate + methyl-beta-D-glucopyranoside
CMP + ?
33% of the activity with Gal-beta-1,4-Glc
-
-
?
CMP-N-acetylneuraminate + methyl-beta-D-glucopyranoside
CMP + ?
52% of the activity with lactose
-
-
?
CMP-N-acetylneuraminate + methyl-beta-D-mannopyranoside
CMP + ?
63% of the activity with Gal-beta-1,4-Glc
-
-
?
CMP-N-acetylneuraminate + methyl-beta-D-mannopyranoside
CMP + ?
57% of the activity with lactose
-
-
?
CMP-N-acetylneuraminate + N-acetyl-D-galactosamine
CMP + ?
43% of the activity with Gal-beta-1,4-Glc
-
-
?
CMP-N-acetylneuraminate + N-acetyl-D-galactosamine
CMP + ?
76% of the activity with acceptor Gal-beta-1,4-Glc
-
-
?
additional information
?
-
-
the bifunctional enzyme also exhibits alpha2,8-sialyltransferase activity
-
-
-
additional information
?
-
-
the bifunctional enzyme also exhibits alpha2,8-sialyltransferase activity
-
-
-
additional information
?
-
no substrate: gangliosides GM1 or GM1b
-
-
-
additional information
?
-
-
Lic3B is a second sialyltransferase in Haemophilus influenzae responsible for the addition of di-sialic acid to the lipopolysaccharides, structure overview, modification of the lipopolysaccharides by di-sialylation confers increased resistance of the organism to the killing effects of normal human serum, as compared with mono-sialylated or non-sialylated species
-
-
-
additional information
?
-
-
Lic3A is a specific alpha-2,3-sialyltransferase, while bifunctional Lic3B has both alpha-2,3- and alpha-2,8-sialyltransferase activities, EC 2.4.99.4 and EC 2.4.99.8
-
-
-
additional information
?
-
-
no or very low activity with Gal-beta1,3-GlcNAc, T-antigen Gal-beta1,3-GalNAc-alpha, and NeuAc-alpha2,3-Gal-beta1,4-Glc
-
-
-
additional information
?
-
-
no or very low activity with Gal-beta1,3-GlcNAc, T-antigen Gal-beta1,3-GalNAc-alpha, and NeuAc-alpha2,3-Gal-beta1,4-Glc
-
-
-
additional information
?
-
-
no activity with Galbeta1-4GlcNAc, GalNAcbeta1-4GlcNAc or Galbeta1-4Glc
-
-
-
additional information
?
-
-
the hST3gal II gene is expressed specifically by alternative promoter utilization and is regulated in a tissue-restricted fashion at the level of transcription
-
-
-
additional information
?
-
-
sialylation of beta1,3Gal must precede the sialylation of beta1,4Gal for favorable biosynthesis of mucin core 2 compounds
-
-
-
additional information
?
-
sialyltransferases catalyze the transfer of sialic acid from CMP-Neu5Ac donor substrate to the terminal nonreducing saccharide of glycoproteins or glycolipids
-
-
-
additional information
?
-
-
thyroid sialyltransferase mRNA level and activity are increased in Graves' disease
-
-
-
additional information
?
-
-
substrate specificities, alpha2,3-sialylation of beta1,3Gal in mucin core 2 can proceed even after alpha1,3 fucosylation of beta1,6-linked LacNAc, alpha2,3 sialylation of the 6-O-sulfoLacNAc moiety in mucin core 2 is facilitated when beta1,3Gal is already alpha2,3 sialylated, a 3- or 4-fluoro substituent in beta1,4Gal results in poor acceptors for the recombinant alpha2,6(N)ST and alpha2,3(N)ST, whereas 4-fluoro- or 4-OMe-Galbeta1,3GalNAc-R is a good acceptor for recombinant alpha2,3(O)ST, 4-O-methylation of beta1,4Gal increases the acceptor efficiency considerably toward alpha2,3(N)ST, either alpha1,3 fucosylation or 6-O-sulfation of the GlcNAc moiety reduces the activity, sialylation of beta1,3Gal in addition to 6-O-sulfation of GlcNAc moiety abolishes the activity, detailed overview
-
-
-
additional information
?
-
-
human enzyme shows specificity towards arrayed oligosaccharides with type 1 terminus including sialyllacto-N-tetraose b Galbeta1-3[Neu5Acalpha2-6]GlcNAcbeta1-3Galbeta1-4Glc, various type 2 termini including poly-LacNAc as well as lactose. O-glycans such as the T-antigen and core 2 structures are good acceptors and enzyme displays some activities towards the alpha2-6 sialyl T-antigen. Extended type 2 structures such as poly-LacNAc are good acceptors but not LacDiNAc
-
-
-
additional information
?
-
ganglioside GD1a is synthesized from GM1 by isoform ST3Gal I
-
-
-
additional information
?
-
ganglioside GD1a is synthesized from GM1 by isoform ST3Gal I
-
-
-
additional information
?
-
ganglioside GD1a is synthesized from GM1 by isoform ST3Gal I
-
-
-
additional information
?
-
ganglioside GD1a is synthesized from GM1 mainly by isoform ST3Gal II
-
-
-
additional information
?
-
ganglioside GD1a is synthesized from GM1 mainly by isoform ST3Gal II
-
-
-
additional information
?
-
ganglioside GD1a is synthesized from GM1 mainly by isoform ST3Gal II
-
-
-
additional information
?
-
the enzyme isoform ST3Gal IV synthesizes sialyl paragloboside
-
-
-
additional information
?
-
the enzyme isoform ST3Gal IV synthesizes sialyl paragloboside
-
-
-
additional information
?
-
the enzyme isoform ST3Gal IV synthesizes sialyl paragloboside
-
-
-
additional information
?
-
-
no activity with Galbeta(1,4)GlcNAcbeta(1,3)Galbeta-4-nitrophenyl, Galbeta(1,4)GlcNAcbeta(1,3)Galbeta(1,4)GlcNAc-4-nitrophenyl, MeO-4-Galbeta(1,4)GlcNAc-OBn, Galbeta(1,4)GlcNAcbeta(1,6)(4F-Galbeta(1,3))GalNAc-OBn, MeO-3-Galbeta(1,3)GalNAc-OBn, and MeO-2-Galbeta(1,3)GlcNAc-OBn
-
-
-
additional information
?
-
-
ST3Gal-I-/- mice show a profound disregulation of CD8 T cell homeostasis, however the enzyme is not required for regulation of CD8-class I MHC binding during T cell development, overview
-
-
-
additional information
?
-
-
ST3Gal-I-/- mice show a profound disregulation of CD8 T cell homeostasis, however the enzyme is not required for regulation of CD8-class I MHC binding during T cell development, overview
-
-
-
additional information
?
-
the enzyme is alternatively active at pH 4.5 as alpha2,3-sialidase and alpha2,3-trans-sialidase and also shows CMP-N-acetyl-neuraminic hydrolase activity at pH 8.0 when no sialyl acceptor substrate is present
-
-
-
additional information
?
-
-
the bifunctional enzyme also catalyzes the formation of alpha2,6-sialyl-glycosides, EC 2.4.99.1
-
-
-
additional information
?
-
-
beta(1->4)-linked galactosyl lipids are better substrates than beta(1->3)-linked galactosyl lipids
-
-
-
additional information
?
-
-
beta(1->4)-linked galactosyl lipids are better substrates than beta(1->3)-linked galactosyl lipids
-
-
-
additional information
?
-
-
no activity with 1L-chiro-inositol and scyllo-inositol
-
-
-
additional information
?
-
-
the enzyme possesses not only sialyltransferase activity but also weak sialidase activity. Lactoside is hydrolyzed faster and completely when CMP-beta-D-N-acetylneuraminic acid is coexistent
-
-
-
additional information
?
-
enzyme is able to degrade pyridylaminated 3'-sialyllactose,at a low level
-
-
-
additional information
?
-
-
enzyme catalyzes transfer of sialic acid from cytidine 5'-monophospho-n-acetylneuraminic acid to an acceptor molecule and enzyme synthesizes CMP-NeuAc by transferring NeuAc from the NeuAcalpha2,3Galbeta1,3GalNAcalpha unit of O-glycans, 3-sialyl globo unit of glycolipids, and sialylated macromolecules to 5'-CMP. CMP-NeuAc produced in situ is utilized by the same enzyme to sialylate other O-glycans and by other sialyltransferases such as ST6Gal-I and ST6GalNAc-I, forming alpha2,6-sialylated compounds. ST3Gal-II also catalyzes the conversion of 5'-uridine monophosphate to UMP-NeuAc, which is an inactive sialyl donor. Reverse sialylation proceeds without the need for free sialic acid, divalent metal ions, or energy
-
-
-
additional information
?
-
-
enzyme displays significant activities towards the type 4 Galbeta1-3GalNAcbeta-structures including asialo-GM1, core 2 antigens and alpha2-6 sialyl T-antigen but not beta2-6 sialyl T-antigen. Rat enzyme can utilize the fucosylated acceptor Lewisa Galbeta1-3[Fucalpha1-4]GlcNAc-oligosaccharide
-
-
-
additional information
?
-
the enzyme mediates alpha2,3-sialylation of Gal in the Galbeta(1->3)GalNAcalpha-unit of O-glycans
-
-
-
additional information
?
-
-
no activity with: 3-sulfoGalbeta1-3GalNAcalpha-O-allyl, 3-sulfoGalbeta1-3GalNAcalpha-O-benzyl, 3-O-Me-Galbeta1-3GalNAcalpha-O-Bn, 3-O-Me-Galbeta1-3(6-O-Me)GalNAcalpha-O-benzyl, 6-sulfoGalbeta1-3GalNAcalpha-O-allyl
-
-
-
additional information
?
-
-
porcine enzyme displays very strong selectivity towards branched oligosaccharides such as core 2 O-glycans but not the core 6, core 4 or core 3 structures lacking the terminal Galbeta3-moiety. Also ganglioside of type 4 Galbeta1-3Gal-NAcbeta-epitopes including GM1 and asialo-GM1 are readily sialylated. Even H-type 3 Fucalpha1-2Galbeta1-3GalNAcalpha-structures are well recognized
-
-
-
additional information
?
-
no substrate: gangliosides GM1 or GM1b
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
CMP-N-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
CMP-N-acetylneuraminate + beta-D-galactosyl-(1->4)-alpha-D-glucosyl-R
CMP + alpha-N-acetylneuraminyl-(2->3)-beta-D-glucosyl-(1->4)-R
CMP-N-acetylneuraminate + beta-D-galactosyl-O-R
CMP + alpha-N-acetylneuraminyl-2,3-beta-D-galactosyl-O-R
-
-
-
-
?
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
-
-
-
-
?
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
K9UUI6
-
-
-
?
CMP-N-acetylneuraminate + beta-D-galactosyl-(1->4)-alpha-D-glucosyl-R
CMP + alpha-N-acetylneuraminyl-(2->3)-beta-D-glucosyl-(1->4)-R
-
-
-
-
?
CMP-N-acetylneuraminate + beta-D-galactosyl-(1->4)-alpha-D-glucosyl-R
CMP + alpha-N-acetylneuraminyl-(2->3)-beta-D-glucosyl-(1->4)-R
-
-
-
-
?
CMP-N-acetylneuraminate + beta-D-galactosyl-1,3-N-acetyl-alpha-D-galactosaminyl-R
?
-
enzyme is involved in O-linked glycosylation pathway for synthesis of core 1 oligosaccharides
-
-
-
CMP-N-acetylneuraminate + beta-D-galactosyl-1,3-N-acetyl-alpha-D-galactosaminyl-R
?
-
enzyme activity is significantly increased in patients with chronic myelogenous leukemia and acute myeloid leukemia
-
-
-
additional information
?
-
-
the bifunctional enzyme also exhibits alpha2,8-sialyltransferase activity
-
-
-
additional information
?
-
-
the bifunctional enzyme also exhibits alpha2,8-sialyltransferase activity
-
-
-
additional information
?
-
-
Lic3B is a second sialyltransferase in Haemophilus influenzae responsible for the addition of di-sialic acid to the lipopolysaccharides, structure overview, modification of the lipopolysaccharides by di-sialylation confers increased resistance of the organism to the killing effects of normal human serum, as compared with mono-sialylated or non-sialylated species
-
-
-
additional information
?
-
-
the hST3gal II gene is expressed specifically by alternative promoter utilization and is regulated in a tissue-restricted fashion at the level of transcription
-
-
-
additional information
?
-
-
sialylation of beta1,3Gal must precede the sialylation of beta1,4Gal for favorable biosynthesis of mucin core 2 compounds
-
-
-
additional information
?
-
Q11201
sialyltransferases catalyze the transfer of sialic acid from CMP-Neu5Ac donor substrate to the terminal nonreducing saccharide of glycoproteins or glycolipids
-
-
-
additional information
?
-
-
thyroid sialyltransferase mRNA level and activity are increased in Graves' disease
-
-
-
additional information
?
-
Q11201
ganglioside GD1a is synthesized from GM1 by isoform ST3Gal I
-
-
-
additional information
?
-
Q11206
ganglioside GD1a is synthesized from GM1 by isoform ST3Gal I
-
-
-
additional information
?
-
Q16842
ganglioside GD1a is synthesized from GM1 by isoform ST3Gal I
-
-
-
additional information
?
-
Q11201
ganglioside GD1a is synthesized from GM1 mainly by isoform ST3Gal II
-
-
-
additional information
?
-
Q11206
ganglioside GD1a is synthesized from GM1 mainly by isoform ST3Gal II
-
-
-
additional information
?
-
Q16842
ganglioside GD1a is synthesized from GM1 mainly by isoform ST3Gal II
-
-
-
additional information
?
-
Q11201
the enzyme isoform ST3Gal IV synthesizes sialyl paragloboside
-
-
-
additional information
?
-
Q11206
the enzyme isoform ST3Gal IV synthesizes sialyl paragloboside
-
-
-
additional information
?
-
Q16842
the enzyme isoform ST3Gal IV synthesizes sialyl paragloboside
-
-
-
additional information
?
-
-
ST3Gal-I-/- mice show a profound disregulation of CD8 T cell homeostasis, however the enzyme is not required for regulation of CD8-class I MHC binding during T cell development, overview
-
-
-
additional information
?
-
-
ST3Gal-I-/- mice show a profound disregulation of CD8 T cell homeostasis, however the enzyme is not required for regulation of CD8-class I MHC binding during T cell development, overview
-
-
-
additional information
?
-
K9UUI6
the enzyme is alternatively active at pH 4.5 as alpha2,3-sialidase and alpha2,3-trans-sialidase and also shows CMP-N-acetyl-neuraminic hydrolase activity at pH 8.0 when no sialyl acceptor substrate is present
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mn2+
additional information
additional information
-
the enzyme does not require a divalent metal for activity
additional information
-
the enzyme does not require a divalent metal ion for its activity. The addition of MnCl2 or MgCl2 for up to 20 mM does not affect the activity of the enzyme
additional information
the enzyme does not require a divalent metal ion for its activity. The addition of MnCl2 or MgCl2 for up to 20 mM does not affect the activity of the enzyme
additional information
-
divalent metal ions are not required by the alpha2->3-sialyltransferase activity
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
Sodium citrate
-
inhibitory to direct sialylation, using CMP-5-N-acetylneuraminate as a substrate, not inhibitory to reverse sialylation, producing CMP-5-N-acetylneuraminate
additional information
-
either alpha1,3 fucosylation or 6-O-sulfation of the GlcNAc moiety reduces the activity, sialylation of beta1,3Gal in addition to 6-O-sulfation of GlcNAc moiety abolishes the activity
-
additional information
-
overexpression of N-acetylglucosaminyltransferase III significantly inhibits alpha2,3-sialylation
-
additional information
-
the addition of EDTA (1 or 10 mM) does not affect the activity significantly
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
phospholipid/octylglucoside liposomes
-
incorporation into phospholipid/octylglucoside liposomes activates enzyme form A
-
NaCl
1.5fold stimulation in presence of 0.5 M or 0.75 M NaCl
Triton X-100
-
activation, enzyme form A only above critical micelle concentration, not form B
additional information
ST3Gal I expression analysis before and after turpentine oil-induced inflammation, ST3Gal I is upregulated, overview; ST3Gal III expression analysis before and after turpentine oil-induced inflammation, ST3Gal III is upregulated, overview
-
additional information
ST3Gal I expression analysis before and after turpentine oil-induced inflammation, ST3Gal I is upregulated, overview; ST3Gal III expression analysis before and after turpentine oil-induced inflammation, ST3Gal III is upregulated, overview
-
additional information
-
2-mercaptoethanol at 1 or 10 mM does not affect enzyme activity
-
additional information
-
enzyme form A is incorporated into liposomes composed of phosphatidylcholine, cholesterol, and a mixture of phospholipid from the membranes of Golgi apparatus from porcine submaxillary glands. Phosphatidylcholine induces the high activity state of the enzyme. Cholesterol has no effect on the activity of the transferase in liposomes. The phospholipids of the Golgi apparatus appear to increase the Km-value for CMPNeuAc. Enzyme form B, lacking the putative lipid-binding domain is not incorporated into phosphatidylcholine liposomes
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
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
0.5
Galbeta1-3[6-O-(4,4-azo)pentyl]GalNAcalpha-benzyl
-
enzyme from acute myeloid leukemia
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
additional information
additional information
-
influence of liposome incorporation on the Km-value
-
0.54
4-methylumbelliferyl 4-O-beta-D-galactosyl-beta-D-glucoside
-
mutant enzyme E271F/R313Y, in Tris-HCl buffer (100 mM, pH 8.5), at 37°C
0.67
4-methylumbelliferyl 4-O-beta-D-galactosyl-beta-D-glucoside
-
mutant enzyme R313Y, in Tris-HCl buffer (100 mM, pH 8.5), at 37°C
0.71
4-methylumbelliferyl 4-O-beta-D-galactosyl-beta-D-glucoside
-
mutant enzyme E271F, in Tris-HCl buffer (100 mM, pH 8.5), at 37°C
1.4
4-methylumbelliferyl 4-O-beta-D-galactosyl-beta-D-glucoside
-
wild type enzyme, in Tris-HCl buffer (100 mM, pH 8.5), at 37°C
0.32
beta-D-galactosyl-1,3-N-acetylgalactosylamide
-
enzyme form A, with 1% Triton X-100 or enzyme form B
0.37
beta-D-galactosyl-1,3-N-acetylgalactosylamide
-
enzyme form A, with 1% lysophosphatidylcholine or without detergent
0.0137
CMP-N-acetylneuraminate
-
truncated enzyme protein consisting of amino acids 57-340, hST3-DELTA56
0.021
CMP-N-acetylneuraminate
-
truncated enzyme protein consisting of amino acids 26-340, hST3-DELTA25
0.18
CMP-N-acetylneuraminate
-
mutant enzyme E271F, in Tris-HCl buffer (100 mM, pH 8.5), at 37°C
0.25
CMP-N-acetylneuraminate
mutant enzyme T116S, at pH 8.0 and 25°C
0.26
CMP-N-acetylneuraminate
at 37 °C in Tris-HCl (200 mM, pH 7.5)
0.34
CMP-N-acetylneuraminate
-
mutant enzyme E271F/R313Y, in Tris-HCl buffer (100 mM, pH 8.5), at 37°C
0.44
CMP-N-acetylneuraminate
-
wild type enzyme, in Tris-HCl buffer (100 mM, pH 8.5), at 37°C
0.62
CMP-N-acetylneuraminate
-
mutant enzyme R313Y, in Tris-HCl buffer (100 mM, pH 8.5), at 37°C
1.3
CMP-N-acetylneuraminate
-
in Tris-HCl buffer (200 mM, pH 8.0), at 37°C
2.91
CMP-N-acetylneuraminate
-
mutant enzyme R313N/T265S, at pH 8.0 and 22°C
4.09
CMP-N-acetylneuraminate
-
mutant enzyme R313H/T265S, at pH 8.0 and 22°C
0.018
Galbeta1-3GalNAcalpha-O-benzyl
-
truncated enzyme protein consisting of amino acids 26-340, hST3-DELTA25
0.023
Galbeta1-3GalNAcalpha-O-benzyl
-
truncated enzyme protein consisting of amino acids 57-340, hST3-DELTA56
4.9
methyl 2-([4-[(3-[[4-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)
28
methyl 2-([4-[(3-[[4-O-(beta-D-galactopyranosyl)-beta-D-glucopyranosyl]oxy]propyl)amino]-4-oxobutanoyl]amino)benzoate
-
in Tris-HCl buffer (200 mM, pH 8.0), at 37°C
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.2
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
0.53
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
0.25
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)
0.132 - 0.75
methyl 2-([4-[(3-[[4-O-(beta-D-galactopyranosyl)-beta-D-glucopyranosyl]oxy]propyl)amino]-4-oxobutanoyl]amino)benzoate
2 - 8
4-methylumbelliferyl 4-O-beta-D-galactosyl-beta-D-glucoside
-
mutant enzyme E271F, in Tris-HCl buffer (100 mM, pH 8.5), at 37°C
17
4-methylumbelliferyl 4-O-beta-D-galactosyl-beta-D-glucoside
-
mutant enzyme E271F/R313Y, in Tris-HCl buffer (100 mM, pH 8.5), at 37°C
19
4-methylumbelliferyl 4-O-beta-D-galactosyl-beta-D-glucoside
-
mutant enzyme R313Y, in Tris-HCl buffer (100 mM, pH 8.5), at 37°C
47
4-methylumbelliferyl 4-O-beta-D-galactosyl-beta-D-glucoside
-
wild type enzyme, in Tris-HCl buffer (100 mM, pH 8.5), at 37°C
0.088
CMP-N-acetylneuraminate
-
in Tris-HCl buffer (200 mM, pH 8.0), at 37°C
0.12
CMP-N-acetylneuraminate
at 37°C in Tris-HCl (200 mM, pH 7.5)
3 - 6
CMP-N-acetylneuraminate
-
mutant enzyme R313N/T265S, at pH 8.0 and 22°C
3
CMP-N-acetylneuraminate
mutant enzyme T116S, at pH 8.0 and 25°C
19
CMP-N-acetylneuraminate
-
mutant enzyme R313Y, in Tris-HCl buffer (100 mM, pH 8.5), at 37°C
23
CMP-N-acetylneuraminate
-
mutant enzyme E271F/R313Y, in Tris-HCl buffer (100 mM, pH 8.5), at 37°C
26
CMP-N-acetylneuraminate
-
mutant enzyme E271F, in Tris-HCl buffer (100 mM, pH 8.5), at 37°C
32
CMP-N-acetylneuraminate
-
wild type enzyme, in Tris-HCl buffer (100 mM, pH 8.5), at 37°C
44.6
CMP-N-acetylneuraminate
-
mutant enzyme R313H/T265S, at pH 8.0 and 22°C
0.132
methyl 2-([4-[(3-[[4-O-(beta-D-galactopyranosyl)-beta-D-glucopyranosyl]oxy]propyl)amino]-4-oxobutanoyl]amino)benzoate
-
in Tris-HCl buffer (200 mM, pH 8.0), at 37°C
0.75
methyl 2-([4-[(3-[[4-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)
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.048
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
0.47
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
0.025
4-methylumbelliferyl-Lewisx
-
in Tris-HCl buffer (200 mM, pH 8.0), at 37°C
0.017
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)
0.005 - 0.15
methyl 2-([4-[(3-[[4-O-(beta-D-galactopyranosyl)-beta-D-glucopyranosyl]oxy]propyl)amino]-4-oxobutanoyl]amino)benzoate
28
4-methylumbelliferyl 4-O-beta-D-galactosyl-beta-D-glucoside
-
mutant enzyme R313Y, in Tris-HCl buffer (100 mM, pH 8.5), at 37°C
32
4-methylumbelliferyl 4-O-beta-D-galactosyl-beta-D-glucoside
-
mutant enzyme E271F/R313Y, in Tris-HCl buffer (100 mM, pH 8.5), at 37°C
34
4-methylumbelliferyl 4-O-beta-D-galactosyl-beta-D-glucoside
-
wild type enzyme, in Tris-HCl buffer (100 mM, pH 8.5), at 37°C
39
4-methylumbelliferyl 4-O-beta-D-galactosyl-beta-D-glucoside
-
mutant enzyme E271F, in Tris-HCl buffer (100 mM, pH 8.5), at 37°C
0.068
CMP-N-acetylneuraminate
-
in Tris-HCl buffer (200 mM, pH 8.0), at 37°C
0.47
CMP-N-acetylneuraminate
at 37°C in Tris-HCl (200 mM, pH 7.5)
10.9
CMP-N-acetylneuraminate
-
mutant enzyme R313H/T265S, at pH 8.0 and 22°C
12.6
CMP-N-acetylneuraminate
-
mutant enzyme R313N/T265S, at pH 8.0 and 22°C
30
CMP-N-acetylneuraminate
-
mutant enzyme R313Y, in Tris-HCl buffer (100 mM, pH 8.5), at 37°C
69
CMP-N-acetylneuraminate
-
mutant enzyme E271F/R313Y, in Tris-HCl buffer (100 mM, pH 8.5), at 37°C
73
CMP-N-acetylneuraminate
-
wild type enzyme, in Tris-HCl buffer (100 mM, pH 8.5), at 37°C
140
CMP-N-acetylneuraminate
-
mutant enzyme E271F, in Tris-HCl buffer (100 mM, pH 8.5), at 37°C
0.005
methyl 2-([4-[(3-[[4-O-(beta-D-galactopyranosyl)-beta-D-glucopyranosyl]oxy]propyl)amino]-4-oxobutanoyl]amino)benzoate
-
in Tris-HCl buffer (200 mM, pH 8.0), at 37°C
0.15
methyl 2-([4-[(3-[[4-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)
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.15
Galbeta1-3GalNAc
-
reaction with asialoGM1 as acceptor, enzyme form ST3GalA.1
3.1
3-deoxy-Galbeta1-3GalNAcalpha-benzyl
-
reaction with enzyme from acute myeloid leukemia
0.07
asialofetuin
-
reaction with Galbeta1-3GalNAc as acceptor, enzyme form ST3GalA.1
-
0.08
asialofetuin
-
reaction with asialoGM1 as acceptor, enzyme form ST3GalA.1; ,reaction with Galbeta1-3GalNAc as acceptor, enzyme form ST3GalA.2
-
0.11
asialoGM1
-
reaction with Galbeta1-3GalNAc as acceptor, enzyme form ST3GalA.2
0.00015
CTP
-
reaction with 1% Triton X-100 or 1% lysophosphatidylcholine, enzyme form A
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
-
quantitative analysis acceptor and donor substrate specificities of recombinant alpha2,3(O)ST and alpha2,3(N)ST, and of alpha2,3(O)ST from LnCaP cells, detailed overview
additional information
-
enzyme activity in healthy thyroid gland, in Graves' disease and toxic or nontoxic thyroid nodules, overview, lipid-bound sialic acid content and ganglioside profile, overview
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.5 - 9
activity decreases dramatically when pH is below 6.0 or reaches 10.0
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
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
5 - 9
5.2 - 7.2
-
direct sialylation, using CMP-5-N-acetylneuraminate as a substrate
5 - 9
-
about 80% of the optimum activity is observed at pH 5.0 and 9.0. The activity decreases drastically when the pH is below 5.0 or above 9.0. Only about 20% of the optimum activity is observed at pH 4.5 and 11.0
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
enzyme activity is significantly increased in patients with chronic myelogenous leukemia and acute myeloid leukemia
-
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
-
slightly expressed in hepatoma and highly expressed in the surrounding tissue
-
type 1 and type 2 mRNA (differ only in 5'-untranslated region)
-
ST3GalI gene is strongly expressed, ST3GalII gene is weakly expressed
-
type 1 and type 2 mRNA (differ only in 5'-untranslated region)
-
mRNA in restricted brain regions. Very high activity in subiculum and pontine nucleus. High activity in allocortex, granule cell layer of olfactory bulb, granule cell layer of hippocampus, medial habenular field, subcommissural organ
ST3Gal I expression analysis; ST3Gal III expression analysis
-
type 1 and type 2 mRNA (differ only in 5'-untranslated region)
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
a Golgi type II transmembrane glycosyltransferase; a Golgi type II transmembrane glycosyltransferase
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PDB
SCOP
CATH
ORGANISM
UNIPROT
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
40000
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
44027
x * 44027, calculated, x * 43995, MALDI-TOF, x * 40000, SDS-PAGE
50000
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
40000
x * 44027, calculated, x * 43995, MALDI-TOF, x * 40000, SDS-PAGE
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
homotetramer
additional information
?
-
x * 72000, recombinant enzyme fused with N-terminal maltose binding protein, SDS-PAGE; x * 72500, recombinant enzyme fused with N-terminal maltose binding protein, calculated from amino acid sequence
?
-
x * 75000, His-tagged and maltose-binding protein-fused recombinant enzyme, SDS-PAGE; x * 79500, His-tagged and maltose-binding protein-fused recombinant enzyme, calculated from amino acid sequence
?
-
x * 75000, His-tagged and maltose-binding protein-fused recombinant enzyme, SDS-PAGE; x * 79500, His-tagged and maltose-binding protein-fused recombinant enzyme, calculated from amino acid sequence
-
?
x * 44027, calculated, x * 43995, MALDI-TOF, x * 40000, SDS-PAGE
?
x * 43921, MALDI-TOF of truncated enzyme with N-terminal Lys2 to Cys22 deletion
?
-
x * 43921, MALDI-TOF of truncated enzyme with N-terminal Lys2 to Cys22 deletion
-
additional information
alpha2,3-sialyltransferases sequence, recognition fold, and three-dimensional structure, a short, cytoplasmic N-terminal domain is followed by a transmembrane domain, a flexible stem region of variable length and a catalytic domain, molecular docking and modeling, structure-function realationship, potential roles of some residues, comparison to the CstII, an alpha2,3/8 dual activity SiaT, from Campylobacter jejuni, overview
additional information
-
the CMP binding site is located in the deep cleft between the two Rossmann domains, no C-terminal extension that interacts with the N-terminal domain in the DELTA24PmST1 structure
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
glycoprotein
glycoprotein
-
correct glycosylation of the enzyme might play a key role in its folding that may be directly related to the enzymatic activity
glycoprotein
-
the recombinant hST3Gal I polypeptides transiently expressed in COS-7 cells are glycosylated with complex and high mannose type glycans on each of the five potential N-glycosylation sites
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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
-
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY
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
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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)
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
N-terminal truncated form of recombinant alpha2,3-sialyltransferase
-
Ni2+-NTA column chromatography
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
-
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
commercial recombinant preparation
expressed in CHO and HEK-293T 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
-
expression in CHO-K1 cells of truncated protein-A-His-tagged enzyme
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 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 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, 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
expression in CHO-K1 cells of truncated protein-A-His-tagged enzyme
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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
-
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
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
H85A
-
the mutant has very low activity compared to the wild type enzyme
H85F
-
the mutant has very low activity compared to the wild type enzyme
H85Y
-
the mutant has very low activity compared to the wild type enzyme
Y125Q
-
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
H85A
-
the mutant has very low activity compared to the wild type enzyme
-
H85F
-
the mutant has very low activity compared to the wild type enzyme
-
H85Y
-
the mutant has very low activity compared to the wild type enzyme
-
Y125Q
-
the mutant is active but less thermostable than the wild type enzyme
-
T116S
the mutation results in a marked increase in alpha2,3-trans-sialidase side activity
E271F
-
the mutation does not affect alpha2-3-sialyltransferase activity
E271F/R313Y
-
the mutations do not affect alpha2-3-sialyltransferase activity
R313H
-
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
-
the mutations improve the enzyme's activity by a factor of 2.37
R313N/T265S
-
the mutations improve the enzyme's activity by a factor of 2.16
R313Y
T265N
-
the mutant shows 126% activity compared to the wild type enzyme
T265S
-
the mutant shows 116% activity compared to the wild type enzyme
additional information
R313Y
-
the mutation does not affect alpha2-3-sialyltransferase activity
R313Y
-
the mutation improves the enzyme's activity by a factor of 1.25
additional information
-
construction of sialyltransferase mutant strains showing reduced sialylation activities, disruption of lic3B eliminates disialylation of lipopolysaccharides, overview
additional information
-
ST3Gal-I-/- mice show a profound disregulation of CD8 T cell homeostasis, however, ST3Gal-I deficiency does not alter the pattern of CD8 noncognate binding by thymocytes, overview
additional information
-
ST3Gal-I-/- mice show a profound disregulation of CD8 T cell homeostasis, however, ST3Gal-I deficiency does not alter the pattern of CD8 noncognate binding by thymocytes, overview
-
additional information
-
truncated protein lacking N-terminal amino acids 2-24 is more soluble without detergent than wild-type
additional information
-
truncated protein lacking N-terminal amino acids 2-24 is more soluble without detergent than wild-type
-
additional information
expression and purification of active truncated enzyme with N-terminal Lys2 to Cys22 deletion
additional information
-
expression and purification of active truncated enzyme with N-terminal Lys2 to Cys22 deletion
-
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
drug development
-
ST3Gal III can serve as a therapeutic target of taxol therapy
medicine
synthesis
medicine
-
a significant level of reverse sialylation, i.e. synthesis of CMP-5-N-acetylneuraminate from CMP, is noted in prostate cancer cell lines LNCaP and PC-3
medicine
the enzyme is a drug target for modulating leukocyte trafficking in human disorders, including autoimmune diseases and cancer
synthesis
-
chemoenzymatic synthesis of sialylated oligosaccharides for their evaluation in a polysialyltransferase assay
synthesis
-
use of glycan microarrays for high-throughput acceptor specificity screening of recombinant sialyltransferases. Donor substrate is cytidine 5'-monophospho-N-acteylneuraminate, which has been biotinylated at position 9. Human enzyme broadly sialylates oligosaccharides of types 1-4
synthesis
-
use of glycan microarrays for high-throughput acceptor specificity screening of recombinant sialyltransferases. Donor substrate is cytidine 5'-monophospho-N-acetylneuraminate, which has been biotinylated at position 9. Rat enzyme ST3Gal-III tolerates fucosylated acceptors such as Lewis
synthesis
-
use of glycan microarrays for high-throughput acceptor specificity screening of recombinant sialyltransferases. Donor substrate is cytidine 5'-monophospho-N-acteylneuraminate, which has been biotinylated at position 9. Porcine enzyme sialylates ganglio-oligosaccharides and core 2 O-glycans
synthesis
-
in vitro glycosylation of human recombinant erythropoietin by using recombinant human N-acetylglucosaminyltransferases and alpha2,3-sialyltransferase for conversion into complex-type glycan with terminal sialic acid. Although glycosylation can be confirmed, the resulting erythropoietin does not lead to a significant increase in the number of reticulocytes when injected into mice
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