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Ligand Gal-beta-1,3-GlcNAc-O-(CH2)8CO2CH3 Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Basic Ligand Information Molecular Structure
C2 4 H4 3 NO1 3
Gal-beta-1,3-GlcNAc-O-(CH2)8CO2CH3
QCWPROARBPOGDI-CYABAIRNSA-N
8-(methoxycarbonyl)octyl beta-D-galactopyranosyl-(1->3)-2-acetamido-2-deoxy-beta-D-glucopyranoside, Galbeta-(1-3)-GlcNAc-O-(CH2)8COOCH3, Galbeta-1,3-GlcNAc-beta-O-(CH2)8COOCH3, Galbeta1,3GlcNAc-O(CH2)8CO2CH3
Roles as Enzyme Ligand
Substrate in Enzyme-catalyzed Reactions (2 results)
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GDP-fucose + Gal-beta-1,3-GlcNAc-O-(CH2)8CO2CH3 = GDP + Gal-beta-1,3[alpha-fucosyl(1,4)]-GLCNAc-O-(CH2)8CO2CH3
-
GDP-beta-L-fucose + Galbeta1,3GlcNAc-O(CH2)8CO2CH3 = ?
-
Enzyme Kinetic Parameters
kcat Value (Turnover Number) (3 results)
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1.1
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truncated enzyme UA948(1-428)
KM Value (6 results)
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5.7
-
truncated enzyme UA948(1-428)
9.7
-
chimeric FucT UA948(1-360)11639(360-478)
13.3
-
full-length enzyme
20.8
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chimeric FucT 11639(347CNDAHYSALH)
22.7
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chimeric FucT UA948(345DNPFIFC)
References & Links Literature References (3)
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C-terminal amino acids of Helicobacter pylori alpha1,3/4 fucosyltransferases determine type I and type II transfer
2003
Ma, B.; Wang, G.; Palcic, M.M.; Hazes, B.; Taylor, D.E.
J. Biol. Chem.
278
21893-21900
Molecular cloning and functional expression of a novel Helicobacter pylori alpha-1,4 fucosyltransferase
2005
Rabbani, S.; Miksa, V.; Wipf, B.; Ernst, B.
Glycobiology
15
1076-1083
Purification, kinetic characterization, and mapping of the minimal catalytic domain and the key polar goups of Helicobacter pylori alpha-(1,3/1,4)-fucosyltransferases
2006
Ma, B.; Audette, G.F.; Lin, S.; Palcic, M.M.; Hazes, B.; Taylor, D.E.
J. Biol. Chem.
281
6385-6394
Links to other databases for Gal-beta-1,3-GlcNAc-O-(CH2)8CO2CH3