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chondroitin galactosaminyltransferase
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acetylgalactosaminyltransferase, uridine diphosphoacetylgalactosamine-chondroitin, I
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chondroitin beta1,4-N-acetylgalactosaminyltransferase-1
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chondroitin galactosaminyltransferase
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chondroitin sulfate beta-1,4-N-acetylgalactosaminyltransferase-1 ChGn-1
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chondroitin sulfate N-acetylgalactosaminyltransferase 1
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chondroitin sulfate N-acetylgalactosaminyltransferase-1
chondroitin sulphate N-acetylgalactosaminyltransferase 1
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glucuronylgalactosylproteoglycan beta-1,4-N-acetylgalactosaminyltransferase
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N-acetylgalactosamineT-II
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N-acetylgalactosaminyltransferase I
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uridine diphosphoacetylgalactosamine-chondroitin acetylgalactosaminyltransferase I
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chondroitin sulfate N-acetylgalactosaminyltransferase-1
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chondroitin sulfate N-acetylgalactosaminyltransferase-1
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CSGalNAcT-1
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CSGalNAcT-1
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chondroitin sulfate N-acetylgalactosaminyltransferase-1
additional information
the enzyme has also N-acetylgalactosaminyltransferase II activity, EC 2.4.1.175, substrates sulfated and unsulfated chondroitin oligo- and polysaccharides
additional information
the enzyme has also N-acetylgalactosaminyltransferase II activity, EC 2.4.1.175, substrates chondroitin oligo- and polysaccharides
additional information
the enzyme has also N-acetylgalactosaminyltransferase II activity, EC 2.4.1.175, substrates chondroitin oligo- and polysaccharides
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UDP-N-acetyl-D-galactosamine + beta-D-glucuronyl-(1->3)-D-galactosyl-proteoglycan
UDP + N-acetyl-D-galactosaminyl-(1->4)-beta-D-glucuronyl-(1->3)-beta-D-galactosyl-proteoglycan
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UDP-N-acetyl-D-galactosamine + beta-D-glucuronyl-1,3-beta-D-galactosyl-1,3-beta-D-galactosyl-1,4-beta-D-xylosyl-1-O-(Gly)Ser-(Gly-Glu)
UDP + N-acetyl-D-galactosamine-1,4-beta-D-glucuronyl-1,3-beta-D-galactosyl-1,3-beta-D-galactosyl-1,4-beta-D-xylosyl-1-O-(Gly)Ser-(Gly-Glu)
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UDP-N-acetyl-D-galactosamine + beta-D-glucuronyl-1,3-beta-D-galactosyl-1,3-beta-D-galactosyl-1,4-beta-D-xylosyl-1-O-Ser
UDP + N-acetyl-D-galactosamine-1,4-beta-D-glucuronyl-1,3-beta-D-galactosyl-1,3-beta-D-galactosyl-1,4-beta-D-xylosyl-1-O-Ser
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UDP-N-acetyl-D-galactosamine + beta-D-glucuronyl-1,3-beta-D-galactosyl-1,3-beta-D-galactosyl-1,4-beta-D-xylosyl-1-O-Ser-peptide
UDP + N-acetyl-D-galactosamine-1,4-beta-D-glucuronyl-1,3-beta-D-galactosyl-1,3-beta-D-galactosyl-1,4-beta-D-xylosyl-1-O-Ser-peptide
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UDP-N-acetyl-D-galactosamine + beta-D-glucuronyl-1,3-beta-D-galactosyl-1-O-C2H4-NH-benzyloxycarbonyl
UDP + N-acetyl-D-galactosamine-1,4-beta-D-glucuronyl-1,3-beta-D-galactosyl-1-O-C2H4-NH-benzyloxycarbonyl
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UDP-N-acetyl-D-galactosamine + glucuronylgalactosyl glycosides
UDP + N-acetyl-D-galactosaminyl-1,4-beta-D-glucuronylgalactosyl glycosides
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UDP-N-acetyl-D-galactosamine + beta-D-glucuronyl-(1->3)-D-galactosyl-proteoglycan
UDP + N-acetyl-D-galactosaminyl-(1->4)-beta-D-glucuronyl-(1->3)-beta-D-galactosyl-proteoglycan
UDP-N-acetyl-D-galactosamine + beta-D-glucuronyl-(1->3)-D-galactosyl-proteoglycan
UDP + N-acetyl-D-galactosaminyl-(1->4)-beta-D-glucuronyl-(1->3)-beta-D-galactosylproteoglycan
UDP-N-acetyl-D-galactosamine + beta-D-glucuronyl-1,3-beta-D-galactosyl-1,3-beta-D-galactosyl-beta-D-xylose-O-methoxyphenyl
UDP + N-acetyl-D-galactosamine-1,4-beta-D-glucuronyl-1,3-beta-D-galactosyl-1,3-beta-D-galactosyl-beta-D-xylose-O-methoxyphenyl
UDP-N-acetyl-D-galactosamine + beta-D-glucuronyl-1,3-beta-D-galactosyl-1-O-C2H4-NH-benzyloxycarbonyl
UDP + N-acetyl-D-galactosamine-1,4-beta-D-glucuronyl-1,3-beta-D-galactosyl-1-O-C2H4-NH-benzyloxycarbonyl
UDP-N-acetyl-D-galactosamine + glucuronylgalactosyl glycosides
UDP + N-acetyl-D-galactosaminyl-1,4-beta-D-glucuronylgalactosyl glycosides
UDP-N-acetyl-D-galactosamine + glucuronylgalactosyl glycosides
UDP + N-acetyl-D-galactosaminylglucuronylgalactosyl glycosides
additional information
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GalNAcT activity of the recombinant enzyme is determined using a trisaccharide analogue of the linkage region linked to a chromophoric aglycone, GlcA-beta1,3-Gal-beta1,3-Gal-O-methoxyphenyl, i.e. GlcA-Gal-Gal-OMP, as a acceptor substrate, Km is 3.8 mM, and with only the trisaccharide GlcA-beta1,3-Gal-beta1,3-Gal, Km 3.39 mM, no activity with Gal-Gal-OMP. The enzyme activity is even higher with 4- and 6-sulfated GlcA-Gal-Gal-OMP, kM values are 0.6 mM and 1.0 mm, respectively, no activity with 6-disulfated GlcA-Gal-Gal-OMP
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UDP-N-acetyl-D-galactosamine + beta-D-glucuronyl-(1->3)-D-galactosyl-proteoglycan
UDP + N-acetyl-D-galactosaminyl-(1->4)-beta-D-glucuronyl-(1->3)-beta-D-galactosyl-proteoglycan
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UDP-N-acetyl-D-galactosamine + beta-D-glucuronyl-(1->3)-D-galactosyl-proteoglycan
UDP + N-acetyl-D-galactosaminyl-(1->4)-beta-D-glucuronyl-(1->3)-beta-D-galactosyl-proteoglycan
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UDP-N-acetyl-D-galactosamine + beta-D-glucuronyl-(1->3)-D-galactosyl-proteoglycan
UDP + N-acetyl-D-galactosaminyl-(1->4)-beta-D-glucuronyl-(1->3)-beta-D-galactosyl-proteoglycan
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UDP-N-acetyl-D-galactosamine + beta-D-glucuronyl-(1->3)-D-galactosyl-proteoglycan
UDP + N-acetyl-D-galactosaminyl-(1->4)-beta-D-glucuronyl-(1->3)-beta-D-galactosylproteoglycan
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UDP-N-acetyl-D-galactosamine + beta-D-glucuronyl-(1->3)-D-galactosyl-proteoglycan
UDP + N-acetyl-D-galactosaminyl-(1->4)-beta-D-glucuronyl-(1->3)-beta-D-galactosylproteoglycan
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UDP-N-acetyl-D-galactosamine + beta-D-glucuronyl-1,3-beta-D-galactosyl-1,3-beta-D-galactosyl-beta-D-xylose-O-methoxyphenyl
UDP + N-acetyl-D-galactosamine-1,4-beta-D-glucuronyl-1,3-beta-D-galactosyl-1,3-beta-D-galactosyl-beta-D-xylose-O-methoxyphenyl
i.e. linkage tetrasaccharide, synthetic substrate
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UDP-N-acetyl-D-galactosamine + beta-D-glucuronyl-1,3-beta-D-galactosyl-1,3-beta-D-galactosyl-beta-D-xylose-O-methoxyphenyl
UDP + N-acetyl-D-galactosamine-1,4-beta-D-glucuronyl-1,3-beta-D-galactosyl-1,3-beta-D-galactosyl-beta-D-xylose-O-methoxyphenyl
best acceptor substrate together with chondroitin polysaccharide
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UDP-N-acetyl-D-galactosamine + beta-D-glucuronyl-1,3-beta-D-galactosyl-1,3-beta-D-galactosyl-beta-D-xylose-O-methoxyphenyl
UDP + N-acetyl-D-galactosamine-1,4-beta-D-glucuronyl-1,3-beta-D-galactosyl-1,3-beta-D-galactosyl-beta-D-xylose-O-methoxyphenyl
transfers GalNAc to GlcA at the non-reducing terminus of the linkage tetrasacharide
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UDP-N-acetyl-D-galactosamine + beta-D-glucuronyl-1,3-beta-D-galactosyl-1-O-C2H4-NH-benzyloxycarbonyl
UDP + N-acetyl-D-galactosamine-1,4-beta-D-glucuronyl-1,3-beta-D-galactosyl-1-O-C2H4-NH-benzyloxycarbonyl
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UDP-N-acetyl-D-galactosamine + beta-D-glucuronyl-1,3-beta-D-galactosyl-1-O-C2H4-NH-benzyloxycarbonyl
UDP + N-acetyl-D-galactosamine-1,4-beta-D-glucuronyl-1,3-beta-D-galactosyl-1-O-C2H4-NH-benzyloxycarbonyl
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UDP-N-acetyl-D-galactosamine + glucuronylgalactosyl glycosides
UDP + N-acetyl-D-galactosaminyl-1,4-beta-D-glucuronylgalactosyl glycosides
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UDP-N-acetyl-D-galactosamine + glucuronylgalactosyl glycosides
UDP + N-acetyl-D-galactosaminyl-1,4-beta-D-glucuronylgalactosyl glycosides
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UDP-N-acetyl-D-galactosamine + glucuronylgalactosyl glycosides
UDP + N-acetyl-D-galactosaminyl-1,4-beta-D-glucuronylgalactosyl glycosides
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UDP-N-acetyl-D-galactosamine + glucuronylgalactosyl glycosides
UDP + N-acetyl-D-galactosaminylglucuronylgalactosyl glycosides
involved in chondroitin initiation and elongation
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UDP-N-acetyl-D-galactosamine + glucuronylgalactosyl glycosides
UDP + N-acetyl-D-galactosaminylglucuronylgalactosyl glycosides
involved in the biosynthesis of chodroitin sulfate. Key enzyme activity for the initiation of chondroitin and dermatan sulfates, transferring GalNAc to the GlcA-Gal-Gal-Xyl-Ser core.
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UDP-N-acetyl-D-galactosamine + beta-D-glucuronyl-(1->3)-D-galactosyl-proteoglycan
UDP + N-acetyl-D-galactosaminyl-(1->4)-beta-D-glucuronyl-(1->3)-beta-D-galactosyl-proteoglycan
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UDP-N-acetyl-D-galactosamine + beta-D-glucuronyl-(1->3)-D-galactosyl-proteoglycan
UDP + N-acetyl-D-galactosaminyl-(1->4)-beta-D-glucuronyl-(1->3)-beta-D-galactosyl-proteoglycan
UDP-N-acetyl-D-galactosamine + beta-D-glucuronyl-(1->3)-D-galactosyl-proteoglycan
UDP + N-acetyl-D-galactosaminyl-(1->4)-beta-D-glucuronyl-(1->3)-beta-D-galactosylproteoglycan
UDP-N-acetyl-D-galactosamine + glucuronylgalactosyl glycosides
UDP + N-acetyl-D-galactosaminylglucuronylgalactosyl glycosides
UDP-N-acetyl-D-galactosamine + beta-D-glucuronyl-(1->3)-D-galactosyl-proteoglycan
UDP + N-acetyl-D-galactosaminyl-(1->4)-beta-D-glucuronyl-(1->3)-beta-D-galactosyl-proteoglycan
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UDP-N-acetyl-D-galactosamine + beta-D-glucuronyl-(1->3)-D-galactosyl-proteoglycan
UDP + N-acetyl-D-galactosaminyl-(1->4)-beta-D-glucuronyl-(1->3)-beta-D-galactosyl-proteoglycan
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UDP-N-acetyl-D-galactosamine + beta-D-glucuronyl-(1->3)-D-galactosyl-proteoglycan
UDP + N-acetyl-D-galactosaminyl-(1->4)-beta-D-glucuronyl-(1->3)-beta-D-galactosyl-proteoglycan
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UDP-N-acetyl-D-galactosamine + beta-D-glucuronyl-(1->3)-D-galactosyl-proteoglycan
UDP + N-acetyl-D-galactosaminyl-(1->4)-beta-D-glucuronyl-(1->3)-beta-D-galactosylproteoglycan
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UDP-N-acetyl-D-galactosamine + beta-D-glucuronyl-(1->3)-D-galactosyl-proteoglycan
UDP + N-acetyl-D-galactosaminyl-(1->4)-beta-D-glucuronyl-(1->3)-beta-D-galactosylproteoglycan
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UDP-N-acetyl-D-galactosamine + glucuronylgalactosyl glycosides
UDP + N-acetyl-D-galactosaminylglucuronylgalactosyl glycosides
involved in chondroitin initiation and elongation
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UDP-N-acetyl-D-galactosamine + glucuronylgalactosyl glycosides
UDP + N-acetyl-D-galactosaminylglucuronylgalactosyl glycosides
involved in the biosynthesis of chodroitin sulfate. Key enzyme activity for the initiation of chondroitin and dermatan sulfates, transferring GalNAc to the GlcA-Gal-Gal-Xyl-Ser core.
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(E)-2-hydroxy-3-isopentyl-4-methoxy-6-styrylbenzoic acid
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(E)-2-hydroxy-4-methoxy-3-(3-methylbut-2-enyl)-6-(2-phenylprop-1-enyl)benzoic acid
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(E)-2-hydroxy-4-methoxy-3-prenyl-6-(2-(thiophen-2-yl)vinyl)-benzoic acid
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(E)-3-(3,7-dimethylocta-2,6-dienyl)-2-hydroxy-4-methoxy-6-phenethylbenzoic acid
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(E)-3-c-6-hydroxy-4-methoxy-5-prenyl-2-styrylbenzoic acid
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(E)-3-methoxy-4-(3-methylbut-2-enyl)-5-styrylphenol
i.e. longistyline C
(E)-6-(2-chlorostyryl)-2-hydroxy-4-methoxy-3-prenylbenzoic acid
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(E)-6-(2-methylstyryl)-2-hydroxy-4-methoxy-3-prenylbenzoic acid
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(E)-6-(3-methylstyryl)-2-hydroxy-4-methoxy-3-prenylbenzoic acid
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(E)-6-(4-fluorostyryl)-2-hydroxy-4-methoxy-3-prenylbenzoic acid
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(E)-6-(4-hydroxystyryl)-2-hydroxy-4-methoxy-3-prenylbenzoic acid
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(E)-6-(4-methylstyryl)-2-hydroxy-4-methoxy-3-prenylbenzoic acid
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(E)-6-(but-1-enyl)-2-hydroxy-4-methoxy-3-prenylbenzoic acid
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(E)-ethyl 2-hydroxy-4-methoxy-3-(3-methylbut-2-enyl)-6-styrylbenzoate
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(E)-isopropyl 2-hydroxy-4-methoxy-3-(3-methylbut-2-enyl)-6-styrylbenzoate
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(E)-methyl 2-hydroxy-3-isopentyl-4-methoxy-6-styrylbenzoate
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(E)-methyl 2-hydroxy-4-methoxy-3-(3-methylbut-2-enyl)-6-(2-phenylprop-1-enyl)benzoate
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(E)-methyl 2-hydroxy-4-methoxy-3-prenyl-6-(2-(thiophen-2-yl)-vinyl)benzoate
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(E)-methyl 6-(2-chlorostyryl)-2-hydroxy-4-methoxy-3-prenylbenzoate
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(E)-methyl 6-(2-methylstyryl)-2-hydroxy-4-methoxy-3-prenylbenzoate
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(E)-methyl 6-(3-methylstyryl)-2-hydroxy-4-methoxy-3-prenylbenzoate
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(E)-methyl 6-(4-(tert-butyldimethylsilyloxy)styryl)-2-hydroxy-4-methoxy-3-prenylbenzoate
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(E)-methyl 6-(4-fluorostyryl)-2-hydroxy-4-methoxy-3-prenylbenzoate
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(E)-methyl 6-(4-hydroxystyryl)-2-hydroxy-4-methoxy-3-prenylbenzoate
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(E)-methyl 6-(4-methylstyryl)-2-hydroxy-4-methoxy-3-prenylbenzoate
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(E)-methyl 6-(but-1-enyl)-2-hydroxy-4-methoxy-3-prenylbenzoate
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(E)-methyl 6-styryl-2-hydroxy-4-methoxy-3-prenylbenzoate
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(E)-N-cyclopropyl-2-hydroxy-4-methoxy-3-(3-methylbut-2-enyl)-6-styrylbenzamide
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(E)-tert-butyl 2-hydroxy-4-methoxy-3-(3-methylbut-2-enyl)-6-styrylbenzoate
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2-hydroxy-3-isopentyl-4-methoxy-6-phenethylbenzoic acid
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2-hydroxy-4-methoxy-3-prenyl-6-((1E,3E)-4-phenylbuta-1,3-dienyl)benzoic acid
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2-hydroxy-4-methoxy-3-prenyl-6-phenethylbenzoic acid
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cajanine
cajanine is a stilbenic component isolated from Cajanus cajan, it is identified as a potent hepatitis C virus (HCV) inhibitor by phenotypic screening with EC50 of 0.00317 mM. Cajanine inhibits HCV infection by targeting cellular CSGalNAcT-1 protein destabilizing the protein. Cajanine does not inhibit HCV replication at the replicative steps of HCV life cycle. CSGalNAcT-1 is important to support HCV replication at the early stage. Structure-activity relationships and the mechanism of action, and analysis of cajanine derivatives, EC50 values, overview. Cajanine might inhibit HCV replication at early steps of the viral life cycle via downregulating of cellular CSGalNAcT-1
methyl 2-hydroxy-4-methoxy-3-prenyl-6-((1E,3E)-4-phenylbuta-1,3-dienyl)benzoate
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methyl 2-hydroxy-4-methoxy-3-prenyl-6-phenethylbenzoate
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additional information
2-hydroxy-4-methoxy-6-[(E)-2-phenylethenyl]benzoic acid is not inhibitory
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Carcinogenesis
Glycosyltransferase expression in human colonic tissue examined by oligonucleotide arrays.
Carcinoma
Glycosylation is an Androgen-Regulated Process Essential for Prostate Cancer Cell Viability.
Hepatitis C
Design and Synthesis of Cajanine Analogues against Hepatitis C Virus through Down-Regulating Host Chondroitin Sulfate N-Acetylgalactosaminyltransferase 1.
Hereditary Sensory and Motor Neuropathy
Chondroitin beta-1,4-N-acetylgalactosaminyltransferase-1 missense mutations are associated with neuropathies.
Infections
Chondroitin sulfate N-acetylgalactosaminyltransferase-2 contributes to the replication of infectious bursal disease virus via interaction with the capsid protein VP2.
Intervertebral Disc Degeneration
Upregulation of glycosaminoglycan synthesis by Neurotropin in nucleus pulposus cells via stimulation of chondroitin sulfate N-acetylgalactosaminyltransferase 1: A new approach to attenuation of intervertebral disc degeneration.
Joint Instability
Biallelic CSGALNACT1-mutations cause a mild skeletal dysplasia.
Joint Instability
Chondroitin Sulfate N-acetylgalactosaminylTransferase-1 (CSGalNAcT-1) Deficiency Results in a Mild Skeletal Dysplasia and Joint Laxity.
Kashin-Beck Disease
Abnormal expression of chondroitin sulphate N-acetylgalactosaminyltransferase 1 and Hapln-1 in cartilage with Kashin-Beck disease and primary osteoarthritis.
Language Development Disorders
CSGALNACT1-congenital disorder of glycosylation: A mild skeletal dysplasia with advanced bone age.
Neoplasm Metastasis
Glycosyltransferase expression in human colonic tissue examined by oligonucleotide arrays.
Neoplasms
Polymorphisms Within the RET Proto-Oncogene and Risk of Sporadic Medullary Thyroid Carcinoma.
Osteoarthritis
Abnormal expression of chondroitin sulphate N-acetylgalactosaminyltransferase 1 and Hapln-1 in cartilage with Kashin-Beck disease and primary osteoarthritis.
Polyneuropathies
Chondroitin beta-1,4-N-acetylgalactosaminyltransferase-1 missense mutations are associated with neuropathies.
Prostatic Neoplasms
Glycosylation is a global target for androgen control in prostate cancer cells.
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metabolism
the first step (GalNAc transfer) of chondroitin sulfate (CS) backbone synthesis is performed by at least two isoforms, CSGALNACT1 (T1) and CSGALNACT2 (T2), which are expressed in different organs, CS metabolism, roles of CS and perineuronal nets (PNNs) in brain function from the perspective of CS synthesis, overview
malfunction
missense mutations are found in gene ChGn-1 in exon 5, H234R, and exon 10, M509R, respectively, in two patients with neuropathy. The mutations might be associated with the pathogenetic mechanisms of the peripheral neuropathies
malfunction
the enzyme is downregulated in Kashin-Beck disease (KBD), an endemic degenerative osteoarthritis, and in primary osteoarthritis, both associated with extracellular matrix degradation. Enzyme CSGalNAcT-1 may be involved in the damage of articular cartilage of Kashin-Beck disease and osteoarthritis by regulating Hapln-1 in the Wnt/beta-catenin signalling pathway. Alterations of involved enzyme expressions in CSGalNAcT gene network in case of Kashin-Beck disease and osteoarthritis
malfunction
after silencing of endogenous CSGalNAcT-1 with specific siRNA, the intracellular hepatitis C virus (HCV) RNA load is largely reduced, and the HCV core protein is declined as well
malfunction
chondroitin sulfate N-acetylgalactosaminyltransferase-1 (CSGalNAcT-1) deficiency results in a mild skeletal dysplasia and joint laxity
malfunction
saturating concentrations of rVAR2 inhibit downstream integrin signaling, which is mimicked by knockdown of the core CS synthesis enzymes beta-1,3-glucuronyltransferase 1 (B3GAT1) and chondroitin sulfate N-acetylgalactosaminyltransferase 1 (CSGALNACT1). rVAR2 inhibits cellular migration, invasion, and anchorage independent growth in cancer. rVAR2 interacts with chondroitin sulfate glycosaminoglycan (ofCS)-modified proteoglycans
metabolism
CSGalNAcT-1 plays a role in chondroitin sulfate and dermatan sulfate synthesis
metabolism
the first step (GalNAc transfer) of chondroitin sulfate (CS) backbone synthesis is performed by at least two isoforms, CSGALNACT1 (T1) and CSGALNACT2 (T2), which are expressed in different organs, CS metabolism, roles of CS and perineuronal nets (PNNs) in brain function from the perspective of CS synthesis, overview
physiological function
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chondroitin sulfate N-acetylgalactosaminyltransferase-1, CSGalNAcT-1, is involved in chondroitin sulfate initiation, but not in elongation
physiological function
ChGn-1 is a key enzyme for production of chondroitin sulfate proteoglycans The clinical course of multiple sclerosis is influenced by the level of expression of the ChGn-1 gene. Chondroitin sulfate proteoglycans are a constituent of the matrix of the central nervous system (CNS), likely participating as regulatory molecules in the process of demyelination, remyelination, axonaldegeneration and regeneration in the CNS
physiological function
chondroitin sulfate N-acetylgalactosaminyl-transferase-1 is an essential enzyme in chondroitin sulfate metabolism and participates in chondroitin sulfate chain formation of aggrecan, and plays an important role in degenerative extracellular matrix of cartilage
physiological function
chondroitin sulfate N-acetylgalactosaminyltransferase 1 initiates synthesis of chondroitin sulfate side chains attached to a core protein of aggrecan, which is a predominant disc matrix component
physiological function
CSGalNAcT-1 is essential for hepatitis C virus (HCV) replication in human cells
physiological function
CSGALNACT1 encodes chondroitin sulfate N-acetylgalactosaminyltransferase-1 (CSGalNAcT-1, ChGn-1), which initiates chondroitin sulfate (CS) chain biosynthesis on the so-called GAG-protein linker region tetrasaccharide
physiological function
the enzymes beta-1,3-glucuronyltransferase 1 (B3GAT1) and chondroitin sulfate N-acetylgalactosaminyltransferase 1 (CSGALNACT1) are key players in the core chondroitin sulfate (CS) synthesis. Oncofetal chondroitin sulfate glycosaminoglycans (ofCSs) are key players in integrin signaling and tumor cell motility, overview
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H234R
naturally occuring mutation in exon 5 of gene ChGn1, the mutant shows neuropathy, Bells palsy and/or hereditary motor and sensory neuropathy, the mutant enzyme is inactive
M509R
naturally occuring mutation in exon 10 of gene ChGn1, the mutant shows neuropathy, Bells palsy and/or hereditary motor and sensory neuropathy, the mutant enzyme is inactive
P384R
site-directed mutagenesis, almost inactive mutant
S126L
naturally occuring inactive ChGN1 mutant
additional information
bi-allelic loss-of-function mutations in CSGALNACT1 produce a skeletal dysplasia reminiscent of the skeletal dysplasia of Csgalnact1-/- mice, and adds to the genetic heterogeneity of Desbuquois dysplasia (DD)
additional information
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bi-allelic loss-of-function mutations in CSGALNACT1 produce a skeletal dysplasia reminiscent of the skeletal dysplasia of Csgalnact1-/- mice, and adds to the genetic heterogeneity of Desbuquois dysplasia (DD)
additional information
saturating concentrations of rVAR2 inhibit downstream integrin signaling, which is mimicked by knockdown of the core chondroitin sulfate (CS) synthesis enzymes beta-1,3-glucuronyltransferase 1 (B3GAT1) and chondroitin sulfate N-acetylgalactosaminyltransferase 1 (CSGALNACT1) via siRNA. The oncofetal chondroitin sulfate glycosaminoglycans (ofCS) modification is highly expressed in both human and murine metastatic lesions in situ and pre-incubation or early intravenous treatment of tumor cells with rVAR2-inhibited seeding and spreading of tumor cells in mice
additional information
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saturating concentrations of rVAR2 inhibit downstream integrin signaling, which is mimicked by knockdown of the core chondroitin sulfate (CS) synthesis enzymes beta-1,3-glucuronyltransferase 1 (B3GAT1) and chondroitin sulfate N-acetylgalactosaminyltransferase 1 (CSGALNACT1) via siRNA. The oncofetal chondroitin sulfate glycosaminoglycans (ofCS) modification is highly expressed in both human and murine metastatic lesions in situ and pre-incubation or early intravenous treatment of tumor cells with rVAR2-inhibited seeding and spreading of tumor cells in mice
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DNA sequence determination, genomic organization and chromosome localization, functional expression as soluble protein fused to protein A IgG-binding domain in COS-1 cells, secretion into the medium
DNA sequence determination and analysis, expression of a truncated form, consisting of the putative catalytic domain, in Spodoptera frugiperda Sf21 insect cells as a soluble FLAG-tagged protein
DNA sequence determination, genomic organization and chromosome localization, functional expression as soluble protein fused to protein A IgG-binding domain in COS-1 cells, secretion into the medium
gene ChGn1, expression of His-tagged wild-type ChGn-1 and soluble mutant enzymes in COS-1 cells, secretion to the medium
gene CSGALNACT1, genotyping and polymorphisms, recombinant expression of His-tagged soluble forms of wild-type ChGn-1 and S126LChGn-1 mutant in COS-1 cells, the enzymes are secreted
gene CSGALNACT1, quantitative real-time PCR enzyme expression analysis
gene CSGalNAcT1, recombinant expression of wild-type and mutant FLAG-tagged CSGalNAcT-1 enzymes in COS-7 cells
LTC cells from rat chondrosarcoma are transfected with chondroitin sulfate N-acetylgalactosaminyltransferase-1 expression plasmid (about 80fold increase of chondroitin sulfate N-acetylgalactosaminyltransferase-1 RNA), metabolic albeling with [35S]sulfate show up to a 2.2fold increase in chondroitin sulfate levels in these cells, but the mRNA level of aggrecan core protein does not change. Aggrecan obained from chondroitin sulfate N-acetylgalactosaminyltransferase-1 overexpressing cells contain a larger amount of chondroitin sulfate, but the chondroitin sulfate chain length is similar to mock-transfected cells.
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Myc-tagged CSGalNAcT-1 expression in HeLa cells
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gene CSGALNACT1, quantitative real-time PCR enzyme expression analysis
gene CSGALNACT1, quantitative real-time PCR enzyme expression analysis
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Gotoh, M.; Sato, T.; Akashima, T.; Iwasaki, H.; Kameyama, A.; Mochizuki, H.; Yada, T.; Inaba, N.; Zhang, Y.; Kikuchi, N.; Kwon, Y.D.; Togayachi, A.; Kudo, T.; Nishihara, S.; Watanabe, H.; Kimata, K.; Narimatsu, H.
Enzymatic synthesis of chondroitin with a novel chondroitin sulfate N-acetylgalactosaminyltransferase that transfers N-acetylgalactosamine to glucuronic acid in initiation and elongation of chondroitin sulfate synthesis
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38189-38196
2002
Homo sapiens (Q8TDX6)
brenda
Uyama, T.; Kitagawa, H.; Tamura, J.I.; Sugahara, K.
Molecular cloning and expression of human chondroitin N-acetylgalactosaminyltransferase. The key enzyme for chain initiation and elongation of chondroitin/dermatan sulfate on the protein linkage region tetrasaccharide shared by heparin/heparan sulfate
J. Biol. Chem.
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8841-8846
2002
Homo sapiens (Q8TDX6)
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Uyama, T.; Kitagawa, H.; Tanaka, J.; Tamura, J.i.; Ogawa, T.; Sugahara, K.
Molecular cloning and expression of a second chondroitin N-acetylgalactosaminyltransferase involved in the initiation and elongation of chondroitin/dermatan sulfate
J. Biol. Chem.
278
3072-3078
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Homo sapiens (Q8N6G5), Homo sapiens (Q8TDX6)
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Sakai, K.; Kimata, K.; Sato, T.; Gotoh, M.; Narimatsu, H.; Shinomiya, K.; Watanabe, H.
Chondroitin sulfate N-acetylgalactosaminyltransferase-1 plays a critical role in chondroitin sulfate synthesis in cartilage
J. Biol. Chem.
282
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2007
Homo sapiens, Mus musculus
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Gulberti, S.; Jacquinet, J.C.; Chabel, M.; Ramalanjaona, N.; Magdalou, J.; Netter, P.; Coughtrie, M.W.; Ouzzine, M.; Fournel-Gigleux, S.
Chondroitin sulfate N-acetylgalactosaminyltransferase-1 (CSGalNAcT-1) involved in chondroitin sulfate initiation: impact of sulfation on activity and specificity
Glycobiology
22
561-571
2012
Homo sapiens
brenda
Saigoh, K.; Izumikawa, T.; Koike, T.; Shimizu, J.; Kitagawa, H.; Kusunoki, S.
Chondroitin beta-1,4-N-acetylgalactosaminyltransferase-1 missense mutations are associated with neuropathies
J. Hum. Genet.
56
143-146
2011
Homo sapiens (Q8TDX6), Homo sapiens
brenda
Zheng, J.; Wu, C.; Ma, W.; Zhang, Y.; Hou, T.; Xu, H.; Wu, S.; Yao, X.; Guo, X.
Abnormal expression of chondroitin sulphate N-acetylgalactosaminyltransferase 1 and Hapln-1 in cartilage with Kashin-Beck disease and primary osteoarthritis
Int. Orthop.
37
2051-2059
2013
Homo sapiens (Q8TDX6)
brenda
Saigoh, K.; Yoshimura, S.; Izumikawa, T.; Miyata, S.; Tabara, Y.; Matsushita, T.; Miki, T.; Miyamoto, K.; Hirano, M.; Kitagawa, H.; Kira, J.I.; Kusunoki, S.
Chondroitin sulfate beta-1,4-N-acetylgalactosaminyltransferase-1 (ChGn-1) polymorphism: association with progression of multiple sclerosis
Neurosci. Res.
108
55-59
2016
Homo sapiens (Q8TDX6)
brenda
Vodopiutz, J.; Mizumoto, S.; Lausch, E.; Rossi, A.; Unger, S.; Janocha, N.; Costantini, R.; Seidl, R.; Greber-Platzer, S.; Yamada, S.; Mueller, T.; Jilma, B.; Ganger, R.; Superti-Furga, A.; Ikegawa, S.; Sugahara, K.; Janecke, A.R.
Chondroitin sulfate N-acetylgalactosaminyltransferase-1 (CSGalNAcT-1) deficiency results in a mild skeletal dysplasia and joint laxity
Hum. Mutat.
38
34-38
2017
Homo sapiens (Q8TDX6), Homo sapiens
brenda
Ji, X.Y.; Chen, J.H.; Zheng, G.H.; Huang, M.H.; Zhang, L.; Yi, H.; Jin, J.; Jiang, J.D.; Peng, Z.G.; Li, Z.R.
Design and synthesis of cajanine analogues against hepatitis C virus through down-regulating host chondroitin sulfate N-acetylgalactosaminyltransferase 1
J. Med. Chem.
59
10268-10284
2016
Homo sapiens (Q8TDX6)
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Clausen, T.M.; Pereira, M.A.; Al Nakouzi, N.; Oo, H.Z.; Agerbaek, M.O.; Lee, S.; Oerum-Madsen, M.S.; Kristensen, A.R.; El-Naggar, A.; Grandgenett, P.M.; Grem, J.L.; Hollingsworth, M.A.; Holst, P.J.; Theander, T.; Sorensen, P.H.; Daugaard, M.; Salanti, A.
Oncofetal chondroitin sulfate glycosaminoglycans are key players in integrin signaling and tumor cell motility
Mol. Cancer Res.
14
1288-1299
2016
Homo sapiens (Q8TDX6), Homo sapiens, Mus musculus (Q8BJQ9), Mus musculus, Mus musculus C57BL/6 (Q8BJQ9)
brenda
Igarashi, M.; Takeuchi, K.; Sugiyama, S.
Roles of CSGalNAcT1, a key enzyme in regulation of CS synthesis, in neuronal regeneration and plasticity
Neurochem. Int.
119
77-83
2018
Homo sapiens (Q8N6G5), Homo sapiens (Q8TDX6), Mus musculus (Q8BJQ9), Mus musculus (Q8C1F4)
brenda
Sakai, D.; Nakai, T.; Hiraishi, S.; Nakamura, Y.; Ando, K.; Naiki, M.; Watanabe, M.
Upregulation of glycosaminoglycan synthesis by neurotropin in nucleus pulposus cells via stimulation of chondroitin sulfate N-acetylgalactosaminyltransferase 1 a new approach to attenuation of intervertebral disc degeneration
PLoS ONE
13
e0202640
2018
Homo sapiens (Q8TDX6), Homo sapiens
brenda