Any feedback?
Please rate this page
(enzyme.php)
(0/150)

BRENDA support

BRENDA Home
show all | hide all No of entries

Information on EC 2.4.1.174 - glucuronylgalactosylproteoglycan 4-beta-N-acetylgalactosaminyltransferase and Organism(s) Homo sapiens and UniProt Accession Q8N6G5

for references in articles please use BRENDA:EC2.4.1.174
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
IUBMB Comments
Requires Mn2+. Involved in the biosynthesis of chondroitin sulfate. Key enzyme activity for the initiation of chondroitin and dermatan sulfates, transferring GalNAc to the GlcA-Gal-Gal-Xyl-Ser core.
Specify your search results
Select one or more organisms in this record: ?
This record set is specific for:
Homo sapiens
UNIPROT: Q8N6G5
Show additional data
Do not include text mining results
Include (text mining) results
Include results (AMENDA + additional results, but less precise)
Word Map
hide
The taxonomic range for the selected organisms is: Homo sapiens
The enzyme appears in selected viruses and cellular organisms
Synonyms
csgalnact1, csgalnact2, chondroitin sulfate n-acetylgalactosaminyltransferase 1, galnact-ii, chondroitin n-acetylgalactosaminyltransferase-1, chondroitin n-acetylgalactosaminyltransferase-2, chondroitin sulfate n-acetylgalactosaminyltransferase 2, n-acetylgalactosaminet-ii, galnact-i, chondroitin beta1,4-n-acetylgalactosaminyltransferase-1, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
chondroitin galactosaminyltransferase
-
CSGALNACT2
-
acetylgalactosaminyltransferase, uridine diphosphoacetylgalactosamine-chondroitin, I
-
-
-
-
chondroitin beta1,4-N-acetylgalactosaminyltransferase-1
-
chondroitin galactosaminyltransferase
-
chondroitin sulfate beta-1,4-N-acetylgalactosaminyltransferase-1 ChGn-1
-
chondroitin sulfate N-acetylgalactosaminyltransferase 1
-
chondroitin sulfate N-acetylgalactosaminyltransferase-1
chondroitin sulphate N-acetylgalactosaminyltransferase 1
-
CSGal-NACT-1
-
CSGalNAcT-1
GalNAcT-II
-
glucuronylgalactosylproteoglycan beta-1,4-N-acetylgalactosaminyltransferase
-
-
-
-
N-acetylgalactosamineT-II
-
N-acetylgalactosaminyltransferase I
-
-
-
-
uridine diphosphoacetylgalactosamine-chondroitin acetylgalactosaminyltransferase I
-
-
-
-
additional information
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hexosyl group transfer
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
UDP-N-acetyl-D-galactosamine:D-glucuronyl-(1->3)-beta-D-galactosyl-proteoglycan 4-beta-N-acetylgalactosaminyltransferase
Requires Mn2+. Involved in the biosynthesis of chondroitin sulfate. Key enzyme activity for the initiation of chondroitin and dermatan sulfates, transferring GalNAc to the GlcA-Gal-Gal-Xyl-Ser core.
CAS REGISTRY NUMBER
COMMENTARY hide
96189-39-8
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
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
show the reaction diagram
-
-
-
?
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)
show the reaction diagram
-
-
-
?
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
show the reaction diagram
-
-
-
?
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
show the reaction diagram
-
-
-
?
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
show the reaction diagram
-
-
-
?
UDP-N-acetyl-D-galactosamine + glucuronylgalactosyl glycosides
UDP + N-acetyl-D-galactosaminyl-1,4-beta-D-glucuronylgalactosyl glycosides
show the reaction diagram
-
-
?
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
show the reaction diagram
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
show the reaction diagram
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
show the reaction diagram
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
show the reaction diagram
UDP-N-acetyl-D-galactosamine + glucuronylgalactosyl glycosides
UDP + N-acetyl-D-galactosaminyl-1,4-beta-D-glucuronylgalactosyl glycosides
show the reaction diagram
UDP-N-acetyl-D-galactosamine + glucuronylgalactosyl glycosides
UDP + N-acetyl-D-galactosaminylglucuronylgalactosyl glycosides
show the reaction diagram
additional information
?
-
-
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
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
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
show the reaction diagram
-
-
-
?
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
show the reaction diagram
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
show the reaction diagram
UDP-N-acetyl-D-galactosamine + glucuronylgalactosyl glycosides
UDP + N-acetyl-D-galactosaminylglucuronylgalactosyl glycosides
show the reaction diagram
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
(E)-2-hydroxy-3-isopentyl-4-methoxy-6-styrylbenzoic acid
-
(E)-2-hydroxy-4-methoxy-3-(3-methylbut-2-enyl)-6-(2-phenylprop-1-enyl)benzoic acid
-
(E)-2-hydroxy-4-methoxy-3-prenyl-6-(2-(thiophen-2-yl)vinyl)-benzoic acid
-
(E)-3-(3,7-dimethylocta-2,6-dienyl)-2-hydroxy-4-methoxy-6-phenethylbenzoic acid
-
(E)-3-c-6-hydroxy-4-methoxy-5-prenyl-2-styrylbenzoic acid
-
(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
-
(E)-6-(2-methylstyryl)-2-hydroxy-4-methoxy-3-prenylbenzoic acid
-
(E)-6-(3-methylstyryl)-2-hydroxy-4-methoxy-3-prenylbenzoic acid
-
(E)-6-(4-fluorostyryl)-2-hydroxy-4-methoxy-3-prenylbenzoic acid
-
(E)-6-(4-hydroxystyryl)-2-hydroxy-4-methoxy-3-prenylbenzoic acid
-
(E)-6-(4-methylstyryl)-2-hydroxy-4-methoxy-3-prenylbenzoic acid
-
(E)-6-(but-1-enyl)-2-hydroxy-4-methoxy-3-prenylbenzoic acid
-
(E)-ethyl 2-hydroxy-4-methoxy-3-(3-methylbut-2-enyl)-6-styrylbenzoate
-
(E)-isopropyl 2-hydroxy-4-methoxy-3-(3-methylbut-2-enyl)-6-styrylbenzoate
-
(E)-methyl 2-hydroxy-3-isopentyl-4-methoxy-6-styrylbenzoate
-
(E)-methyl 2-hydroxy-4-methoxy-3-(3-methylbut-2-enyl)-6-(2-phenylprop-1-enyl)benzoate
-
(E)-methyl 2-hydroxy-4-methoxy-3-prenyl-6-(2-(thiophen-2-yl)-vinyl)benzoate
-
(E)-methyl 6-(2-chlorostyryl)-2-hydroxy-4-methoxy-3-prenylbenzoate
-
(E)-methyl 6-(2-methylstyryl)-2-hydroxy-4-methoxy-3-prenylbenzoate
-
(E)-methyl 6-(3-methylstyryl)-2-hydroxy-4-methoxy-3-prenylbenzoate
-
(E)-methyl 6-(4-(tert-butyldimethylsilyloxy)styryl)-2-hydroxy-4-methoxy-3-prenylbenzoate
-
(E)-methyl 6-(4-fluorostyryl)-2-hydroxy-4-methoxy-3-prenylbenzoate
-
(E)-methyl 6-(4-hydroxystyryl)-2-hydroxy-4-methoxy-3-prenylbenzoate
-
(E)-methyl 6-(4-methylstyryl)-2-hydroxy-4-methoxy-3-prenylbenzoate
-
(E)-methyl 6-(but-1-enyl)-2-hydroxy-4-methoxy-3-prenylbenzoate
-
(E)-methyl 6-styryl-2-hydroxy-4-methoxy-3-prenylbenzoate
-
(E)-N-cyclopropyl-2-hydroxy-4-methoxy-3-(3-methylbut-2-enyl)-6-styrylbenzamide
-
(E)-tert-butyl 2-hydroxy-4-methoxy-3-(3-methylbut-2-enyl)-6-styrylbenzoate
-
2-hydroxy-3-isopentyl-4-methoxy-6-phenethylbenzoic acid
-
2-hydroxy-4-methoxy-3-prenyl-6-((1E,3E)-4-phenylbuta-1,3-dienyl)benzoic acid
-
2-hydroxy-4-methoxy-3-prenyl-6-phenethylbenzoic acid
-
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
longistyline A
-
methyl 2-hydroxy-4-methoxy-3-prenyl-6-((1E,3E)-4-phenylbuta-1,3-dienyl)benzoate
-
methyl 2-hydroxy-4-methoxy-3-prenyl-6-phenethylbenzoate
-
additional information
2-hydroxy-4-methoxy-6-[(E)-2-phenylethenyl]benzoic acid is not inhibitory
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
SwissProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
peripheral blood
Manually annotated by BRENDA team
-
-
Manually annotated by BRENDA team
articular
Manually annotated by BRENDA team
low content
Manually annotated by BRENDA team
melanoma cell line
Manually annotated by BRENDA team
very high content
Manually annotated by BRENDA team
-
chondrosarcoma cell line
Manually annotated by BRENDA team
thyroid cancer cell line
Manually annotated by BRENDA team
low content
Manually annotated by BRENDA team
low content
Manually annotated by BRENDA team
myeloma cell line
Manually annotated by BRENDA team
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
type II membrane protein topology
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
metabolism
physiological function
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
CGAT2_HUMAN
542
1
62572
Swiss-Prot
Secretory Pathway (Reliability: 1)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
95000
x * 95000, recombinant enzyme, SDS-PAGE
70000
x * 70000, about, recombinant His-tagged soluble forms of wild-type ChGn-1 and S126LChGn-1 mutant enzymes, SDS-PAGE
95000
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 95000, recombinant enzyme, SDS-PAGE
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
glycoprotein
2 potential N-glycosylation sites, either one or both of which are used in COS-1 cells during expression of the recombinant fusion protein
glycoprotein
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
H234R
naturally occuring mutation in exon 5 of gene ChGn1, the mutant shows neuropathy, Bell’s 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, Bell’s 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
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant His-tagged soluble forms of wild-type ChGn-1 and S126LChGn-1 mutant from COS-1 cellsby nickel affinity chromatography
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
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.
-
Myc-tagged CSGalNAcT-1 expression in HeLa cells
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
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, overview. Cajanine might inhibit HCV replication at early steps of the viral life cycle via downregulating of cellular CSGalNAcT-1
enzyme expression is induced by Neutropin (NTP). Neurotropin activates the phosphatidylinositol 3-kinase-AKT pathway and AKT stimulation, it stimulate glycosaminoglycan synthesis through upregulation of expression of mRNA for chondroitin sulfate N-acetylgalactosaminyltransferase 1. Gene expression profiling shows over 2fold upregulation of 697 genes in response to Neurotropin treatment. Upregulation of IGF1, ANG1, and CSGALNACT1 expression by NTP. Neurotropin (NTP) is a nonprotein extract from inflamed rabbit skin inoculated with vaccinia virus, it has been widely used in Japan and China as an analgesic drug for treatment of chronic pain, such as LBP, postherpetic neuralgia, neck-shoulder-arm syndrome, hyperesthesia of subacute myelo-optic neuropathy, and fibromyalgia. Addition of NTP to the culture medium of nucleus pulposus cells enhances proteoglycan synthesis to halt progressive intervertebral disc (IVD) degeneration
induction of gene CSGalNAcT-2 by NTP is much lower compared to CSGalNAcT-1
the enzyme is downregulated in Kashin-Beck disease (KBD), an endemic degenerative osteoarthritis, and in primary osteoarthritis, both associated with extracellular matrix degradation
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
drug development
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
J. Biol. Chem.
277
38189-38196
2002
Homo sapiens (Q8TDX6)
Manually annotated by BRENDA team
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.
277
8841-8846
2002
Homo sapiens (Q8TDX6)
Manually annotated by BRENDA team
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
2003
Homo sapiens (Q8N6G5), Homo sapiens (Q8TDX6)
Manually annotated by BRENDA team
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
4152-4161
2007
Homo sapiens, Mus musculus
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team