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Information on EC 2.8.2.17 - chondroitin 6-sulfotransferase and Organism(s) Mus musculus and UniProt Accession Q9EP78
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EC Tree
2.8.2.17 chondroitin 6-sulfotransferaseIUBMB Comments
The sulfation is at the 6-position of N-acetylgalactosamine residues of chondroitin. Not identical with EC 2.8.2.5 chondroitin 4-sulfotransferase.
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Word Map
- 2.8.2.17
-
sulfotransferases
- proteoglycans
- glycosaminoglycans
- n-acetylgalactosamine
- keratan
- 6-sulfate
-
spondyloepiphyseal
-
4-sulfotransferase
-
6-o-sulfated
-
omani
-
2-o-sulfotransferase
-
chst15
-
uronyl
-
kyphoscoliosis
-
larsen
-
6-sulphated
- medicine
- synthesis
The taxonomic range for the selected organisms is: Mus musculus
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Reaction Schemes
Synonyms
chst3, c6st, c6st-1, chondroitin 6-sulfotransferase, carbohydrate sulfotransferase 3, c6st1, chondroitin 6-o-sulfotransferase, chondroitin 6-o-sulfotransferase-1, chondroitin-6-sulfotransferase, chondroitin 6-sulfotransferase-1, 
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topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
3'-phosphoadenosine 5'-phosphosulfate:chondroitin sulfate sulfotransferase
-
-
-
-
C6ST
-
-
-
-
chondroitin 6-O-sulfotransferase
-
-
-
-
CST
-
-
-
-
sulfotransferase, chondroitin 6-
-
-
-
-
terminal 6-sulfotransferase
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
sulfate group transfer
-
-
-
-
PATHWAY SOURCE
PATHWAYS
-
-
SYSTEMATIC NAME
IUBMB Comments
3'-phosphoadenylyl-sulfate:chondroitin 6'-sulfotransferase
The sulfation is at the 6-position of N-acetylgalactosamine residues of chondroitin. Not identical with EC 2.8.2.5 chondroitin 4-sulfotransferase.
CAS REGISTRY NUMBER
COMMENTARY
37292-93-6
-
83589-04-2
-
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
3'-phosphoadenylyl sulfate + chondroitin
adenosine 3',5'-bisphosphate + chondroitin 6'-sulfate
-
-
-
?
3'-phosphoadenylyl sulfate + chondroitin
adenosine 3',5'-bisphosphate + chondroitin 6-sulfate
-
-
-
?
3'-phosphoadenylyl sulfate + native chondroitin
adenosine 3',5'-bisphosphate + native chondroitin sulfate
-
-
-
-
r
3'-phosphoadenylylsulfate + chondroitin
adenosine 3',5'-bisphosphate + chondroitin 6'-sulfate
adenosine 3',5'-bisphosphate + desulfated chondroitin sulfate
3'-phosphoadenylyl sulfate + desulfated chondroitin
-
-
-
-
r
3'-phosphoadenylylsulfate + chondroitin
adenosine 3',5'-bisphosphate + chondroitin 6'-sulfate
-
-
-
?
3'-phosphoadenylylsulfate + chondroitin
adenosine 3',5'-bisphosphate + chondroitin 6'-sulfate
-
-
-
?
3'-phosphoadenylylsulfate + chondroitin
adenosine 3',5'-bisphosphate + chondroitin 6'-sulfate
-
native chondroitin is the best acceptor, chemically desulfated chondroitin sulfate has the lowest rate of sulfation
-
?
3'-phosphoadenylylsulfate + chondroitin
adenosine 3',5'-bisphosphate + chondroitin 6'-sulfate
-
involved in the maintenance of native T lymphocytes in the spleen
-
?
additional information
?
-
-
dermatan sulfate and keratan sulfate preparations which contain covalently bound chondroitin sulfate act as sulfate acceptors
-
-
?
NATURAL SUBSTRATE
NATURAL 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
3'-phosphoadenylyl sulfate + chondroitin
adenosine 3',5'-bisphosphate + chondroitin 6'-sulfate
-
-
-
?
3'-phosphoadenylyl sulfate + chondroitin
adenosine 3',5'-bisphosphate + chondroitin 6-sulfate
-
-
-
?
3'-phosphoadenylylsulfate + chondroitin
adenosine 3',5'-bisphosphate + chondroitin 6'-sulfate
-
involved in the maintenance of native T lymphocytes in the spleen
-
?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.00034
3'-phosphoadenylyl sulfate
pH 6.8, 37°C, recombinant mutant N250S, with chondroitin
0.0004
3'-phosphoadenylyl sulfate
pH 6.8, 37°C, recombinant mutant N457S, with chondroitin
0.0011
3'-phosphoadenylyl sulfate
pH 6.8, 37°C, recombinant wild-type enzyme, with chondroitin
0.0029
3'-phosphoadenylyl sulfate
pH 6.8, 37°C, recombinant mutant N413S, with keratan sulfate
0.0038
3'-phosphoadenylyl sulfate
pH 6.8, 37°C, recombinant wild-type enzyme, with keratan sulfate
0.00417
3'-phosphoadenylyl sulfate
pH 6.8, 37°C, recombinant mutant N413S, with chondroitin
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
overexpression of chondroitin 6-sulfotransferase-1 selectively decreases aggrecan, a major chondroitin sulfate proteoglycans in perineuronal nets, in the aged brain without affecting other perineuronal net components
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). CHST7_MOUSE
484
1
54767
Swiss-Prot
Secretory Pathway (Reliability: 1)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
54000
x * 67000, glycosylated recombinant enzyme, SDS-PAGE, x * 54000, deglycosylated recombinant enzyme, SDS-PAGE
67000
x * 67000, glycosylated recombinant enzyme, SDS-PAGE, x * 54000, deglycosylated recombinant enzyme, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
?
x * 67000, glycosylated recombinant enzyme, SDS-PAGE, x * 54000, deglycosylated recombinant enzyme, SDS-PAGE
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
glycoprotein
the enzyme contains N-linked oligosaccharide side chains, which have essential roles in the generation of the active enzyme and in its keratan sulfate sulfotransferase activity, overview, six potential N-glycosylation sites
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
N250S
site-directed mutagenesis, mutation of a putative N-glycosylation site, deletion of the fourth N-glycosylation site from the N-terminus of the enzyme inhibits production of the active C6ST-1, the mutant remains in the endoplasmic reticulum, while all other wild-type and mutant enzymes are located in the Golgi apparatus
N413S
site-directed mutagenesis, mutation of a putative N-glycosylation site, deletion of the fourth or sixth N-glycosylation site from the N-terminus of the enzyme inhibits production of the active C6ST-1
N457S
site-directed mutagenesis, mutation of a putative N-glycosylation site, deletion of the fifth N-glycosylation site from the N-terminus of the enzyme results in a marked loss of the keratan sulfate sulfotransferase activity
N63S
site-directed mutagenesis, mutation of a putative N-glycosylation site
N74S
site-directed mutagenesis, mutation of a putative N-glycosylation site
N96S
site-directed mutagenesis, mutation of a putative N-glycosylation site
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant wild-type and mutant FLAG-tagged C6ST-1s from COS-7 cells by anti-FLAG-tag immunoaffinity and wheat germ agglutinin affinity chromatography
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene C6st, expression of wild-type and mutant FLAG-tagged C6ST-1s in COS-7 cells, addition of tunicamycin completely abolishes N-glycosylation of the recombinant enzyme and enzyme activity, overview
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
the levels of chondroitin 6-O-sulfotransferase 1 mRNA and protein increase after cortical stab injury of wild type mice. Old astrocyte specifically induced substance upregulates the transcription of the enzyme
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Momburg, M.; Stuhlsatz, H.W.; Greiling, H.
Isolation and substrate specificity of a 3-phosphoadenyl sulfate: chondroitin 6-sulfotransferase from mouse liver
Hoppe-Seyler's Z. Physiol. Chem.
353
1351-1361
1972
Mus musculus
Bhakta, S.; Bartes, A.; Bowman, K.G.; Kao, W.M.; Polsky, I.; Lee, J.K.; Cook, B.N.; Bruehl, R.E.; Rosen, S.D.; Bertozzi, C.R.; Hemmerich, S.
Sulfation of N-acetylglucosamine by chondroitin 6-sulfotransferase 2 (GST-5)
J. Biol. Chem.
275
40226-40234
2000
Homo sapiens, Mus musculus (Q9EP78), Mus musculus
Uchimura, K.; Kadomatsu, K.; Fan, Q.W.; Muramatsu, H.; Kurosawa, N.; Kaname, T.; Yamamura, K.; Fukuta, M.; Habuchi, O.; Muramatsu, T.
Mouse chondroitin 6-sulfotransferase: molecular cloning, characterization and chromosomal mapping
Glycobiology
8
489-496
1998
Mus musculus (O88199), Mus musculus
Uchimura, K.; Kadomatsu, K.; Nishimura, H.; Muramatsu, H.; Nakamura, E.; Kurosawa, N.; Habuchi, O.; El-Fasakhany, F.M.; Yoshikai, Y.; Muramatsu, T.
Functional analysis of the chondroitin 6-sulfotransferase gene in relation to lymphocyte subpopulations, brain development, and oversulfated chondroitin sulfates
J. Biol. Chem.
277
1443-1450
2002
Mus musculus
Yusa, A.; Kitajima, K.; Habuchi, O.
N-linked oligosaccharides on chondroitin 6-sulfotransferase-1 are required for production of the active enzyme, Golgi localization, and sulfotransferase activity toward keratan sulfate
J. Biol. Chem.
281
20393-20403
2006
Mus musculus (O88199)
Okuda, H.; Tatsumi, K.; Horii-Hayashi, N.; Morita, S.; Okuda-Yamamoto, A.; Imaizumi, K.; Wanaka, A.
OASIS regulates chondroitin 6-O-sulfotransferase 1 gene transcription in the injured adult mouse cerebral cortex
J. Neurochem.
130
612-625
2014
Mus musculus (O88199), Mus musculus
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