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Information on EC 2.8.2.8 - [heparan sulfate]-glucosamine N-sulfotransferase and Organism(s) Homo sapiens and UniProt Accession O95803

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IUBMB Comments
The enzyme also catalyses the sulfation of chondroitin 4-sulfate and dermatan sulfate, but to a much more limited extent.
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Select one or more organisms in this record:
This record set is specific for:
Homo sapiens
UNIPROT: O95803
Word Map
The taxonomic range for the selected organisms is: Homo sapiens
The enzyme appears in selected viruses and cellular organisms
Synonyms
3'-phosphoadenylyl-sulfate:heparitin N-sulfotransferase, 3'-phosphoadenylylsulfate:N-desulfoheparin N-sulfotransferase, 3'-phosphoadenylylsulfate:N-desulfoheparin sulfotransferase, desulfoheparin sulfotransferase, EC 2.8.2.12, GlcNAc N-deacetylase/GlcN N-sulfotransferase, GlcNAc N-deacetylase/GlcN N-sulfotransferase 1, GlcNAc N-deacetylase/N-sulfotransferase, glucosaminyl N-deacetylase/N-sulfotransferase, heparan sulfate 2-N-sulfotransferase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
3'-phosphoadenylyl-sulfate:heparitin N-sulfotransferase
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3'-phosphoadenylylsulfate:N-desulfoheparin N-sulfotransferase
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3'-phosphoadenylylsulfate:N-desulfoheparin sulfotransferase
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desulfoheparin sulfotransferase
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GlcNAc N-deacetylase/GlcN N-sulfotransferase
272990
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GlcNAc N-deacetylase/N-sulfotransferase
272984
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heparan sulfate 2-N-sulfotransferase
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heparan sulfate N-deacetylase/N-sulfotransferase
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heparan sulfate N-deacetylase/N-sulfotransferase 2
247
bifunctional enzyme
heparan sulfate N-sulfotransferase
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heparan sulfate sulfotransferase
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heparin N-sulfotransferase
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heparitin sulfotransferase
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HSNST
247
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N-deacetylase/N-sulfotransferase
247
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N-deacetylase/N-sulfotransferase 1
306577
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N-desulfoheparin sulfotransferase
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N-heparan sulfate sulfotransferase
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N-HSST
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NDST-1
306577
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Ndst1
247
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NDST2
247
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PAPS:DSH sulfotransferase
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PAPS:N-desulfoheparin sulfotransferase
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sulfotransferase, desulfoheparin
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
3'-phosphoadenylyl sulfate + [heparan sulfate]-glucosamine = adenosine 3',5'-bisphosphate + [heparan sulfate]-N-sulfoglucosamine
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
sulfate group transfer
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PATHWAY SOURCE
PATHWAYS
SYSTEMATIC NAME
IUBMB Comments
3'-phosphoadenylyl-sulfate:[heparan sulfate]-glucosamine N-sulfotransferase
The enzyme also catalyses the sulfation of chondroitin 4-sulfate and dermatan sulfate, but to a much more limited extent.
CAS REGISTRY NUMBER
COMMENTARY hide
9026-75-9
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
3'-phosphoadenylyl sulfate + [heparan sulfate]-glucosamine
adenosine 3',5'-bisphosphate + [heparan sulfate]-N-sulfoglucosamine
show the reaction diagram
3'-phosphoadenylyl sulfate + heparosan
adenosine 3',5'-bisphosphate + heparosan sulfate
show the reaction diagram
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-
-
?
3'-phosphoadenylyl sulfate + [heparan sulfate]-glucosamine
adenosine 3',5'-bisphosphate + [heparan sulfate]-N-sulfoglucosamine
show the reaction diagram
3'-phosphoadenylylsulfate + N,O-desulfated heparan sulfate
adenosine 3',5'-bisphosphate + O-desulfated heparan sulfate
show the reaction diagram
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no activity with
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3'-phosphoadenylylsulfate + N-acetylated heparan sulfate
?
show the reaction diagram
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no activity with
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3'-phosphoadenylylsulfate + N-desulfated heparan sulfate
adenosine 3',5'-bisphosphate + heparan sulfate
show the reaction diagram
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best substrate
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?
3'-phosphoadenylylsulfate + N-desulfated heparin
?
show the reaction diagram
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?
additional information
?
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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
3'-phosphoadenylyl sulfate + [heparan sulfate]-glucosamine
adenosine 3',5'-bisphosphate + [heparan sulfate]-N-sulfoglucosamine
show the reaction diagram
additional information
?
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NDST1 and NDST2 have no redundant activities but rather have complementary activities in making N-sulfated heparan sulfate motifs with cyclophilin B-binding properties. Synthesis of heparan sulfate with cyclophilin B-binding properties is determined by cell type-specific expression of sulfotransferases
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
divalent metal ions are not required for N-sulfotransferase activity of NDST-1
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
not inhibited by EDTA
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.02
3'-phosphoadenylylsulfate
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pH 7.0, 37°C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
231
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purified recombinant sulfotransferase domain, substrate is at all positions completely desulfated heparin
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7
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assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37
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assay at
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
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adult; low activity
Manually annotated by BRENDA team
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clone E6-1, ATCC TIB-152
Manually annotated by BRENDA team
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high expression level of isozyme NDST2
Manually annotated by BRENDA team
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high expression level of isozyme NDST2. The expression of NDST2 in monocytes is modified following cell activation or maturation, although the same treatment has no significant effect on the level of mRNAencoding NDST1
Manually annotated by BRENDA team
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CD4+ cells, high expression level of isozyme NDST2. NDST1 is barely detected in naive T-lymphocytes by comparison with memory and activated CD4 T cells, whereas no notable variation in the expression of NDST2 can be distinguished between T cell subsets
Manually annotated by BRENDA team
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promonocytic leukemia cells
Manually annotated by BRENDA team
additional information
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NDST1 and NDST2 are widely expressed in all the tissues analyzed, overview. Synthesis of heparan sulfate with cyclophilin B-binding properties is determined by cell type-specific expression of sulfotransferases
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
additional information
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
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in the general scheme of heparan sulfate biosynthesis, GlcNAc N-deacetylation and N-sulfation by NDSTs create the prerequisite substrate needed for the next enzymatic modifications
physiological function
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NDST1 is required for initiation of N-sulfation of the nascent precursor, whereas NDST2 may fill in or extend the sections of N-sulfated residues in heparin and highly sulfated heparan sulfate species
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
Sequence
NDST3_HUMAN
873
1
100902
Swiss-Prot
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
CRYSTALLIZATION/commentary
ORGANISM
UNIPROT
LITERATURE
18 mg/ml, 0.1 M Tris-HCl, pH 8.3, 0.1 M NaCl, 4 mM 3'-phosphoadenosine 5'-phosphate, reservoir solution: Bis-Tris-propane, pH 7.0, 0.2 M NaCl, 30% PEG 3000, room temperature, X-ray diffraction structure determination and analysis; purified recombinant bacterially expressed sulfotransferase domain
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18 mg/ml, 0.1 M Tris-HCl, pH 8.3, 0.1 M NaCl, 4 mM 3'-phosphoadenosine 5'-phosphate, reservoir solution: Bis-Tris-propane, pH 7.0, 0.2 M NaCl, 30% PEG 3000, room temperature, X-ray diffraction structure determination and analysis; purified recombinant selenomethionyl sulfotransferase domain NST1
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structure
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
K614A
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site-directed mutagenesis of the sulfotransferase domain of the bifunctional enzyme, complete loss of N-sulfotransferase activity
additional information
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lack of NDST1 affects heparan sulfate structure in all tissues tested, with a dramatic reduction in N- and O-sulfation of the polysaccharide. Silencing the expression of NDST1, NDST2, 2-OST, and 3-OST3 by RNA interference efficiently decreases binding and activity of cyclophilin B
PURIFICATION/commentary
ORGANISM
UNIPROT
LITERATURE
heparin-Toyopearl column chromatography and nickel-agarose column chromatography
recombinant fusion tagged sulfotransferase domain from Escherichia coli BL21 cells by affinity chromatography
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recombinant sulfotransferase domain NST1 from Escherichia coli strain B834 (DE3)
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CLONED/commentary
ORGANISM
UNIPROT
LITERATURE
brain cDNA library, DNA sequence determination and analysis; construction of a chimeric enzyme consisiting of a soluble enzyme form NDST3 N-terminally fused to a protein A fragment, expression in COS-7 cells
isozyme NDST3, chromosomal localisation
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DNA sequence determination, analysis, and expression of the wild-type and mutated sulfotransferase domain of the bifunctional enzyme in Escherichia coli BL21 cells as fusion tagged protein
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expressed in Sf9 insect cells
expression of the selenomethionyl sulfotransferase domain NST1 in methionine auxotrophic Escherichia coli strain B834 (DE3)
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isozyme NDST4, DNA sequence determination and analysis, chromosomal localization
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isozymes NDST1 and NDST2
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the N-terminal domain (A66-P604) of the bifunctional enzyme heparan sulfate N-deacetylase/N-sulfotransferase 2 is cloned as a (His)6-fusion protein, expression in Escherichia coli. The N-terminal domain contains functional N-deacetylase activity
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Sueyoshi, T.; Kakuta, Y.; Pedersen, L.C.; Wall, F.E.; Pedersen, L.G.; Negishi, M.
A role of Lys614 in the sulfotransferase activity of human heparan sulfate N-deacetylase/N-sulfotransferase
FEBS Lett.
433
211-214
1998
Homo sapiens
Manually annotated by BRENDA team
Kakuta, Y.; Sueyoshi, T.; Negishi, M.; Pedersen, L.C.
Crystal structure of the sulfotransferase domain of human heparan sulfate N-deacetylase/N-sulfotransferase 1
J. Biol. Chem.
274
10673-10676
1999
Homo sapiens
Manually annotated by BRENDA team
Aikawa, J.; Esko, J.D.
Molecular cloning and expression of a third member of the heparan sulfate/heparin GlcNAc N-deacetylase/N-sulfotransferase family
J. Biol. Chem.
274
2690-2695
1999
Cricetulus griseus, Homo sapiens, Homo sapiens (O95803)
Manually annotated by BRENDA team
Gorokhov, A.; Perera, L.; Darden, T.A.; Negishi, M.; Pedersen, L.C.; Pedersen, L.G.
Heparan sulfate biosynthesis: a theoretical study of the initial sulfation step by N-deacetylase/N-sulfotransferase
Biophys. J.
79
2909-2917
2000
Homo sapiens
Manually annotated by BRENDA team
Aikawa, J.; Grobe, K.; Tsujimoto, M.; Esko, J.D.
Multiple isozymes of heparan sulfate/heparin GlcNAc N-deacetylase/GlcN N-sulfotransferase. Structure and activity of the fourth member, NDST4
J. Biol. Chem.
276
5876-5882
2001
Homo sapiens, Homo sapiens (O95803), Homo sapiens (Q9H3R1), Mus musculus, Mus musculus (P52850), Mus musculus (Q3UHN9), Mus musculus (Q9EQH7), Mus musculus (Q9EQW8)
Manually annotated by BRENDA team
Grobe, K.; Ledin, J.; Ringvall, M.; Holmborn, K.; Forsberg, E.; Esko, J.D.; Kjellen, L.
Heparan sulfate and development: differential roles of the N-acetylglucosamine N-deacetylase/N-sulfotransferase isozymes
Biochim. Biophys. Acta
1573
209-215
2002
Caenorhabditis elegans, Drosophila melanogaster, Homo sapiens, Homo sapiens (O95803), Homo sapiens (Q9H3R1), Mus musculus, Mus musculus (Q9EQW8), vertebrata
Manually annotated by BRENDA team
Duncan, M.B.; Liu, M.; Fox, C.; Liu, J.
Characterization of the N-deacetylase domain from the heparan sulfate N-deacetylase/N-sulfotransferase 2
Biochem. Biophys. Res. Commun.
339
1232-1237
2006
Homo sapiens
Manually annotated by BRENDA team
Deligny, A.; Denys, A.; Marcant, A.; Melchior, A.; Mazurier, J.; van Kuppevelt, T.H.; Allain, F.
Synthesis of heparan sulfate with cyclophilin B-binding properties is determined by cell type-specific expression of sulfotransferases
J. Biol. Chem.
285
1701-1715
2010
Homo sapiens
Manually annotated by BRENDA team
Dou, W.; Xu, Y.; Pagadala, V.; Pedersen, L.C.; Liu, J.
Role of deacetylase activity of N-deacetylase/n-sulfotransferase 1 in forming n-sulfated domain in heparan sulfate
J. Biol. Chem.
290
20427-20437
2015
Homo sapiens (P52848)
Manually annotated by BRENDA team
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