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3'-phosphoadenylyl sulfate + [heparan sulfate]-glucosamine = adenosine 3',5'-bisphosphate + [heparan sulfate]-N-sulfoglucosamine
comparison of catalytic mechanism aspects of the NDST isozymes, overview
3'-phosphoadenylyl sulfate + [heparan sulfate]-glucosamine = adenosine 3',5'-bisphosphate + [heparan sulfate]-N-sulfoglucosamine
3'-phosphoadenylyl sulfate + [heparan sulfate]-glucosamine = adenosine 3',5'-bisphosphate + [heparan sulfate]-N-sulfoglucosamine
binding mechanism, interaction scheme, sulfuryl transfer mechanism
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3'-phosphoadenylyl sulfate + [heparan sulfate]-glucosamine = adenosine 3',5'-bisphosphate + [heparan sulfate]-N-sulfoglucosamine
residues 558-882 provide the sulfotransferase domain of the bifunctional enzyme, with Lys614 as a catalytically important conserved residue
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3'-phosphoadenylyl sulfate + [heparan sulfate]-glucosamine = adenosine 3',5'-bisphosphate + [heparan sulfate]-N-sulfoglucosamine
important residue are Glu642, Lys614, Lys883, with possible involvement of Thr617 and Thr618, in binding 3'-phosphoadenosine 5'-phosphosulfate
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3'-phosphoadenylyl sulfate + [heparan sulfate]-glucosamine = adenosine 3',5'-bisphosphate + [heparan sulfate]-N-sulfoglucosamine
5'-phosphate binding and active site structure
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3'-phosphoadenylyl sulfate + [heparan sulfate]-glucosamine = adenosine 3',5'-bisphosphate + [heparan sulfate]-N-sulfoglucosamine
comparison of catalytic mechanism aspects of the NDST isozymes, overview
3'-phosphoadenylyl sulfate + [heparan sulfate]-glucosamine = adenosine 3',5'-bisphosphate + [heparan sulfate]-N-sulfoglucosamine
complex mechanism of GAG biosynthesis, mechanism of forward motion and hydrogen bond network analysis, overview
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3'-phosphoadenylyl sulfate + [heparan sulfate]-glucosamine
adenosine 3',5'-bisphosphate + [heparan sulfate]-N-sulfoglucosamine
3'-phosphoadenylyl sulfate + GlcA-GlcNAc-GlcA-GlcNS-GlcA-pNP
adenosine 3',5'-bisphosphate + ?
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?
3'-phosphoadenylyl sulfate + heparosan
adenosine 3',5'-bisphosphate + heparosan sulfate
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-
-
?
3'-phosphoadenylyl sulfate + [heparan sulfate]-glucosamine
adenosine 3',5'-bisphosphate + [heparan sulfate]-N-sulfoglucosamine
3'-phosphoadenylylsulfate + N,O-desulfated heparan sulfate
adenosine 3',5'-bisphosphate + O-desulfated heparan sulfate
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no activity with
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-
?
3'-phosphoadenylylsulfate + N-acetylated heparan sulfate
?
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no activity with
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-
?
3'-phosphoadenylylsulfate + N-desulfated heparan sulfate
adenosine 3',5'-bisphosphate + heparan sulfate
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best substrate
-
?
3'-phosphoadenylylsulfate + N-desulfated heparin
?
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-
-
?
additional information
?
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3'-phosphoadenylyl sulfate + [heparan sulfate]-glucosamine
adenosine 3',5'-bisphosphate + [heparan sulfate]-N-sulfoglucosamine
-
-
?
3'-phosphoadenylyl sulfate + [heparan sulfate]-glucosamine
adenosine 3',5'-bisphosphate + [heparan sulfate]-N-sulfoglucosamine
-
-
?
3'-phosphoadenylyl sulfate + [heparan sulfate]-glucosamine
adenosine 3',5'-bisphosphate + [heparan sulfate]-N-sulfoglucosamine
-
-
?
3'-phosphoadenylyl sulfate + [heparan sulfate]-glucosamine
adenosine 3',5'-bisphosphate + [heparan sulfate]-N-sulfoglucosamine
-
-
-
?
3'-phosphoadenylyl sulfate + [heparan sulfate]-glucosamine
adenosine 3',5'-bisphosphate + [heparan sulfate]-N-sulfoglucosamine
-
-
-
?
3'-phosphoadenylyl sulfate + [heparan sulfate]-glucosamine
adenosine 3',5'-bisphosphate + [heparan sulfate]-N-sulfoglucosamine
-
-
?
3'-phosphoadenylyl sulfate + [heparan sulfate]-glucosamine
adenosine 3',5'-bisphosphate + [heparan sulfate]-N-sulfoglucosamine
-
-
-
-
?
3'-phosphoadenylyl sulfate + [heparan sulfate]-glucosamine
adenosine 3',5'-bisphosphate + [heparan sulfate]-N-sulfoglucosamine
-
-
?
3'-phosphoadenylyl sulfate + [heparan sulfate]-glucosamine
adenosine 3',5'-bisphosphate + [heparan sulfate]-N-sulfoglucosamine
-
-
-
?
3'-phosphoadenylyl sulfate + [heparan sulfate]-glucosamine
adenosine 3',5'-bisphosphate + [heparan sulfate]-N-sulfoglucosamine
-
-
-
?
3'-phosphoadenylyl sulfate + [heparan sulfate]-glucosamine
adenosine 3',5'-bisphosphate + [heparan sulfate]-N-sulfoglucosamine
-
-
-
?
3'-phosphoadenylyl sulfate + [heparan sulfate]-glucosamine
adenosine 3',5'-bisphosphate + [heparan sulfate]-N-sulfoglucosamine
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substrate needs to be deacetylated
-
?
3'-phosphoadenylyl sulfate + [heparan sulfate]-glucosamine
adenosine 3',5'-bisphosphate + [heparan sulfate]-N-sulfoglucosamine
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NDST1 is able to partially sulfate exogenous substrate in the absence of NDST2 but not vice versa
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-
?
additional information
?
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the enzyme NDST removes the acetyl group from the GlcNAc residue and transfers a sulfate group to the primary amine forming a GlcNS substitute. Isozyme NDST3 has relatively higher N-deacetylase activity and lower sulfotransferase activity
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additional information
?
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the enzyme NDST removes the acetyl group from the GlcNAc residue and transfers a sulfate group to the primary amine forming a GlcNS substitute. Isozyme NDST3 has relatively higher N-deacetylase activity and lower sulfotransferase activity
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additional information
?
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the enzyme NDST removes the acetyl group from the GlcNAc residue and transfers a sulfate group to the primary amine forming a GlcNS substitute. Isozyme NDST3 has relatively higher N-deacetylase activity and lower sulfotransferase activity
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additional information
?
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the enzyme NDST removes the acetyl group from the GlcNAc residue and transfers a sulfate group to the primary amine forming a GlcNS substitute. Isozyme NDST3 has relatively higher N-deacetylase activity and lower sulfotransferase activity
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additional information
?
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no activity with N-acetylated substrates
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?
additional information
?
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substrate binding structures, overview
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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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-
?
additional information
?
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NDST-1 is a bifunctional enzyme that displays N-deacetylase and N-sulfotransferase activities to convert an N-acetylated glucosamine residue to an N-sulfoglucosamine residue
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?
additional information
?
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substrate specificity of recombinant NDST-1 (rNDST-1), full-length enzyme and individual N-deacetylase and N-sulfotransferase domains, with model oligosaccharides, detailed overview. Saccharides N-sulfated by NDST-1 are highly ordered, alternately containing N-S domains and N-Ac domains. Domain cooperation plays an essential role in NDST-1 production of HS with specific structures, and N-deacetylation is the limiting step. Recombinant NDST-1 clearly displayed bifunctional activity, it shows N-deacetylase and N-sulfotransferase activity, and the minimum-sized substrate for the bifunctional activity is a hexasaccharide
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additional information
?
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substrate specificity of recombinant NDST-1 (rNDST-1), full-length enzyme and individual N-deacetylase and N-sulfotransferase domains, with model oligosaccharides, detailed overview. Saccharides N-sulfated by NDST-1 are highly ordered, alternately containing N-S domains and N-Ac domains. Domain cooperation plays an essential role in NDST-1 production of HS with specific structures, and N-deacetylation is the limiting step. Recombinant NDST-1 clearly displayed bifunctional activity, it shows N-deacetylase and N-sulfotransferase activity, and the minimum-sized substrate for the bifunctional activity is a hexasaccharide
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additional information
?
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substrate specificity of recombinant NDST-1 (rNDST-1), full-length enzyme and individual N-deacetylase and N-sulfotransferase domains, with model oligosaccharides, detailed overview. Saccharides N-sulfated by NDST-1 are highly ordered, alternately containing N-S domains and N-Ac domains. Domain cooperation plays an essential role in NDST-1 production of HS with specific structures, and N-deacetylation is the limiting step. Recombinant NDST-1 clearly displayed bifunctional activity, it shows N-deacetylase and N-sulfotransferase activity, and the minimum-sized substrate for the bifunctional activity is a hexasaccharide
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additional information
?
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substrate specificity of recombinant NDST-4 (rNDST-4) with model oligosaccharides, detailed overview. Full-length rNDST-4 lacks obvious N-deacetylase activity, and displays only N-sulfotransferase activity. NDST-4 does not show directional N-sulfotransferase activity and the N-deacetylase domain is inactive. rNDST-4 modified heparosan only contained below 5% disaccharide units with the structure of GlcA-GlcNS. rNDST-4 displays low N-deacetylase activity toward polysaccharide. rNDST-4 is not active with a heptasaccharide substrate or smaller
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additional information
?
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substrate specificity of recombinant NDST-4 (rNDST-4) with model oligosaccharides, detailed overview. Full-length rNDST-4 lacks obvious N-deacetylase activity, and displays only N-sulfotransferase activity. NDST-4 does not show directional N-sulfotransferase activity and the N-deacetylase domain is inactive. rNDST-4 modified heparosan only contained below 5% disaccharide units with the structure of GlcA-GlcNS. rNDST-4 displays low N-deacetylase activity toward polysaccharide. rNDST-4 is not active with a heptasaccharide substrate or smaller
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additional information
?
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substrate specificity of recombinant NDST-4 (rNDST-4) with model oligosaccharides, detailed overview. Full-length rNDST-4 lacks obvious N-deacetylase activity, and displays only N-sulfotransferase activity. NDST-4 does not show directional N-sulfotransferase activity and the N-deacetylase domain is inactive. rNDST-4 modified heparosan only contained below 5% disaccharide units with the structure of GlcA-GlcNS. rNDST-4 displays low N-deacetylase activity toward polysaccharide. rNDST-4 is not active with a heptasaccharide substrate or smaller
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-
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additional information
?
-
the enzyme NDST removes the acetyl group from the GlcNAc residue and transfers a sulfate group to the primary amine forming a GlcNS substitute
-
-
-
additional information
?
-
the enzyme NDST removes the acetyl group from the GlcNAc residue and transfers a sulfate group to the primary amine forming a GlcNS substitute
-
-
-
additional information
?
-
the enzyme NDST removes the acetyl group from the GlcNAc residue and transfers a sulfate group to the primary amine forming a GlcNS substitute
-
-
-
additional information
?
-
the enzyme NDST removes the acetyl group from the GlcNAc residue and transfers a sulfate group to the primary amine forming a GlcNS substitute
-
-
-
additional information
?
-
the enzyme NDST removes the acetyl group from the GlcNAc residue and transfers a sulfate group to the primary amine forming a GlcNS substitute. Isozyme NDST4 has relatively higher sulfotransferase activity and lower N-deacetylase activity
-
-
-
additional information
?
-
the enzyme NDST removes the acetyl group from the GlcNAc residue and transfers a sulfate group to the primary amine forming a GlcNS substitute. Isozyme NDST4 has relatively higher sulfotransferase activity and lower N-deacetylase activity
-
-
-
additional information
?
-
the enzyme NDST removes the acetyl group from the GlcNAc residue and transfers a sulfate group to the primary amine forming a GlcNS substitute. Isozyme NDST4 has relatively higher sulfotransferase activity and lower N-deacetylase activity
-
-
-
additional information
?
-
the enzyme NDST removes the acetyl group from the GlcNAc residue and transfers a sulfate group to the primary amine forming a GlcNS substitute. Isozyme NDST4 has relatively higher sulfotransferase activity and lower N-deacetylase activity
-
-
-
additional information
?
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the enzyme NDST removes the acetyl group from the GlcNAc residue and transfers a sulfate group to the primary amine forming a GlcNS substitute. The catalytic mechanism of NDST1 is responsible for determining the distribution of GlcNS residues in the heparan sulfate (HS) chains. NDST1 binds to its substrates in a random manner, but the processes catalyzed by this enzyme are nonrandom, leading to the formation of specific products in different regions of the chains. During this process, NDST1 can bind to any of the internal GlcNAc residues on the chain. Once the sulfation process has been initiated, NDST1 can then convert the GlcNAc residues to GlcNS residues in sequence from the nonreducing to the reducing end of the chain until it reaches a GlcNS residue located five units away from the reducing end. The establishment of this catalytic model for NDST1 provides direct proof that NDST1 plays a decisive role in the distribution of GlcNS residues
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-
-
additional information
?
-
the enzyme NDST removes the acetyl group from the GlcNAc residue and transfers a sulfate group to the primary amine forming a GlcNS substitute. The catalytic mechanism of NDST1 is responsible for determining the distribution of GlcNS residues in the heparan sulfate (HS) chains. NDST1 binds to its substrates in a random manner, but the processes catalyzed by this enzyme are nonrandom, leading to the formation of specific products in different regions of the chains. During this process, NDST1 can bind to any of the internal GlcNAc residues on the chain. Once the sulfation process has been initiated, NDST1 can then convert the GlcNAc residues to GlcNS residues in sequence from the nonreducing to the reducing end of the chain until it reaches a GlcNS residue located five units away from the reducing end. The establishment of this catalytic model for NDST1 provides direct proof that NDST1 plays a decisive role in the distribution of GlcNS residues
-
-
-
additional information
?
-
the enzyme NDST removes the acetyl group from the GlcNAc residue and transfers a sulfate group to the primary amine forming a GlcNS substitute. The catalytic mechanism of NDST1 is responsible for determining the distribution of GlcNS residues in the heparan sulfate (HS) chains. NDST1 binds to its substrates in a random manner, but the processes catalyzed by this enzyme are nonrandom, leading to the formation of specific products in different regions of the chains. During this process, NDST1 can bind to any of the internal GlcNAc residues on the chain. Once the sulfation process has been initiated, NDST1 can then convert the GlcNAc residues to GlcNS residues in sequence from the nonreducing to the reducing end of the chain until it reaches a GlcNS residue located five units away from the reducing end. The establishment of this catalytic model for NDST1 provides direct proof that NDST1 plays a decisive role in the distribution of GlcNS residues
-
-
-
additional information
?
-
the enzyme NDST removes the acetyl group from the GlcNAc residue and transfers a sulfate group to the primary amine forming a GlcNS substitute. The catalytic mechanism of NDST1 is responsible for determining the distribution of GlcNS residues in the heparan sulfate (HS) chains. NDST1 binds to its substrates in a random manner, but the processes catalyzed by this enzyme are nonrandom, leading to the formation of specific products in different regions of the chains. During this process, NDST1 can bind to any of the internal GlcNAc residues on the chain. Once the sulfation process has been initiated, NDST1 can then convert the GlcNAc residues to GlcNS residues in sequence from the nonreducing to the reducing end of the chain until it reaches a GlcNS residue located five units away from the reducing end. The establishment of this catalytic model for NDST1 provides direct proof that NDST1 plays a decisive role in the distribution of GlcNS residues
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Albuminuria
Modulation of heparan sulfate in the glomerular endothelial glycocalyx decreases leukocyte influx during experimental glomerulonephritis.
Amyotrophic Lateral Sclerosis
NDST3 deacetylates ?-tubulin and suppresses V-ATPase assembly and lysosomal acidification.
Anophthalmos
Heparan sulfate biosynthetic gene Ndst1 is required for FGF signaling in early lens development.
Asthma
Endothelial and leukocyte heparan sulfates regulate the development of allergen-induced airway remodeling in a mouse model.
Ataxia
A girl with developmental delay, ataxia, cranial nerve palsies, severe respiratory problems in infancy-Expanding NDST1 syndrome.
Breast Neoplasms
Methylation-regulated miR-149 modulates chemoresistance by targeting GlcNAc N-deacetylase/N-sulfotransferase-1 in human breast cancer.
Carcinoma
Functional Cellular Anti-Tumor Mechanisms are Augmented by Genetic Proteoglycan Targeting.
Carcinoma
Glycan Sulfation Modulates Dendritic Cell Biology and Tumor Growth.
Carcinoma
Heparan sulfate proteoglycans mediate renal carcinoma metastasis.
Carcinoma
IDUA, NDST1, SAP30L, CRYBA4, and SI as novel prognostic signatures clear cell renal cell carcinoma.
Carcinoma
MicroRNA-191 targets N-deacetylase/N-sulfotransferase 1 and promotes cell growth in human gastric carcinoma cell line MGC803.
Carcinoma, Lewis Lung
Functional Cellular Anti-Tumor Mechanisms are Augmented by Genetic Proteoglycan Targeting.
Carcinoma, Lewis Lung
Glycan Sulfation Modulates Dendritic Cell Biology and Tumor Growth.
Carcinoma, Renal Cell
Heparan sulfate proteoglycans mediate renal carcinoma metastasis.
Carcinoma, Renal Cell
IDUA, NDST1, SAP30L, CRYBA4, and SI as novel prognostic signatures clear cell renal cell carcinoma.
Colorectal Neoplasms
Alteration of colonic epithelial cell differentiation in mice deficient for glucosaminyl N-deacetylase/N-sulfotransferase 4.
Colorectal Neoplasms
NDST4 is a novel candidate tumor suppressor gene at chromosome 4q26 and its genetic loss predicts adverse prognosis in colorectal cancer.
Coronary Disease
Genome-wide association analysis identifies TYW3/CRYZ and NDST4 loci associated with circulating resistin levels.
Cranial Nerve Diseases
A girl with developmental delay, ataxia, cranial nerve palsies, severe respiratory problems in infancy-Expanding NDST1 syndrome.
Craniofacial Abnormalities
A girl with developmental delay, ataxia, cranial nerve palsies, severe respiratory problems in infancy-Expanding NDST1 syndrome.
Demyelinating Diseases
Mature oligodendrocytes bordering lesions limit demyelination and favor myelin repair via heparan sulfate production.
Double Outlet Right Ventricle
Heparan sulfate expression in the neural crest is essential for mouse cardiogenesis.
Embolic Stroke
Integrative Analysis Identified IRF6 and NDST1 as Potential Causal Genes for Ischemic Stroke.
Encephalitis, Japanese
Genome-Wide Screening Uncovers the Significance of N-Sulfation of Heparan Sulfate as a Host Cell Factor for Chikungunya Virus Infection.
Frontotemporal Dementia
NDST3 deacetylates ?-tubulin and suppresses V-ATPase assembly and lysosomal acidification.
Glioblastoma
MiRNA-191 functions as an oncogene in primary glioblastoma by directly targeting NDST1.
Heart Septal Defects, Ventricular
Heparan sulfate expression in the neural crest is essential for mouse cardiogenesis.
Hernias, Diaphragmatic, Congenital
Down-regulation of N-deacetylase-N-sulfotransferase-1 signaling in the developing diaphragmatic vasculature of nitrofen-induced congenital diaphragmatic hernia.
Holoprosencephaly
Integrated clinical and omics approach to rare diseases: novel genes and oligogenic inheritance in holoprosencephaly.
Infections
Enterovirus 71 uses cell surface heparan sulfate glycosaminoglycan as an attachment receptor.
Infections
Genome-Wide Screening Uncovers the Significance of N-Sulfation of Heparan Sulfate as a Host Cell Factor for Chikungunya Virus Infection.
Intellectual Disability
NDST1 missense mutations in autosomal recessive intellectual disability.
Intellectual Disability
Two Cases of Recessive Intellectual Disability Caused by NDST1 and METTL23 Variants.
Ischemic Stroke
Integrative Analysis Identified IRF6 and NDST1 as Potential Causal Genes for Ischemic Stroke.
Mastocytoma
3'-Phosphoadenylylsulfate:N-desulfoheparin sulfotransferase associated with a postmicrosomal particulate mastocytoma fraction.
Mastocytoma
cDNA cloning and sequencing of mouse mastocytoma glucosaminyl N-deacetylase/N-sulfotransferase, an enzyme involved in the biosynthesis of heparin.
Mastocytoma
Molecular cloning and expression of a glycosaminoglycan N-acetylglucosaminyl N-deacetylase/N-sulfotransferase from a heparin-producing cell line.
Melanoma
Decreasing the Susceptibility of Malignant Cells to Infection Does Not Impact the Overall Efficacy of Myxoma Virus-Based Oncolytic Virotherapy.
Melanoma
Epac1 promotes melanoma metastasis via modification of heparan sulfate.
Mucopolysaccharidoses
NDST1 Preferred Promoter Confirmation and Identification of Corresponding Transcriptional Inhibitors as Substrate Reduction Agents for Multiple Mucopolysaccharidosis Disorders.
Neoplasm Metastasis
Heparan sulfate proteoglycans mediate renal carcinoma metastasis.
Neoplasms
Alteration of colonic epithelial cell differentiation in mice deficient for glucosaminyl N-deacetylase/N-sulfotransferase 4.
Neoplasms
Cell surface heparan sulfate promotes replication of Toxoplasma gondii.
Neoplasms
Deep sequencing of a recurrent oligodendroglioma and the derived xenografts reveals new insights into the evolution of human oligodendroglioma and candidate driver genes.
Neoplasms
Functional Importance of a Proteoglycan Coreceptor in Pathologic Lymphangiogenesis.
Neoplasms
Glycan Sulfation Modulates Dendritic Cell Biology and Tumor Growth.
Neoplasms
Heparan sulfate proteoglycans mediate renal carcinoma metastasis.
Neoplasms
Inhibition of thrombosis in melanoma allografts in mice by endogenous mast cell heparin.
Neoplasms
Methylation-regulated miR-149 modulates chemoresistance by targeting GlcNAc N-deacetylase/N-sulfotransferase-1 in human breast cancer.
Neoplasms
NDST4 is a novel candidate tumor suppressor gene at chromosome 4q26 and its genetic loss predicts adverse prognosis in colorectal cancer.
Neoplasms
Transcriptional Activity of Heparan Sulfate Biosynthetic Machinery is Specifically Impaired in Benign Prostate Hyperplasia and Prostate Cancer.
Nephrosis
Altered expression of NDST-1 messenger RNA in puromycin aminonucleoside nephrosis.
Neurodegenerative Diseases
NDST3 deacetylates ?-tubulin and suppresses V-ATPase assembly and lysosomal acidification.
Oligodendroglioma
Deep sequencing of a recurrent oligodendroglioma and the derived xenografts reveals new insights into the evolution of human oligodendroglioma and candidate driver genes.
Paralysis
A girl with developmental delay, ataxia, cranial nerve palsies, severe respiratory problems in infancy-Expanding NDST1 syndrome.
Perinatal Death
Targeted disruption of NDST-1 gene leads to pulmonary hypoplasia and neonatal respiratory distress in mice.
Proteinuria
Altered expression of NDST-1 messenger RNA in puromycin aminonucleoside nephrosis.
Pulmonary Atelectasis
Targeted disruption of NDST-1 gene leads to pulmonary hypoplasia and neonatal respiratory distress in mice.
Respiratory Distress Syndrome, Newborn
Targeted disruption of NDST-1 gene leads to pulmonary hypoplasia and neonatal respiratory distress in mice.
Respiratory Insufficiency
A girl with developmental delay, ataxia, cranial nerve palsies, severe respiratory problems in infancy-Expanding NDST1 syndrome.
Thrombosis
Inhibition of thrombosis in melanoma allografts in mice by endogenous mast cell heparin.
Truncus Arteriosus, Persistent
Heparan sulfate expression in the neural crest is essential for mouse cardiogenesis.
Vascular System Injuries
Heparan sulfate Ndst1 regulates vascular smooth muscle cell proliferation, vessel size and vascular remodeling.
Yellow Fever
Genome-Wide Screening Uncovers the Significance of N-Sulfation of Heparan Sulfate as a Host Cell Factor for Chikungunya Virus Infection.
[heparan sulfate]-glucosamine n-sulfotransferase deficiency
A girl with developmental delay, ataxia, cranial nerve palsies, severe respiratory problems in infancy-Expanding NDST1 syndrome.
[heparan sulfate]-glucosamine n-sulfotransferase deficiency
Alteration of colonic epithelial cell differentiation in mice deficient for glucosaminyl N-deacetylase/N-sulfotransferase 4.
[heparan sulfate]-glucosamine n-sulfotransferase deficiency
Functional Importance of a Proteoglycan Coreceptor in Pathologic Lymphangiogenesis.
[heparan sulfate]-glucosamine n-sulfotransferase deficiency
Heparan sulfate deficiency disrupts developmental angiogenesis and causes congenital diaphragmatic hernia.
[heparan sulfate]-glucosamine n-sulfotransferase deficiency
Loss of the heparan sulfate sulfotransferase, Ndst1, in mammary epithelial cells selectively blocks lobuloalveolar development in mice.
[heparan sulfate]-glucosamine n-sulfotransferase deficiency
Lymphatic endothelial heparan sulfate deficiency results in altered growth responses to VEGF-C.
[heparan sulfate]-glucosamine n-sulfotransferase deficiency
Mice deficient in heparan sulfate N-deacetylase/N-sulfotransferase 1.
[heparan sulfate]-glucosamine n-sulfotransferase deficiency
Selective Deletion of Heparan Sulfotransferase Enzyme, Ndst1, in Donor Endothelial and Myeloid Precursor Cells Significantly Decreases Acute Allograft Rejection.
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predominantly
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brain
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predominantly
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clone E6-1, ATCC TIB-152
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high expression level of isozyme NDST2
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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
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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
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promonocytic leukemia cells
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EXT1, NDST1, and NDST2 differentially regulate heparan sulfate biosynthesis in human tooth germ
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adult
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fetal
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low activity
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adult
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low level in adult brain tissue
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additional information
NDST3 and NDST4 are predominantly expressed during embryonic development, although NDST3 is also found in adult heart and brain tissues, whereas NDST4 is only present at low levels in adult brain tissue
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additional information
NDST3 and NDST4 are predominantly expressed during embryonic development, although NDST3 is also found in adult heart and brain tissues, whereas NDST4 is only present at low levels in adult brain tissue
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additional information
NDST3 and NDST4 are predominantly expressed during embryonic development, although NDST3 is also found in adult heart and brain tissues, whereas NDST4 is only present at low levels in adult brain tissue
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additional information
NDST3 and NDST4 are predominantly expressed during embryonic development, although NDST3 is also found in adult heart and brain tissues, whereas NDST4 is only present at low levels in adult brain tissue
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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
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additional information
NDST3 and NDST4 are predominantly expressed during embryonic development, although NDST3 is also found in adult heart and brain tissues, whereas NDST4 is only present at low levels in adult brain tissue
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additional information
NDST3 and NDST4 are predominantly expressed during embryonic development, although NDST3 is also found in adult heart and brain tissues, whereas NDST4 is only present at low levels in adult brain tissue
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additional information
NDST3 and NDST4 are predominantly expressed during embryonic development, although NDST3 is also found in adult heart and brain tissues, whereas NDST4 is only present at low levels in adult brain tissue
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additional information
NDST3 and NDST4 are predominantly expressed during embryonic development, although NDST3 is also found in adult heart and brain tissues, whereas NDST4 is only present at low levels in adult brain tissue
brenda
additional information
the mRNAs of NDST1 and NDST2 are transcribed in all embryonic and adult tissues, but at different levels during the different stages of development, as well as different organs. NDST1 is widely distributed in the body
brenda
additional information
the mRNAs of NDST1 and NDST2 are transcribed in all embryonic and adult tissues, but at different levels during the different stages of development, as well as different organs. NDST1 is widely distributed in the body
brenda
additional information
the mRNAs of NDST1 and NDST2 are transcribed in all embryonic and adult tissues, but at different levels during the different stages of development, as well as different organs. NDST1 is widely distributed in the body
brenda
additional information
the mRNAs of NDST1 and NDST2 are transcribed in all embryonic and adult tissues, but at different levels during the different stages of development, as well as different organs. NDST1 is widely distributed in the body
brenda
additional information
the mRNAs of NDST1 and NDST2 are transcribed in all embryonic and adult tissues, but at different levels during the different stages of development, as well as different organs. NDST2 is only expressed in connective tissue-type mast cells, which produce heparin in vivo
brenda
additional information
the mRNAs of NDST1 and NDST2 are transcribed in all embryonic and adult tissues, but at different levels during the different stages of development, as well as different organs. NDST2 is only expressed in connective tissue-type mast cells, which produce heparin in vivo
brenda
additional information
the mRNAs of NDST1 and NDST2 are transcribed in all embryonic and adult tissues, but at different levels during the different stages of development, as well as different organs. NDST2 is only expressed in connective tissue-type mast cells, which produce heparin in vivo
brenda
additional information
the mRNAs of NDST1 and NDST2 are transcribed in all embryonic and adult tissues, but at different levels during the different stages of development, as well as different organs. NDST2 is only expressed in connective tissue-type mast cells, which produce heparin in vivo
brenda
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evolution
four NDST isoforms are present in humans
physiological function
heparan sulfate (HS) is widely distributed in mammalian tissues in the form of HS proteoglycans, which play essential roles in various physiological and pathological processes. In contrast to the template-guided processes involved in the synthesis of DNA and proteins, HS biosynthesis is not believed to involve a template. But the final structure of HS chains is strictly regulated. Two major steps, namely coding and decoding steps, are involved in the biosynthesis of HS, which strictly regulate its chemical structure and biological activity. The coding process in this context is based on the distribution of sulfate moieties on the amino groups of the glucosamine residues in the HS chains. The sulfation of these amine groups is catalyzed by N-deacetylase/N-sulfotransferase, which has four isozymes. The composition and distribution of sulfate groups and iduronic acid residues on the glycan chains of HS are determined by several other modification enzymes, which can recognize these coding sequences (i.e. the decoding process). The degree and pattern of the sulfation and epimerization in the HS chains determines the extent of their interactions with several different protein factors, which further influences their biological activity. Mammalian cells can regulate the expression of the four different NDST isozymes as required during the different stages of their development and spatial orientation. In this way, the cells can make use of the different catalytic modes of activity of the NDSTs to adjust the length of the GlcNS clusters on the HS side chains, as well as the ratio of GlcNS to GlcNH2 residues
evolution
four NDST isoforms are present in humans
evolution
four NDST isoforms are present in humans
evolution
four NDST isoforms are present in the human. NDST-1 is the most widely distributed isoform in tissues and organisms, and is considered to exhibit profound physiological functions during all stages of human development
malfunction
a complete lack of NDST1 results in an inability to synthesize HS glycan chains, which is ultimately lethal
malfunction
-
heparan sulfate (HS) is a sulfated polysaccharide that plays a key role in morphogenesis, physiology and pathogenesis. The biosynthesis of HS takes place in the Golgi apparatus by a group of enzymes that polymerize, epimerize and sulfate the sugar chain. This biosynthetic process introduces varying degrees of sulfate substitution, which are tightly regulated and directly dictate binding specificity to different cytokines, morphogens and growth factors. Molecular dynamics simulations to investigate the dynamics of substrate recognition of two glycosaminoglycan (GAG) sulfotransferases, N-deacetylase-N-sulfotransferase and 2-O-sulfotransferaseto the HS chain during the biosynthetic process. Fine-tuned complex mechanism of GAG biosynthesis
metabolism
-
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
metabolism
the enzymes is involved in heparan sulfate biosynthesis. EXT1, NDST1, and NDST2 differentially regulate heparan sulfate biosynthesis in human tooth germ
physiological function
-
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
physiological function
the enzyme is involved in heparan sulfate biosynthesis
physiological function
heparan sulfate (HS) is widely distributed in mammalian tissues in the form of HS proteoglycans, which play essential roles in various physiological and pathological processes. In contrast to the template-guided processes involved in the synthesis of DNA and proteins, HS biosynthesis is not believed to involve a template. But the final structure of HS chains is strictly regulated. Two major steps, namely coding and decoding steps, are involved in the biosynthesis of HS, which strictly regulate its chemical structure and biological activity. The coding process in this context is based on the distribution of sulfate moieties on the amino groups of the glucosamine residues in the HS chains. The sulfation of these amine groups is catalyzed by N-deacetylase/N-sulfotransferase, which has four isozymes. The composition and distribution of sulfate groups and iduronic acid residues on the glycan chains of HS are determined by several other modification enzymes, which can recognize these coding sequences (i.e. the decoding process). The degree and pattern of the sulfation and epimerization in the HS chains determines the extent of their interactions with several different protein factors, which further influences their biological activity. Mammalian cells can regulate the expression of the four different NDST isozymes as required during the different stages of their development and spatial orientation. In this way, the cells can make use of the different catalytic modes of activity of the NDSTs to adjust the length of the GlcNS clusters on the HS side chains, as well as the ratio of GlcNS to GlcNH2 residues
physiological function
-
NDST, the first modifying enzyme, removes the acetyl group from GlcNAc and adds a sulfate group, generating N-sulfoglucosamine (GlcNS). The generation of GlcNS introduces N-sulfated (NS) domains along the HS chain. When these NS domains are flanked by unmodified N-acetylated domains (NA domains) NA/NS domains are generated. This organization specifies different protein-binding motifs, overview
physiological function
NDSTs are potential bifunctional enzymes that contain two independent catalytic domains: the N-deacetylase domain removes the acetyl group from GlcNAc to form GlcNH2, and the N-sulfo-transferase domain transfers a sulfo group to the GlcNH2 residue to form GlcNS. The enzyme is involved in the synthesis of heparan sulfate (HS), a highly sulfated linear glycosaminoglycan polysaccharide, consisting of a disaccharide repeating unit of sulfated derivatives of glucosamine and glucuronic acid (GlcA) or iduronic acid (IdoA) residues. HS is widely present in proteoglycan saccharide chains in mammalian tissues and the extracellular matrix. The final structure of HS chains is strictly regulated in vivo, though the biosynthesis is not guided by a template process. N-Deacetylase/N-sulfotransferase (NDST) is the first modification enzyme in the HS biosynthetic pathway. The N-sulfo groups introduced by NDST are reportedly involved in determination of the susceptibility to subsequent processes catalyzed by C5-epimerse and 3-O-sulfotranferases. NDST-4 plays a limited role in heparan sulfate biosynthesis
physiological function
NDSTs are potential bifunctional enzymes that contain two independent catalytic domains: the N-deacetylase domain removes the acetyl group from GlcNAc to form GlcNH2, and the N-sulfo-transferase domain transfers a sulfo group to the GlcNH2 residue to form GlcNS. The enzyme is involved in the synthesis of heparan sulfate (HS), a highly sulfated linear glycosaminoglycan polysaccharide, consisting of a disaccharide repeating unit of sulfated derivatives of glucosamine and glucuronic acid (GlcA) or iduronic acid (IdoA) residues. HS is widely present in proteoglycan saccharide chains in mammalian tissues and the extracellular matrix. The final structure of HS chains is strictly regulated in vivo, though the biosynthesis is not guided by a template process. N-Deacetylase/N-sulfotransferase (NDST) is the first modification enzyme in the HS biosynthetic pathway. The N-sulfo groups introduced by NDST are reportedly involved in determination of the susceptibility to subsequent processes catalyzed by C5-epimerse and 3-O-sulfotranferases
additional information
analysis of the mode of action of NDST-4
additional information
analysis of the mode of action of NDST-4
additional information
-
analysis of the mode of action of NDST-4
additional information
NDST-1 has two catalytic domains
additional information
NDST-1 has two catalytic domains
additional information
-
NDST-1 has two catalytic domains
additional information
-
sulfotransferases contain a conserved interspaced positively charged amino acid residues that form a patch which controls the protein-GAG binding equilibrium. The amphipathic random coil positions the putative charged active site residue side chains of Glu641 and Glu642 toward the center of the cleft, while the opposing region of the cleft contains side chains of residues required for binding, His716, Gln717 and His720, molecular dynamics simulations
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K614A
-
site-directed mutagenesis of the sulfotransferase domain of the bifunctional enzyme, complete loss of N-sulfotransferase activity
additional information
-
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
additional information
overexpression of NDST1 or NDST2 in recombinant human embryonic kidney 293 cells gives rise to different heparan sulfate (HS) N-sulfation patterns. The HS produced in cells transfected with NDST1 and NDST2 typically shows increased levels of N-sulfation. However, compared with cells overexpressing NDST1, the HS generated by cells overexpressing NDST2 has longer N-sulfation regions and a higher degree of N-sulfation
additional information
overexpression of NDST1 or NDST2 in recombinant human embryonic kidney 293 cells gives rise to different heparan sulfate (HS) N-sulfation patterns. The HS produced in cells transfected with NDST1 and NDST2 typically shows increased levels of N-sulfation. However, compared with cells overexpressing NDST1, the HS generated by cells overexpressing NDST2 has longer N-sulfation regions and a higher degree of N-sulfation
additional information
overexpression of NDST1 or NDST2 in recombinant human embryonic kidney 293 cells gives rise to different heparan sulfate (HS) N-sulfation patterns. The HS produced in cells transfected with NDST1 and NDST2 typically shows increased levels of N-sulfation. However, compared with cells overexpressing NDST1, the HS generated by cells overexpressing NDST2 has longer N-sulfation regions and a higher degree of N-sulfation
additional information
overexpression of NDST1 or NDST2 in recombinant human embryonic kidney 293 cells gives rise to different heparan sulfate (HS) N-sulfation patterns. The HS produced in cells transfected with NDST1 and NDST2 typically shows increased levels of N-sulfation. However, compared with cells overexpressing NDST1, the HS generated by cells overexpressing NDST2 has longer N-sulfation regions and a higher degree of N-sulfation
additional information
overexpression of NDST1 or NDST2 in recombinant human embryonic kidney 293 cells gives rise to different heparan sulfate (HS) N-sulfation patterns. The HS produced in cells transfected with NDST1 and NDST2 typically shows increased levels of N-sulfation. However, compared with cells overexpressing NDST1, the HS generated by cells overexpressing NDST2 has longer N-sulfation regions and a higher degree of N-sulfation. Furthermore, the transfection of NDST-deficient COS cells with NDST1 results in the formation of HS with a high affinity for FGF. In contrast, the overexpression of NDST1 in wild-type COS cells has very little effect on the N-acetylation to N-sulfation ratio of HS
additional information
overexpression of NDST1 or NDST2 in recombinant human embryonic kidney 293 cells gives rise to different heparan sulfate (HS) N-sulfation patterns. The HS produced in cells transfected with NDST1 and NDST2 typically shows increased levels of N-sulfation. However, compared with cells overexpressing NDST1, the HS generated by cells overexpressing NDST2 has longer N-sulfation regions and a higher degree of N-sulfation. Furthermore, the transfection of NDST-deficient COS cells with NDST1 results in the formation of HS with a high affinity for FGF. In contrast, the overexpression of NDST1 in wild-type COS cells has very little effect on the N-acetylation to N-sulfation ratio of HS
additional information
overexpression of NDST1 or NDST2 in recombinant human embryonic kidney 293 cells gives rise to different heparan sulfate (HS) N-sulfation patterns. The HS produced in cells transfected with NDST1 and NDST2 typically shows increased levels of N-sulfation. However, compared with cells overexpressing NDST1, the HS generated by cells overexpressing NDST2 has longer N-sulfation regions and a higher degree of N-sulfation. Furthermore, the transfection of NDST-deficient COS cells with NDST1 results in the formation of HS with a high affinity for FGF. In contrast, the overexpression of NDST1 in wild-type COS cells has very little effect on the N-acetylation to N-sulfation ratio of HS
additional information
overexpression of NDST1 or NDST2 in recombinant human embryonic kidney 293 cells gives rise to different heparan sulfate (HS) N-sulfation patterns. The HS produced in cells transfected with NDST1 and NDST2 typically shows increased levels of N-sulfation. However, compared with cells overexpressing NDST1, the HS generated by cells overexpressing NDST2 has longer N-sulfation regions and a higher degree of N-sulfation. Furthermore, the transfection of NDST-deficient COS cells with NDST1 results in the formation of HS with a high affinity for FGF. In contrast, the overexpression of NDST1 in wild-type COS cells has very little effect on the N-acetylation to N-sulfation ratio of HS
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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.
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211-214
1998
Homo sapiens
brenda
Kakuta, Y.; Sueyoshi, T.; Negishi, M.; Pedersen, L.C.
Crystal structure of the sulfotransferase domain of human heparan sulfate N-deacetylase/N-sulfotransferase 1
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274
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1999
Homo sapiens
brenda
Aikawa, J.; Esko, J.D.
Molecular cloning and expression of a third member of the heparan sulfate/heparin GlcNAc N-deacetylase/N-sulfotransferase family
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274
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Cricetulus griseus, Homo sapiens (O95803), Homo sapiens
brenda
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
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Homo sapiens
brenda
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
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276
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Homo sapiens (O95803), Homo sapiens (Q9H3R1), Homo sapiens, Mus musculus (P52850), Mus musculus (Q3UHN9), Mus musculus (Q9EQH7), Mus musculus (Q9EQW8), Mus musculus
brenda
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
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2002
Caenorhabditis elegans, Drosophila melanogaster, Homo sapiens, Homo sapiens (O95803), Homo sapiens (Q9H3R1), Mus musculus, Mus musculus (Q9EQW8), vertebrata
brenda
Duncan, M.B.; Liu, M.; Fox, C.; Liu, J.
Characterization of the N-deacetylase domain from the heparan sulfate N-deacetylase/N-sulfotransferase 2
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339
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Homo sapiens
brenda
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
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Homo sapiens
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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
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290
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2015
Homo sapiens (P52848)
brenda
Kero, D.; Bilandzija, T.; Arapovic, L.; Vukojevic, K.; Saraga-Babic, M.
Syndecans and enzymes involved in heparan sulfate biosynthesis and degradation are differentially expressed during human dontogenesis
Front. Physiol.
9
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Homo sapiens (P52848), Homo sapiens (P52849), Homo sapiens
brenda
Ushakov, V.; Tsidulko, A.; De La Bourdonnaye, G.; Kazanskaya, G.; Volkov, A.; Kiselev, R.; Kobozev, V.; Kostromskaya, D.; Gaytan, A.; Krivoshapkin, A.; Aidagulova, S.; Grigorieva, E.
Heparan sulfate biosynthetic system is inhibited in human glioma due to EXT1/2 and HS6ST1/2 down-regulation
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18
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2017
Homo sapiens (P52848), Homo sapiens (P52849)
brenda
Li, Y.J.; Yin, F.X.; Zhang, X.K.; Yu, J.; Zheng, S.; Song, X.L.; Wang, F.S.; Sheng, J.Z.
Characterization of heparan sulfate N-deacetylase/N-sulfotransferase isoform 4 using synthetic oligosaccharide substrates
Biochim. Biophys. Acta
1862
547-556
2018
Homo sapiens (P52848), Homo sapiens (Q9H3R1), Homo sapiens
brenda
Zhang, X.; Wang, F.; Sheng, J.
''Coding'' and ''Decoding'' hypothesis for the regulatory mechanism involved in heparan sulfate biosynthesis
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brenda
Gesteira, T.F.; Coulson-Thomas, V.J.
Structural basis of oligosaccharide processing by glycosaminoglycan sulfotransferases
Glycobiology
28
885-897
2018
Homo sapiens
brenda