This enzyme sulfates the residues marked with an asterisk in sequences containing at least -> IdoA2S-> GlcN*-> or -> GlcA2S-> GlcN*-> (symbols as in {iupac/2carb/38::2-Carb-38}). Preference for GlcN2S vs. unmodified GlcN has not yet been established. Additional structural features are presumably required for substrate recognition, since the 3-O-sulfated residue is of low abundance, whereas the above IdoA-containing sequence is quite abundant. This enzyme differs from the other [heparan sulfate]-glucosamine 3-sulfotransferases by modifying selected glucosamine residues preceded by GlcA2S; EC 2.8.2.23 ([heparan sulfate]-glucosamine 3-sulfotransferase 1) prefers GlcA or IdoA, whereas EC 2.8.2.30 ([heparan sulfate]-glucosamine 3-sulfotransferase 3) prefers IdoA2S.
This enzyme sulfates the residues marked with an asterisk in sequences containing at least IdoA2S-GlcN*- or ?GlcA2S.GlcN*-. Preference for GlcN2S vs. unmodified GlcN has not yet been established. Additional structural features are presumably required for substrate recognition, since the 3-O-sulfated residue is of low abundance, whereas the above IdoA-containing sequence is quite abundant. This enzyme differs from the other, [heparan sulfate]-glucosamine 3-sulfotransferases by modifying selected glucosamines residues preceded by GlcA2S. EC 2.8.2.23, [heparan sulfate]-glucosamine 3-sulfotransferase 1, prefers GlcA or IdoA, whereas EC 2.8.2.30, [heparan sulfate]-glucosamine 3-sulfotransferase 3, prefers IdoAS
This enzyme sulfates the residues marked with an asterisk in sequences containing at least -> IdoA2S-> GlcN*-> or -> GlcA2S-> GlcN*-> (symbols as in {iupac/2carb/38::2-Carb-38}). Preference for GlcN2S vs. unmodified GlcN has not yet been established. Additional structural features are presumably required for substrate recognition, since the 3-O-sulfated residue is of low abundance, whereas the above IdoA-containing sequence is quite abundant. This enzyme differs from the other [heparan sulfate]-glucosamine 3-sulfotransferases by modifying selected glucosamine residues preceded by GlcA2S; EC 2.8.2.23 ([heparan sulfate]-glucosamine 3-sulfotransferase 1) prefers GlcA or IdoA, whereas EC 2.8.2.30 ([heparan sulfate]-glucosamine 3-sulfotransferase 3) prefers IdoA2S.
i.e. HSgD+, 3-O-sulfated motifs that bind the gD envelope protein of Herpes simplex virus 1 mediating the viral cellular entry, overview, i.e. HSgD+, 3-O-sulfated motifs that bind the gD envelope protein of Herpes simplex virus 1
heparan sulfate chains contain sulfated domains termed the HS fine structure, which gives HS specific binding affinities for extracellular ligands, heparan sulfate 3-O-sulfotransferases catalyze the transfer of sulfate groups to the 3-O position of glucosamine residues of heparan sulfate, a rare, but essential heparan sulfate chain modification required for HS fine structure
modification of heparan sulfate and the ability of 3-OST-2 to generate receptors for both wild-types and some mutant forms of HSV-1, spreading of receptors mediating cell-to-cell fusion
HSV-1 glycoprotein gD, both the wild-type and the mutant Rid1 form, can interact with [heparan sulfate]-glucosamine 3-sulfate generated by HS 3-OST-2, overview
heparan sulfate chains contain sulfated domains termed the HS fine structure, which gives HS specific binding affinities for extracellular ligands, heparan sulfate 3-O-sulfotransferases catalyze the transfer of sulfate groups to the 3-O position of glucosamine residues of heparan sulfate, a rare, but essential heparan sulfate chain modification required for HS fine structure
modification of heparan sulfate and the ability of 3-OST-2 to generate receptors for both wild-types and some mutant forms of HSV-1, spreading of receptors mediating cell-to-cell fusion
Methylation-associated silencing of heparan sulfate D-glucosaminyl 3-O-sulfotransferase-2 (3-OST-2) in human breast, colon, lung and pancreatic cancers.
The Pro-Tumoral Activity of Heparan Sulfate 3-O-Sulfotransferase 3B (HS3ST3B) in Breast Cancer MDA-MB-231 Cells Is Dependent on the Expression of Neuropilin-1.
Epigenetics: methylation-associated repression of heparan sulfate 3-O-sulfotransferase gene expression contributes to the invasive phenotype of H-EMC-SS chondrosarcoma cells.
Methylation-associated silencing of heparan sulfate D-glucosaminyl 3-O-sulfotransferase-2 (3-OST-2) in human breast, colon, lung and pancreatic cancers.
Methylation-associated silencing of heparan sulfate D-glucosaminyl 3-O-sulfotransferase-2 (3-OST-2) in human breast, colon, lung and pancreatic cancers.
Promoter hypermethylation of HS3ST2, SEPTIN9 and SLIT2 combined with FGFR3 mutations as a sensitive/specific urinary assay for diagnosis and surveillance in patients with low or high-risk non-muscle-invasive bladder cancer.
developmental expression analysis of the 3-OST gene family, mRNA expression patterns in several tissues/organs throughout early zebrafish development, including early cleavage stages, somites, brain, internal body organ primordial, and pectoral fin development, overview
3-O-sulfotransferase-2-generated heparan sulfate serves as a receptor during herpes simplex virus type-1 entry and spread. The enzyme plays a role in HSV-1 pathogenesis
expression of 3-OST-2 renders CHO-K1 cell, which are normally resistant, susceptible to viral entry of wild-type and a Q27P mutant, Rid1, forms of HSV-1, requiring the gD receptors, Rid1 mutation at gD prevents its entry via some receptors including HVEM and 3-OS HS generated by 3-OST-3, overview
DNA and amino acid sequence determination and analysis and developmental expression analysis of the 3-OST gene family, sequence comparisons, phylogentic analysis, overview
the results provide evidence for specific epigenetic regulation of 3-OST genes resulting in altered heparan sulfate proteoglycans and point to a defect of heparan sulfate-3-O-sulfation as a factor in cancer progression
Methylation-associated silencing of heparan sulfate D-glucosaminyl 3-O-sulfotransferase-2 (3-OST-2) in human breast, colon, lung and pancreatic cancers
Bui, C.; Ouzzine, M.; Talhaoui, I.; Sharp, S.; Prydz, K.; Coughtrie, M.W.; Fournel-Gigleux, S.
Epigenetics: methylation-associated repression of heparan sulfate 3-O-sulfotransferase gene expression contributes to the invasive phenotype of H-EMC-SS chondrosarcoma cells
Comprehensive analysis of herpes simplex virus 1 (HSV-1) entry mediated by zebrafish 3-O-sulfotransferase isoforms: implications for the development of a zebrafish model of HSV-1 infection
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2.8.2.29 [heparan sulfate]-glucosamine 3-sulfotransferase 2
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