EC Number   |
General Information |
Reference |
|---|
   2.8.2.23 | evolution |
HS3STs represent the largest family of HS-modifying enzymes, and yet the reaction of 3-O-sulfation is the rarest maturation step, when compared to other sulfations. Seven HS3STs have been characterized in human, for which the expression is dependent on cell type and tissue environment |
761164 |
| 2.8.2.23 | evolution |
significant structural similarity between sHs and the human heparan sulfate 3-O-suIfotransferase isoform 5, phylogenetic analysis. The enzyme from Litopenaeus vannamei belongs to the O-sulfotransferase family |
762088 |
| 2.8.2.23 | malfunction |
enhanced 3-O-sulfation increases binding to antithrombin, which enhances Factor Xa inhibition, and binding of neuropilin-1 |
762294 |
| 2.8.2.23 | malfunction |
expression of the genes encoding HS-modifying enzymes is frequently dysregulated in cancer and other diseases. The enzymes show either anti-oncogenic or tumor-promoting effects |
761164 |
| 2.8.2.23 | malfunction |
expression of the genes encoding HS-modifying enzymes is frequently dysregulated in cancer and other diseases. The enzymes show either anti-oncogenic or tumor-promoting effects. Hypermethylation in proximal regions of the HS3ST1 gene in chondrosarcoma. Exposure to a demethylating agent restores its expression, confirming that aberrant methylation has affected its transcription |
761164 |
| 2.8.2.23 | malfunction |
expression of the genes encoding HS-modifying enzymes is frequently dysregulated in cancer and other diseases. The enzymes show either anti-oncogenic or tumor-promoting effects. Re-expression of HS3ST4 in MDA-MB-231 cells leads to an increase in cell viability and invasion, MDA-MB-231 cells carrying HS3ST4 expression display a significant increase in proliferation and survival |
761164 |
| 2.8.2.23 | metabolism |
HS3ST-mediated 3-O-sulfation leads to at least two distinct forms of 3-O-sulfated motifs. HS3ST1 and HS3ST5 participate in the generation of anticoagulant-active HS/heparin sequences for antithrombin-III, while HS3ST2, HS3ST3A, HS3ST3B, HS3ST4, and HS3ST6 are described to provide the HS-binding motifs for the glycoprotein gD of herpes simplex virus-1 (HSV-1). HS3ST regulations in cancer cells, cell proliferation, and tumor progression, overview |
761164 |
| 2.8.2.23 | metabolism |
role of 3-O-sulfotransferase in heparan sulfate biosynthesis. 3-O-sulfation can occur in distinct biosynthetic steps either being the last HS sulfotransferase in the biosynthesis process or the first one in a non-hierarchical way, according to the oligosaccharides tested |
762088 |
| 2.8.2.23 | metabolism |
the sulfation at the 3-OH position of glucosamine is an important modification in forming structural domains for heparan sulfate to enable its biological functions. Seven 3-O-sulfotransferase isoforms in the human genome are involved in the biosynthesis of 3-O-sulfated heparan sulfate |
761349 |
| 2.8.2.23 | metabolism |
ZNF263, a C2H2 zinc finger protein, is a negative transcriptional regulator of heparin and heparan sulfate biosynthesis, which shows distinctively low expression in mast cells compared with other (non-heparin-producing) immune cells. ZNF263 is a transcriptional repressor, and its inactivation or silencing enhances mRNA expression of HS3ST1 and HS3ST3A1 (EC 2.8.2.30), enzymes involved in the formation of binding sites for antithrombin and neuropilin-1 (NRP1) and glycoprotein D of herpes simplex virus, respectively. Heparan sulfate (HS) biosynthetic genes exhibit the ZNF263 consensus motif |
762294 |
