EC Number   |
General Information |
Reference |
|---|
    2.8.2.35 | malfunction |
adducted thumb-clubfoot syndrome is caused by homozygous nonsense and missense mutations in CHST14 which encodes N-acetylgalactosamine 4-O-sulfotransferase 1 leading to congenital malformations, contractures of thumbs and feet, and a typical facial appearance |
726422 |
| 2.8.2.35 | malfunction |
adducted thumb-clubfoot syndrome is genetically homogeneous and is caused by loss-of-function mutations in CHST14 leading to a deficiency of sulfated dermatan in affected tissues |
701609 |
| 2.8.2.35 | malfunction |
enzyme deficiency results in impaired neuronal differentiation and diminished neural stem cell proliferation both in vitro and in vivo, associated with an upregulation of the expression of epidermal growth factor receptor and fibroblast growth factor receptor 1and changes in distinct subpopulations of radial glial cells |
725595 |
| 2.8.2.35 | malfunction |
germline ablation of dermatan-4O-sulfotransferase1 reduces regeneration after mouse spinal cord injury |
739179 |
| 2.8.2.35 | metabolism |
During the biosynthesis of chondroitin/dermatan sulfate (CS/DS), a variable fraction of glucuronic acid is converted to iduronic acid through the activities of two epimerases, dermatan sulfate epimerases 1 (DS-epi1) and 2 (DS-epi2). Without association with other enzymes, DS-epi1 activity produces structures that have only a few adjacent iduronic acid units. In vivo, concomitant with epimerization, dermatan 4-O-sulfotransferase 1 (D4ST1) sulfates the GalNAc adjacent to iduronic acid. This sulfation facilitates DSepi1 activity and enables the formation of long blocks of sulfated iduronic acid-containing domains, which can be major components of CS/DS. Concerted action of DS-epi1 and D4ST1. D4ST1 directly interacts with DS-epi1, but not with DS-epi2. The iduronic acid-forming enzymes operate in complexes, similar to other enzymes active in glycosaminoglycan biosynthesis. siRNA-mediated reduction of DS-epi2 in MCF 10a cells results in a marked reduction of the two epimerases and IdoA biosynthesis |
761482 |
| 2.8.2.35 | physiological function |
D4ST-1 is indispensable in the formation of the important functional domains composed of alternating iduronic acid and 4-O-sulfated N-acetylgalactosamine residues (named 4-O-sulfated iduronic acid blocks) in dermatan sulfate and cannot be compensated by other 4-O-sulfotransferases |
703888 |
