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Literature summary for 2.8.2.35 extracted from

  • Tykesson, E.; Hassinen, A.; Zielinska, K.; Thelin, M.A.; Frati, G.; Ellervik, U.; Westergren-Thorsson, G.; Malmstroem, A.; Kellokumpu, S.; Maccarana, M.
    Dermatan sulfate epimerase 1 and dermatan 4-O-sulfotransferase 1 form complexes that generate long epimerized 4-O-sulfated blocks (2018), J. Biol. Chem., 293, 13725-13735 .
    View publication on PubMedView publication on EuropePMC
Search for more literature for 2.8.2.35

Cloned(Commentary)

Cloned (Comment) Organism
gene D4ST1, quantitative RT-PCR enzyme expression analysis, overexpression of enzyme D4ST1 in COS-7 cells, co-expression with dermatan sulfate epimerases DS-epi1 and DS-epi2 Homo sapiens

Localization

Localization Comment Organism GeneOntology No. Textmining
Golgi apparatus co-localization with dermatan sulfate epimerase 1 (DS-epi1) Homo sapiens 5794
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Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3'-phospho-5'-adenylyl sulfate + [dermatan]-N-acetyl-D-galactosamine Homo sapiens
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 adenosine 3',5'-bisphosphate + [dermatan]-4-O-sulfo-N-acetyl-D-galactosamine
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 ?
additional information Homo sapiens dermatan sulfate epimerase 1 and dermatan 4-O-sulfotransferase 1 form complexes that generate long epimerized 4-O-sulfated blocks ?
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Organism

Organism UniProt Comment Textmining
Homo sapiens Q8NCH0
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3'-phospho-5'-adenylyl sulfate + [dermatan]-N-acetyl-D-galactosamine
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 Homo sapiens adenosine 3',5'-bisphosphate + [dermatan]-4-O-sulfo-N-acetyl-D-galactosamine
-
 ?
additional information dermatan sulfate epimerase 1 and dermatan 4-O-sulfotransferase 1 form complexes that generate long epimerized 4-O-sulfated blocks Homo sapiens ?
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Synonyms

Synonyms Comment Organism
D4ST1
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 Homo sapiens
dermatan 4-O-sulfotransferase 1
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 Homo sapiens

General Information

General Information Comment Organism
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 Homo sapiens