Information on EC 2.8.2.35 - dermatan 4-sulfotransferase

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Word Map on EC 2.8.2.35
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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
2.8.2.35
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RECOMMENDED NAME
GeneOntology No.
dermatan 4-sulfotransferase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
3'-phospho-5'-adenylyl sulfate + [dermatan]-N-acetyl-D-galactosamine = adenosine 3',5'-bisphosphate + [dermatan]-4-O-sulfo-N-acetyl-D-galactosamine
show the reaction diagram
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
dermatan sulfate biosynthesis (late stages)
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Glycosaminoglycan biosynthesis - chondroitin sulfate / dermatan sulfate
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SYSTEMATIC NAME
IUBMB Comments
3'-phospho-5'-adenylyl sulfate:[dermatan]-N-acetyl-D-galactosamine 4-sulfotransferase
The sulfation takes place at the 4-position of N-acetyl-D-galactosamine residues of dermatan. D4ST-1 shows a strong preference in vitro for sulfate transfer to IdoUAalpha(1,3)GalNAcbeta(1,4) that is flanked by GlcUAbeta(1,3)GalNAcbeta(1,4) as compared with IdoUAalpha(1,3)GalNAcbeta(1,4) flanked by IdoUAalpha(1,3)GalNAcbeta(1,4) [1].
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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Manually annotated by BRENDA team
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UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
physiological function
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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
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
3'-phospho-5'-adenylyl sulfate + [dermatan]-N-acetyl-D-galactosamine
adenosine 3',5'-bisphosphate + [dermatan]-4-O-sulfo-N-acetyl-D-galactosamine
show the reaction diagram
3'-phospho-5'-adenylyl sulfate + [dermatan]-N-acetylgalactosamine
adenosine 3'-5'-bisphosphate + [dermatan]-4-O-sulfo-N-acetylgalactosamine
show the reaction diagram
additional information
?
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the enzyme catalyzes the 4-O-sulfation of N-acetylgalactosamine in the repeating iduronic acid-alpha-1,3-N-acetylgalactosamine disaccharide sequence to form dermatan sulfate
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
3'-phospho-5'-adenylyl sulfate + [dermatan]-N-acetyl-D-galactosamine
adenosine 3',5'-bisphosphate + [dermatan]-4-O-sulfo-N-acetyl-D-galactosamine
show the reaction diagram
3'-phospho-5'-adenylyl sulfate + [dermatan]-N-acetylgalactosamine
adenosine 3'-5'-bisphosphate + [dermatan]-4-O-sulfo-N-acetylgalactosamine
show the reaction diagram
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?
additional information
?
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the enzyme catalyzes the 4-O-sulfation of N-acetylgalactosamine in the repeating iduronic acid-alpha-1,3-N-acetylgalactosamine disaccharide sequence to form dermatan sulfate
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.8
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assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37
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assay at
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
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no change in activity in dermatan 4-O sulfotransferase is observed, and only a minor decrease in dermatan 4-O-sulfotransferase-1 (D4ST-1) mRNA is observed after treatment with with transforming growth factor-beta (TGF-beta)
Manually annotated by BRENDA team
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low levels
Manually annotated by BRENDA team
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fetal, most highly expressed
Manually annotated by BRENDA team
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most highly expressed
Manually annotated by BRENDA team
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most highly expressed
Manually annotated by BRENDA team
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low levels
Manually annotated by BRENDA team
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most highly expressed
Manually annotated by BRENDA team
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most highly expressed
Manually annotated by BRENDA team
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most highly expressed
Manually annotated by BRENDA team
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Cos-1 cells
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
downregulation of D4ST-1 in primary human lung fibroblasts leads to a drastic specific reduction of iduronic acid blocks. No change of epimerase activity is found, indicating that the influence of D4ST-1 on epimerization is not due to an altered expression level of the DS-epimerases. Analysis of the dermatan sulfate chains shows that D4ST-1 is essential for the biosynthesis of the disulfated structure iduronic acid-2-O-sulfate-N-acetylgalactosamine-4-O-sulfate, thus confirmed to be strictly connected with the iduronic acid blocks. Also the biologically important residue hexuronic acid-N-acetylgalactosamine-4,6-O-disulfate considerably decreases after D4ST-1 downregulation
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