Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 2.8.2.8 extracted from

  • Gesteira, T.F.; Coulson-Thomas, V.J.
    Structural basis of oligosaccharide processing by glycosaminoglycan sulfotransferases (2018), Glycobiology, 28, 885-897 .
    View publication on PubMed
Search for more literature for 2.8.2.8

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
 additional information binding kinetics, ligand-binding free energy calculations, modeling Homo sapiens

Localization

Localization Comment Organism GeneOntology No. Textmining
Golgi apparatus
-
 Homo sapiens 5794
-

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3'-phosphoadenylyl sulfate + [heparan sulfate]-glucosamine Homo sapiens
-
 adenosine 3',5'-bisphosphate + [heparan sulfate]-N-sulfoglucosamine
-
 ?

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
-
-

Reaction

Reaction Comment Organism Reaction ID
3'-phosphoadenylyl sulfate + [heparan sulfate]-glucosamine = adenosine 3',5'-bisphosphate + [heparan sulfate]-N-sulfoglucosamine complex mechanism of GAG biosynthesis, mechanism of forward motion and hydrogen bond network analysis, overview Homo sapiens
a

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3'-phosphoadenylyl sulfate + [heparan sulfate]-glucosamine
-
 Homo sapiens adenosine 3',5'-bisphosphate + [heparan sulfate]-N-sulfoglucosamine
-
 ?
additional information substrate binding structures, overview Homo sapiens ?
-
-

Synonyms

Synonyms Comment Organism
GAG sulfotransferase
-
 Homo sapiens
glycosaminoglycan sulfotransferase
-
 Homo sapiens
NDST
-
 Homo sapiens

General Information

General Information Comment Organism
malfunction heparan sulfate (HS) is a sulfated polysaccharide that plays a key role in morphogenesis, physiology and pathogenesis. The biosynthesis of HS takes place in the Golgi apparatus by a group of enzymes that polymerize, epimerize and sulfate the sugar chain. This biosynthetic process introduces varying degrees of sulfate substitution, which are tightly regulated and directly dictate binding specificity to different cytokines, morphogens and growth factors. Molecular dynamics simulations to investigate the dynamics of substrate recognition of two glycosaminoglycan (GAG) sulfotransferases, N-deacetylase-N-sulfotransferase and 2-O-sulfotransferaseto the HS chain during the biosynthetic process. Fine-tuned complex mechanism of GAG biosynthesis Homo sapiens
additional information sulfotransferases contain a conserved interspaced positively charged amino acid residues that form a patch which controls the protein-GAG binding equilibrium. The amphipathic random coil positions the putative charged active site residue side chains of Glu641 and Glu642 toward the center of the cleft, while the opposing region of the cleft contains side chains of residues required for binding, His716, Gln717 and His720, molecular dynamics simulations Homo sapiens
physiological function NDST, the first modifying enzyme, removes the acetyl group from GlcNAc and adds a sulfate group, generating N-sulfoglucosamine (GlcNS). The generation of GlcNS introduces N-sulfated (NS) domains along the HS chain. When these NS domains are flanked by unmodified N-acetylated domains (NA domains) NA/NS domains are generated. This organization specifies different protein-binding motifs, overview Homo sapiens