EC Number |
Reaction |
Reference |
---|
2.8.2.8 | 3'-phosphoadenylyl sulfate + [heparan sulfate]-glucosamine = adenosine 3',5'-bisphosphate + [heparan sulfate]-N-sulfoglucosamine |
5'-phosphate binding and active site structure |
645940 |
2.8.2.8 | 3'-phosphoadenylyl sulfate + [heparan sulfate]-glucosamine = adenosine 3',5'-bisphosphate + [heparan sulfate]-N-sulfoglucosamine |
binding mechanism, interaction scheme, sulfuryl transfer mechanism |
645942 |
2.8.2.8 | 3'-phosphoadenylyl sulfate + [heparan sulfate]-glucosamine = adenosine 3',5'-bisphosphate + [heparan sulfate]-N-sulfoglucosamine |
comparison of catalytic mechanism aspects of the NDST isozymes, overview |
760812 |
2.8.2.8 | 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 |
761218 |
2.8.2.8 | 3'-phosphoadenylyl sulfate + [heparan sulfate]-glucosamine = adenosine 3',5'-bisphosphate + [heparan sulfate]-N-sulfoglucosamine |
important residue are Glu642, Lys614, Lys883, with possible involvement of Thr617 and Thr618, in binding 3'-phosphoadenosine 5'-phosphosulfate |
645942 |
2.8.2.8 | 3'-phosphoadenylyl sulfate + [heparan sulfate]-glucosamine = adenosine 3',5'-bisphosphate + [heparan sulfate]-N-sulfoglucosamine |
residues 558-882 provide the sulfotransferase domain of the bifunctional enzyme, with Lys614 as a catalytically important conserved residue |
645937, 645942 |
2.8.2.8 | 3'-phosphoadenylyl sulfate + [heparan sulfate]-glucosamine = adenosine 3',5'-bisphosphate + [heparan sulfate]-N-sulfoglucosamine |
The enzyme also catalyses the sulfation of chondroitin 4-sulfate and dermatan sulfate, but to a much more limited extent |
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