Heparan sulphate N-sulphotransferase activity: reaction mechanism and substrate recognition.

@article{Kakuta2003HeparanSN,
  title={Heparan sulphate N-sulphotransferase activity: reaction mechanism and substrate recognition.},
  author={Yoshimitsu Kakuta and Lingjun Li and Lars C Pedersen and Lee G. Pedersen and Masahiko Negishi},
  journal={Biochemical Society transactions},
  year={2003},
  volume={31 2},
  pages={331-4}
}
Human heparan sulphate N-deacetylase/N-sulphotransferase 1 sulphates the NH(3) (+) group of the glucosamine moiety of the heparan chain in heparan sulphate/heparin biosynthesis. An open cleft that runs perpendicular to the sulphate donor 3'-phosphoadenosine 5'-phosphosulphate may constitute the acceptor substrate-binding site of the sulphotransferase domain (hNST1) [Kakuta, Sueyoshi, Negishi and Pedersen (1999) J. Biol. Chem. 274, 10673-10676]. When a hexasaccharide model chain is docked into… CONTINUE READING