Interaction of arylsulfatase-A (ASA) with its natural sulfoglycolipid substrates: a computational and site-directed mutagenesis study

@article{Schenk2008InteractionOA,
  title={Interaction of arylsulfatase-A (ASA) with its natural sulfoglycolipid substrates: a computational and site-directed mutagenesis study},
  author={Matthias Schenk and Chaitanya A. K. Koppisetty and Daniela Costa de Oliveira Santos and Eur{\'i}dice Carmona and Shailender Bhatia and Per-Georg Nyholm and Nongnuj Tanphaichitr},
  journal={Glycoconjugate Journal},
  year={2008},
  volume={26},
  pages={1029-1045}
}
Arylsulfatase A (ASA) hydrolyzes sulfate esters with a pH optimum of 5. Interactions between p-nitrocatechol sulfate (NCS, artificial substrate) and active site residues of ASA are revealed from their co-crystal structure. Since equivalent ASA interactions with its natural substrates, sulfogalactosylceramide (SGC) and sulfogalactosylglycerolipid (SGG), are not known, we computationally docked SGC/SGG to the ASA crystal structure. Our dockings suggested that Cys69 was the active site residue… CONTINUE READING

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