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Literature summary for 1.20.4.1 extracted from

  • Roos, G.; Loverix, S.; Brosens, E.; Van Belle, K.; Wyns, L.; Geerlings, P.; Messens, J.
    The activation of electrophile, nucleophile and leaving group during the reaction catalysed by pI258 arsenate reductase (2006), Chembiochem, 7, 981-989.
    View publication on PubMed

Protein Variants

Protein Variants Comment Organism
N13A decrease in activity due to lower local softness, analysis of S-As bond length, Wiberg bond orders, lewaving group energy and nucleofugality Staphylococcus aureus
R16A decrease in activity due to lower local softness, analysis of S-As bond length, Wiberg bond orders, lewaving group energy and nucleofugality Staphylococcus aureus
S17A decrease in activity due to lower local softness, analysis of S-As bond length, Wiberg bond orders, lewaving group energy and nucleofugality Staphylococcus aureus

Organism

Organism UniProt Comment Textmining
Staphylococcus aureus P0A006
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Reaction

Reaction Comment Organism Reaction ID
arsenate + glutathione + glutaredoxin = arsenite + a glutaredoxin-glutathione disulfide + H2O first reaction step is a nucleophilic displacement reaction by C10 on dianionic arsenate. Second step is a preferential nucleophilic attack of C82 on the monoanionic C10-arsenate intermediate stabilized by S17. Thiolate form of C82 is stabilized by an eight-residue alpha helix flanked by C82 and C89 and a hydrogen bond with T11. during the final step, C89 is activated as a nucleophile by structural alterations of the redox helix Staphylococcus aureus