Literature summary 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.

Protein Variants

EC Number	Protein Variants	Comment	Organism
1.20.4.1	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
1.20.4.1	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
1.20.4.1	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

EC Number	Organism	UniProt	Comment	Textmining
1.20.4.1	Staphylococcus aureus	P0A006	-	-

Reaction

EC Number	Reaction	Comment	Organism	Reaction ID
1.20.4.1	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	a

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Release 2023.1 (January 2023)