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 |
|