1.20.4.1	arsenate + glutathione + glutaredoxin = arsenite + a glutaredoxin-glutathione disulfide + H2O	-	-	
1.20.4.1	arsenate + glutathione + glutaredoxin = arsenite + a glutaredoxin-glutathione disulfide + H2O	arsenate reduction by glyceraldehyde-3-phosphate dehydrogenase may take place during or as a consequence of, the arsenolytic cleavage of the thioester bond formed between the enzyme’s C149 and the 3-phosphoglycerol moiety of the substrate	677207	
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	673087	
1.20.4.1	arsenate + glutathione + glutaredoxin = arsenite + a glutaredoxin-glutathione disulfide + H2O	reaction mechanism	660258