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Such changes could reduce the transamination activity, as suggested by an interference with the formation of diaminovalerate, a proposed metabolic intermediate in this catalytic reaction of GSAAT ( In light of experimental evidence showing the different monomeric and dimeric states of the Cys substitution mutants compared to GSAAT(WT), we propose that Cys168 and Cys190 are cruical for the protein activity and likely function as redox-active residues

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