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However, this finding is consistent with the outcomes of thiol-dependent affinity chromatography of TRX-f1 and TRX-m1, in which GSAAT was pulled down from extracts of Spinacia oleracea ( 3.5 In-vitro modifications of the structure and activity of GSAAT cysteine substitution mutants under redox conditions To examine the relevance of the conserved Cys residues of GSAAT At for its structure and activity, the WT and the four single Cys (C) to Ser (S) substitution mutant proteins - designated as GSAAT(WT), GSAAT(C138S), GSAAT(C168S), GSAAT(C190S) and GSAAT(C396S), respectively - and the double mutant GSAAT(C168S/C190S), were heterologously expressed as His-tagged proteins and subsequently purified