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3 Results 3.1 Structural analysis and protein sequence alignments reveal four highly conserved cysteine residues in Arabidopsis GSAAT A X-ray crystallographic structure of Arabidopsis GSAAT1 (GSAAT At ) has been reported at 1.25 A resolution ( Synechocystis GSAAT (GSAAT Syn ), GSAAT At forms an asymmetric dimer, which reflects the differential binding of its substrates pyridoxal 5-phosphate (PLP) and pyridoxamine 5-phosphate (PMP) as cofactors to the two subunits, respectively ( At precursor) is located close to the bound cofactor PLP, with which it forms a Schiff-base linkage ( GSAAT At has four conserved Cys residues, Cys138, Cys168, Cys190 (all present in the catalytic domain) and Cys396 (at the C-terminus)