Fig. 1.

ClustalW alignment of amino acid sequences of X. humilis HC205 (AY570978) and the A. thaliana orthologue (At1g07645), with known glyoxalase I genes, including L07837 (Homo sapiens), Y13239 (Brassica juncea), At1g08110 (A. thaliana), and Z48183 (Lycopersicon esculentum). The asterisks represent amino acids that are identical in all of the six sequences. The βαβββ structural repeat determined in the X-ray crystal structure of the human glyoxalase I protein is indicated. This structural repeat is represented by β₁α₂β₂β₃β₄ in the first domain (α₁−β₄), and by β₅α₄β₆β₇β₈ in the second domain (β₅−α₆) (Cameron et al., 1997). Conserved amino acids that constitute the glutathione binding sites of glyoxalase I are highlighted in grey. Conserved amino acids which form the zinc binding sites are in bold and are boxed.