Current Projects: L-amino acid oxidase
We have recently determined the structure of the flavoenzyme, L-amino acid oxidase.  The structure reveals an active site buried deep inside the protein core accessible from the outside by a narrow funnel.  The structure in the presence of the inhibitor, o-amino benzoate shows the ligand bound at the active site as well as a further two positions in the funnel entrance.  Comparisons of the structures of L-amino acid oxidase and D-amino acid oxidase show that although the two enzymes are significantly different in structure and their active sites have evolved to specifically bind and recognize the correct enantiomeric substrate, the atoms involved in the catalytic mechanism are spatially conserved on a mirror plane.
L-amino acid oxidase  |  Cholesterol oxidase  |  Formiminotransferase-cyclodeaminase (FTCD) DmpFG  |  LuxCDE
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