Abstract
Fructosyl valyl-histidine, which is released from protease digestion of the major diabetes indicator HbA1c, is recognized as a target molecule for HbA1c sensors. The flavoenzyme fructosyl amino acid oxidase (FAOD) is an enzyme catalyzing the oxidative deglycation of fructosyl amino acids, with those also possessing high activity towards fructosyl dipeptides being referred to as fructosyl peptidyl oxidases (FPOXs). The high oxygen reactivity of FAODs and FPOXs limits their potential utility in amperometric enzyme sensors employing artificial electron mediators. We successfully modified the proton relay system of Pichia N1-1 FAOD, significantly decreasing its catalytic ability to employ oxygen as the electron acceptor, while having little effect on the dye-mediated dehydrogenase activity employing artificial electron acceptors instead of oxygen. We expect that similar engineering of a recently discovered FPOX will produce an enzyme that is ideally suited for HbA1c sensing.
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