Fructosyl-Amino Acid Oxidase from Corynebacterium sp. (C15-1425-125)

General description

Fructosyl amino acid oxidase [fructosyl-a-l-amino acid:oxygen oxidoreductase] is a flavoprotein that catalyzes the oxidation of fructosyl amino acids to form glucosone, amino acid and hydrogen peroxide.

Enzyme Commission (E.C.) 1.5.3.x

Application

Fructosyl-Amino Acid Oxidase from Corynebacterium sp has been used in glycated haemoglobin HbA1c detection in blood samples using quartz crystal microbalance (QCM) based detection.

Fructosyl-amino acid oxidase can be used to detect the levels of glycated proteins, which are markers for diabetes mellitus.

Biochem/physiol Actions

Fructosamines are formed when glucose is condensed amino group of amino acids or proteins. Fructosamine oxidases (FAOX) catalyze the oxidative deglycation of low molecular weight fructosamines. Fructosyl amino acid oxidase catalyzes the oxidation of the C-N bond linking the C1 of the fructosyl moiety and the nitrogen of the amino group of fructosyl amino acids.

Fructosyl-Amino Acid Oxidase (FAOD) comprises of FAD-binding motifs and is classified into three types based on substrate specificity. The engineered Corynebacterium Fructosyl-Amino Acid Oxidase is stable at 45°C and could be exploited for the development of glycated protein biosensing system and glycated hemoglobin HbA1c measurements. FAOD shares sequence homology with fructosyl peptide oxidase and both are effective on α-fructosyl substrates.

Suitable for the determination of fructosyl-L-amino acid.

Unit Definition

One unit will produce 1.0 μmole of hydrogen peroxide per minute at pH 8.0 at 37 °C.