The glycosylation site of glycosylated hemoglobin in human blood is the valine NH2 residue. Therefore, the preparation of a simulated substrate for glycosylated hemoglobin in human blood, namely fructose valine [N - (1-deoxy-D-fructose-1-yl) - valine], is particularly important for screening highly active, stable, and specific fructose valine oxidase and studying its enzymatic properties. The glycosylated hemoglobin in the blood reflects the blood sugar level in the organism for a period of time, and has been used as an important indicator for the diagnosis and treatment of diabetes in recent years. At present, enzymatic methods are mainly used in the market to detect the content of glycosylated hemoglobin in the human body. Using this method to determine glycosylated hemoglobin requires a special type of enzyme - fructose valine oxidase. This enzyme acts on glycosylated peptides or glycosylated amino acids, and its product undergoes a series of oxidation-reduction reactions. Finally, the content of glycosylated hemoglobin is determined by the color development of the final product. Therefore, fructose valine oxidase is a key enzyme in the determination of glycated hemoglobin.

CAS NO:9000-88-8

EC NO:232-563-5

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Synonyms:;D-Amino acid oxidase;Oxidase, D-amino acid;

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