Occurrence, characteristics, and applications of fructosyl amine oxidases (amadoriases).
Amadori compounds, formed by the Maillard reaction between reducing sugars (e.g., glucose) and amines (e.g., lysine residues in proteins), are ubiquitous in nature and have been implicated in aging and several chronic diseases. Fructosyl amine oxidases (FAOXs) are a relatively new class of enzymes that cleave amadori compounds and have been found in fungi, yeast, and bacteria. This mini-review summarizes over a dozen of FAOXs with different substrate specificities have been isolated, characterized, and engineered to date. All known FAOX sequences except one have the consensus motif for the ADP-binding betaalphabeta-fold common to all FAD and NAD enzymes, and a recently solved crystal structure provides important clues for this class of enzymes. FAOXs have been explored for applications in diabetes diagnosis, detergents, and food processing. Given that naturally occurring FAOXs can only react directly with small glycated amino acids or short peptides, it is of great interest to engineer and expand the accessibility of the substrate binding sites of these enzymes.
Lin
Zhanglin
Z
Department of Chemical Engineering, Tsinghua University, One Tsinghua Garden Road, Beijing, 100084, China. zhanglinlin@mail.tsinghua.edu.cn
Zheng
Jing
J
D000594:Amino Acid Oxidoreductases / Q000737:chemistry / Q000302:isolation & purification / Q000378:metabolism*; D000596:Amino Acids / Q000378:metabolism; D001419:Bacteria / Q000201:enzymology; D001665:Binding Sites; D005658:Fungi / Q000201:enzymology; D006031:Glycosylation; D015416:Maillard Reaction; D015202:Protein Engineering; D017434:Protein Structure, Tertiary; D011506:Proteins / Q000378:metabolism; D013379:Substrate Specificity
D000596:Amino Acids; D011506:Proteins; D000594:Amino Acid Oxidoreductases; C103012:amadoriase