Structural functionality, catalytic mechanism modeling and molecular allergenicity of phenylcoumaran benzylic ether reductase, an olive pollen (Ole e 12) allergen

• Published in: Journal of computer-aided molecular design Vol. 27; no. 10; pp. 873 - 895
• Main Authors: Jimenez-Lopez, Jose C., Kotchoni, Simeon O., Hernandez-Soriano, Maria C., Gachomo, Emma W., Alché, Juan D.
• Format: Journal Article
• Language: English
• Published: Dordrecht Springer Netherlands 01.10.2013; Springer Nature B.V
• Subjects: Allergens; Allergens - chemistry; Allergens - immunology; Allergies; Amino Acid Sequence; Animal Anatomy; Catalysis; Catalytic Domain; Chemistry; Chemistry and Materials Science; Cloning, Molecular; Comparative studies; Computer Applications in Chemistry; Enzymes; Epitopes - chemistry; Epitopes - genetics; Epitopes - immunology; Flavonoids; Food allergies; Histology; Humans; Immunotherapy; Metabolites; Models, Molecular; Molecular biology; Morphology; Olea - enzymology; Olea - immunology; Oxidoreductases - chemistry; Oxidoreductases - immunology; Oxidoreductases - metabolism; Phylogeny; Physical Chemistry; Physicochemical properties; Pollen; Pollen - enzymology; Pollen - immunology; Proteins; Sequence Homology, Amino Acid; Structure-Activity Relationship; Isoflavone reductase; Olive; Flavonoids; Homology modeling; Polyphenols; NAD(P)H; Pollen; Sequence polymorphism; Electrostatic potential; Molecular docking; Allergen; B- and T-cell epitopes

Isoflavone reductase-like proteins (IRLs) are enzymes with key roles in the metabolism of diverse flavonoids. Last identified olive pollen allergen (Ole e 12) is an IRL relevant for allergy amelioration, since it exhibits high prevalence among atopic patients. The goals of this study are the charact...