Theoretical Study on the Disparate Spatial Arrangement of 3’,4’,5,7-tetrahydroxy-3-flavene Towards Jack Bean Urease Enzyme Active Site

• Published in: Malaysian Journal of Fundamental and Applied Sciences
• Main Author: Yaakob M.H.; Ghani Z.A.; Fauzi S.S.M.; Shuhaime N.; Zuber S.Z.H.S.; Ang L.S.
• Format: Article
• Language: English
• Published: Penerbit UTM Press 2024
• Online Access: https://www.scopus.com/inward/record.uri?eid=2-s2.0-85204881661&doi=10.11113%2fmjfas.v20n4.3403&partnerID=40&md5=cc06f639eccfa5c38fdb0e7451e543a1

Urease enzyme plays crucial role in the hydrolysis of urea. Excessive hydrolysis of urea can have significant impacts on the environment. In recent years, there has been growing interest in identifying natural compounds that can inhibit urease activity. Flavonoids, phytochemical compounds present in plants, have shown promising potential as urease inhibitors. Studies have revealed that certain flavonoids, such as 3’,4’,5,7-tetrahydroxy-3-flavene, abbreviated as H4FLA for convenient, exhibit potent inhibition of urease, surpassing the efficacy of well-known synthetic inhibitors. In the present study, we report quantum mechanical calculations that mainly investigate the interaction of H4FLA towards urease at disparate spatial arrangement. It was found that the most favourable position between H4FLA and active site of urease has interaction energy of −3.80 eV. Topology analysis revealed that there is no typical covalent bond found between atoms involved in the interaction. Only weak interactions were detected. The hydroxyl groups with highest (negative) local potential throughout the structure, contribute mainly to the formation of non-covalent interaction with the nickel centers, indicating their potential involvement in the inhibitory activity of flavonoids against urease. ©Copyright Yaakob.