Structural and biochemical characterization of the curcumin-reducing activity of CurA from Vibrio vulnificus

College

College of Science

Department/Unit

Chemistry

Document Type

Article

Source Title

Journal of Agricultural and Food Chemistry

Volume

66

First Page

10608

Last Page

10616

Publication Date

2018

Abstract

Curcumin is a yellow-colored ingredient in dietary spice turmeric (Curcuma longa Linn). This nontoxic polyphenol has antitumor, anti-inflammatory, apoptotic, and antioxidant activities. The ingested curcumin is reduced to multihydrated forms with more potent therapeutic potentials by the curcumin reductase (CurA) from commensal Escherichia coli. In this study, we demonstrated that Vibrio vulnificus CurA (VvCurA) with 87% sequence similarity to the E. coli CurA exhibits the curcumin-reducing activity through spectrophotometric detection of NADPH oxidation and high performance liquid chromatographic analysis of curcumin consumption and product generation. Afterward, we determined the crystal structures of VvCurA and the VvCurA/NADPH complex, and made the in silico model of the VvCurA/NADPH/curcumin ternary complex through induced fit docking. Based on structural information, active site residues that play critical roles in catalysis have been identified and characterized by mutational and kinetic studies, leading us to propose the reaction mechanism of CurA.

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Digitial Object Identifier (DOI)

10.1021/acs.jafc.8b03647

Disciplines

Chemistry

Keywords

Curcumin; Vibrio vulnificus

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