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Structural and Biochemical Characterization of the Curcumin-Reducing Activity of CurA from Vibrio vulnificus
- Structural and Biochemical Characterization of the Curcumin-Reducing Activity of CurA from Vibrio vulnificus
- Park, Soo-Bong; Bae, Da-Woon; Clavio, Nina Abigail B.; Zhao, Lei; Jeong, Chang-Sook; Choi, Bo Mee; Macalino, Stephani Joy Y.; Cha, Hee-Jeong; Park, Jin-Byung; Lee, Jun Hyuck; Nam, Sang-Jip; Choi, Sun; Kim, Min-Kyu; Cha, Sun-Shin
- Ewha Authors
- 최선; 박진병; 남상집; 차선신
- SCOPUS Author ID
- 최선; 박진병; 남상집; 차선신
- Issue Date
- Journal Title
- JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY
- JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY vol. 66, no. 40, pp. 10608 - 10616
- curcumin-reducing enzyme; crystal structure of apo VvCurA; crystal structure of the VvCurA/NADPH complex; in silico model of the VvCurA/NADPH/curcumin complex; enzyme mechanism
- AMER CHEMICAL SOC
- SCI; SCIE; SCOPUS
- Document Type
- 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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