Structural and Biochemical Characterization of the Curcumin-Reducing Activity of CurA from Vibrio vulnificus
- 주제(키워드) 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
- 주제(기타) Agriculture, Multidisciplinary; Chemistry, Applied; Food Science & Technology
- 설명문(일반) [Park, Soo-Bong; Bae, Da-Woon; Choi, Bo Mee; Nam, Sang-Jip; Cha, Sun-Shin] Ewha Womans Univ, Dept Chem & Nanosci, Seoul 03760, South Korea; [Clavio, Nina Abigail B.; Macalino, Stephani Joy Y.; Choi, Sun] Ewha Womans Univ, Coll Pharm, Seoul 03760, South Korea; [Clavio, Nina Abigail B.; Macalino, Stephani Joy Y.; Choi, Sun] Ewha Womans Univ, Grad Sch Pharmaceut Sci, Seoul 03760, South Korea; [Zhao, Lei; Kim, Min-Kyu] KAERI, Biotechnol Res Div, Jeongeup 56212, South Korea; [Jeong, Chang-Sook; Lee, Jun Hyuck; Kim, Min-Kyu] Univ Sci & Technol, Daejeon, South Korea; [Jeong, Chang-Sook; Lee, Jun Hyuck] Korea Polar Res Inst, Unit Polar Genom, Incheon 21990, South Korea; [Cha, Hee-Jeong; Park, Jin-Byung] Ewha Womans Univ, Dept Food Sci & Engn, Seoul 03760, South Korea
- 등재 SCIE, SCOPUS
- 발행기관 AMER CHEMICAL SOC
- 발행년도 2018
- URI http://www.dcollection.net/handler/ewha/000000156656
- 본문언어 영어
- Published As http://dx.doi.org/10.1021/acs.jafc.8b03647
초록/요약
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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