Structural and Biochemical Characterization of the Curcumin-Reducing Activity of CurA from Vibrio vulnificus

Soo Bong Park, Da Woon Bae, Nina Abigail B. Clavio, Lei Zhao, Chang Sook Jeong, Bo Mee Choi, Stephani Joy Y. Macalino, Hee Jeong Cha, Jin Byung Park, Jun Hyuck Lee, Sang Jip Nam, Sun Choi, Min Kyu Kim, Sun Shin Cha

Research output: Contribution to journalArticlepeer-review

9 Scopus citations


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.

Original languageEnglish
Pages (from-to)10608-10616
Number of pages9
JournalJournal of Agricultural and Food Chemistry
Issue number40
StatePublished - 10 Oct 2018


  • crystal structure of apo VvCurA
  • crystal structure of the VvCurA/NADPH complex
  • curcumin-reducing enzyme
  • enzyme mechanism
  • in silico model of the VvCurA/NADPH/curcumin complex


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