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

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.

Original languageEnglish
Pages (from-to)10608-10616
Number of pages9
JournalJournal of Agricultural and Food Chemistry
Volume66
Issue number40
DOIs
StatePublished - 10 Oct 2018

Bibliographical note

Funding Information:
This work was supported by a grant from Marine Biotechnology Program (20170305 Development of biomedical materials based on marine proteins) funded by Ministry of Oceans and Fisheries, Korea and by National Research Foundation of Korea (NRF) grants funded by the Korean government (MSIT; NRF-2015M1A5A1037480 and NRF-2018R1A5A2025286).

Funding Information:
∇S.-B.P., D.-W.B, and N.A.B.C. contributed equally to this work. Funding This work was supported by a grant from Marine Biotechnology Program (20170305, Development of biomedical materials based on marine proteins) funded by Ministry of Oceans and Fisheries, Korea and by National Research Foundation of Korea (NRF) grants funded by the Korean government (MSIT; NRF-2015M1A5A1037480 and NRF-2018R1A5A2025286). Notes The authors declare no competing financial interest.

Publisher Copyright:
© 2018 American Chemical Society.

Keywords

  • 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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