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

doi:10.1021/acs.jafc.8b03647

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

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13 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 language	English
Pages (from-to)	10608-10616
Number of pages	9
Journal	Journal of Agricultural and Food Chemistry
Volume	66
Issue number	40
DOIs	https://doi.org/10.1021/acs.jafc.8b03647
State	Published - 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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10.1021/acs.jafc.8b03647

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Park, S. B., Bae, D. W., Clavio, N. A. B., Zhao, L., Jeong, C. S., Choi, B. M., Macalino, S. J. Y., Cha, H. J., Park, J. B., Lee, J. H., Nam, S. J., Choi, S., Kim, M. K., & Cha, S. S. (2018). Structural and Biochemical Characterization of the Curcumin-Reducing Activity of CurA from Vibrio vulnificus. Journal of Agricultural and Food Chemistry, 66(40), 10608-10616. https://doi.org/10.1021/acs.jafc.8b03647

@article{f01dff12fb83487ba52ae750cf79e321,

title = "Structural and Biochemical Characterization of the Curcumin-Reducing Activity of CurA from Vibrio vulnificus",

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.",

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",

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

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: {\textcopyright} 2018 American Chemical Society.",

year = "2018",

month = oct,

day = "10",

doi = "10.1021/acs.jafc.8b03647",

language = "English",

volume = "66",

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Park, SB, Bae, DW, Clavio, NAB, Zhao, L, Jeong, CS, Choi, BM, Macalino, SJY, Cha, HJ, Park, JB, Lee, JH, Nam, SJ , Choi, S, Kim, MK & Cha, SS 2018, 'Structural and Biochemical Characterization of the Curcumin-Reducing Activity of CurA from Vibrio vulnificus', Journal of Agricultural and Food Chemistry, vol. 66, no. 40, pp. 10608-10616. https://doi.org/10.1021/acs.jafc.8b03647

TY - JOUR

T1 - Structural and Biochemical Characterization of the Curcumin-Reducing Activity of CurA from Vibrio vulnificus

AU - Park, Soo Bong

AU - Bae, Da Woon

AU - Clavio, Nina Abigail B.

AU - Zhao, Lei

AU - Jeong, Chang Sook

AU - Choi, Bo Mee

AU - Macalino, Stephani Joy Y.

AU - Cha, Hee Jeong

AU - Park, Jin Byung

AU - Lee, Jun Hyuck

AU - Nam, Sang Jip

AU - Choi, Sun

AU - Kim, Min Kyu

AU - Cha, Sun Shin

N1 - 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.

PY - 2018/10/10

Y1 - 2018/10/10

N2 - 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.

AB - 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.

KW - crystal structure of apo VvCurA

KW - crystal structure of the VvCurA/NADPH complex

KW - curcumin-reducing enzyme

KW - enzyme mechanism

KW - in silico model of the VvCurA/NADPH/curcumin complex

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U2 - 10.1021/acs.jafc.8b03647

DO - 10.1021/acs.jafc.8b03647

M3 - Article

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AN - SCOPUS:85054373209

SN - 0021-8561

VL - 66

SP - 10608

EP - 10616

JO - Journal of Agricultural and Food Chemistry

JF - Journal of Agricultural and Food Chemistry

IS - 40

ER -

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

Abstract

Bibliographical note

Keywords

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