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Curcumin degradation in a soil microorganism: Screening and characterization of a ß-diketone hydrolase.
Hashimoto, Yoshiteru; Ishigami, Kana; Hassaninasab, Azam; Kishi, Katsuhiro; Kumano, Takuto; Kobayashi, Michihiko.
Afiliación
  • Hashimoto Y; Institute of Applied Biochemistry and Graduate School of Life and Environmental Sciences, The University of Tsukuba, , Tsukuba, Ibaraki, Japan; Microbiology Research Center for Sustainability (MiCS), The University of Tsukuba, Tsukuba, Ibaraki, Japan. Electronic address: hashimoto.y.gu@u.tsukuba.ac.
  • Ishigami K; Institute of Applied Biochemistry and Graduate School of Life and Environmental Sciences, The University of Tsukuba, , Tsukuba, Ibaraki, Japan.
  • Hassaninasab A; Institute of Applied Biochemistry and Graduate School of Life and Environmental Sciences, The University of Tsukuba, , Tsukuba, Ibaraki, Japan.
  • Kishi K; Institute of Applied Biochemistry and Graduate School of Life and Environmental Sciences, The University of Tsukuba, , Tsukuba, Ibaraki, Japan.
  • Kumano T; Institute of Applied Biochemistry and Graduate School of Life and Environmental Sciences, The University of Tsukuba, , Tsukuba, Ibaraki, Japan; Microbiology Research Center for Sustainability (MiCS), The University of Tsukuba, Tsukuba, Ibaraki, Japan.
  • Kobayashi M; Institute of Applied Biochemistry and Graduate School of Life and Environmental Sciences, The University of Tsukuba, , Tsukuba, Ibaraki, Japan; Microbiology Research Center for Sustainability (MiCS), The University of Tsukuba, Tsukuba, Ibaraki, Japan; Center for Quantum and Information LifeSciences,
J Biol Chem ; 300(9): 107647, 2024 Aug 08.
Article en En | MEDLINE | ID: mdl-39122010
ABSTRACT
Curcumin is a plant-derived secondary metabolite exhibiting antitumor, neuroprotective, antidiabetic activities, and so on. We previously isolated Escherichia coli as an enterobacterium exhibiting curcumin-converting activity from human feces, and discovered an enzyme showing this activity (CurA) and named it NADPH-dependent curcumin/dihydrocurcumin reductase. From soil, here, we isolated a curcumin-degrading microorganism (No. 34) using the screening medium containing curcumin as the sole carbon source and identified as Rhodococcus sp. A curcumin-degrading enzyme designated as CurH was purified from this strain and characterized, and compared with CurA. CurH catalyzed hydrolytic cleavage of a carbon-carbon bond in the ß-diketone moiety of curcumin and its analogs, yielding two products bearing a methyl ketone terminus and a carboxylic acid terminus, respectively. These findings demonstrated that a curcumin degradation reaction catalyzed by CurH in the soil environment was completely different from the one catalyzed by CurA in the human microbiome. Of all the curcumin analogs tested, suitable substrates for the enzyme were curcuminoids (i.e., curcumin and bisdemethoxycurcumin) and tetrahydrocurcuminoids. Thus, we named this enzyme curcuminoid hydrolase. The deduced amino acid sequence of curH exhibited similarity to those of members of acetyl-CoA C-acetyltransferase family. Considering results of oxygen isotope analyses and a series of site-directed mutagenesis experiments on our enzyme, we propose a possible catalytic mechanism of CurH, which is unique and distinct from those of enzymes degrading ß-diketone moieties such as ß-diketone hydrolases known so far.
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Idioma: En Revista: J Biol Chem Año: 2024 Tipo del documento: Article Pais de publicación: Estados Unidos
Texto completo
Añadir a Mi BVS
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Idioma: En Revista: J Biol Chem Año: 2024 Tipo del documento: Article Pais de publicación: Estados Unidos