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Carving the Active Site of CYP153A7 Monooxygenase for Improving Terminal Hydroxylation of Medium-Chain Fatty Acids.
Dong, Ya-Li; Chong, Gang-Gang; Li, Chun-Xiu; Chen, Qi; Pan, Jiang; Li, Ai-Tao; Xu, Jian-He.
Afiliación
  • Dong YL; State Key Laboratory of Bioreactor Engineering and, Shanghai Collaborative Innovation Centre for Biomanufacturing and, Frontiers Science Center for Materiobiology and Dynamic Chemistry, East China University of Science and Technology, Shanghai, 200237, China.
  • Chong GG; State Key Laboratory of Bioreactor Engineering and, Shanghai Collaborative Innovation Centre for Biomanufacturing and, Frontiers Science Center for Materiobiology and Dynamic Chemistry, East China University of Science and Technology, Shanghai, 200237, China.
  • Li CX; State Key Laboratory of Bioreactor Engineering and, Shanghai Collaborative Innovation Centre for Biomanufacturing and, Frontiers Science Center for Materiobiology and Dynamic Chemistry, East China University of Science and Technology, Shanghai, 200237, China.
  • Chen Q; State Key Laboratory of Bioreactor Engineering and, Shanghai Collaborative Innovation Centre for Biomanufacturing and, Frontiers Science Center for Materiobiology and Dynamic Chemistry, East China University of Science and Technology, Shanghai, 200237, China.
  • Pan J; State Key Laboratory of Bioreactor Engineering and, Shanghai Collaborative Innovation Centre for Biomanufacturing and, Frontiers Science Center for Materiobiology and Dynamic Chemistry, East China University of Science and Technology, Shanghai, 200237, China.
  • Li AT; Hubei Collaborative Innovation Center for Green Transformation of Bio-resources Hubei Key Laboratory of Industrial Biotechnology, College of Life Science, Hubei University, Wuhan, 430062, China.
  • Xu JH; State Key Laboratory of Bioreactor Engineering and, Shanghai Collaborative Innovation Centre for Biomanufacturing and, Frontiers Science Center for Materiobiology and Dynamic Chemistry, East China University of Science and Technology, Shanghai, 200237, China.
Chembiochem ; 23(9): e202200063, 2022 05 04.
Article en En | MEDLINE | ID: mdl-35257464
ABSTRACT
The P450-mediated terminal hydroxylation of non-activated C-H bonds is a chemically challenging reaction. CYP153A7 monooxygenase, discovered in Sphingomonas sp. HXN200, belongs to the CYP153A subfamily and shows a pronounced terminal selectivity. Herein, we report the significantly improved terminal hydroxylation activity of CYP153A7 by redesign of the substrate binding pocket based on molecular docking of CYP153A7-C80 and sequence alignments. Some of the resultant single mutants were advantageous over the wild-type enzyme with higher reaction rates, achieving a complete conversion of n-octanoic acid (C80, 1 mM) in a shorter time period. Especially, a single-mutation variant, D258E, showed 3.8-fold higher catalytic efficiency than the wild type toward the terminal hydroxylation of medium-chain fatty acid C80 to the high value-added product 8-hydroxyoctanoic acid.
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Sistema Enzimático del Citocromo P-450 / Ácidos Grasos Idioma: En Revista: Chembiochem Asunto de la revista: BIOQUIMICA Año: 2022 Tipo del documento: Article País de afiliación: China
Texto completo
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Sistema Enzimático del Citocromo P-450 / Ácidos Grasos Idioma: En Revista: Chembiochem Asunto de la revista: BIOQUIMICA Año: 2022 Tipo del documento: Article País de afiliación: China