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Crystal Structure and Biochemical Analysis of a Cytochrome P450 Steroid Hydroxylase (BaCYP106A6) from Bacillus Species.
Kim, Ki-Hwa; Do, Hackwon; Lee, Chang Woo; Subedi, Pradeep; Choi, Mieyoung; Nam, Yewon; Lee, Jun Hyuck; Oh, Tae-Jin.
Afiliação
  • Kim KH; Department of Life Science and Biochemical Engineering, Sunmoon University, Asan 31460, Republic of Korea.
  • Do H; Research Unit of Cryogenic Novel Materials, Korea Polar Research Institute, Incheon 21990, Republic of Korea.
  • Lee CW; Department of Polar Sciences, University of Science and Technology, Incheon 21990, Republic of Korea.
  • Subedi P; Research Unit of Cryogenic Novel Materials, Korea Polar Research Institute, Incheon 21990, Republic of Korea.
  • Choi M; Department of Life Science and Biochemical Engineering, Sunmoon University, Asan 31460, Republic of Korea.
  • Nam Y; Department of Pharmaceutical Engineering and Biotechnology, Sunmoon University, Asan 31460, Republic of Korea.
  • Lee JH; Research Unit of Cryogenic Novel Materials, Korea Polar Research Institute, Incheon 21990, Republic of Korea.
  • Oh TJ; Research Unit of Cryogenic Novel Materials, Korea Polar Research Institute, Incheon 21990, Republic of Korea.
J Microbiol Biotechnol ; 33(3): 387-397, 2023 Mar 28.
Article em En | MEDLINE | ID: mdl-36655276
ABSTRACT
Cytochrome P450 (CYP) is a heme-containing enzyme that catalyzes hydroxylation reactions with various substrate molecules. Steroid hydroxylases are particularly useful for effectively introducing hydroxyl groups into a wide range of steroids in the pharmaceutical industry. This study reports a newly identified CYP steroid hydroxylase (BaCYP106A6) from the bacterium Bacillus sp. and characterizes it using an in vitro enzyme assay and structural investigation. Bioconversion assays indicated that BaCYP106A1 catalyzes the hydroxylation of progesterone and androstenedione, whereas no or low conversion was observed with 11ß-hydroxysteroids such as cortisol, corticosterone, dexamethasone, and prednisolone. In addition, the crystal structure of BaCYP106A6 was determined at a resolution of 2.8 Å to investigate the configuration of the substrate-binding site and understand substrate preference. This structural characterization and comparison with other bacterial steroid hydroxylase CYPs allowed us to identify a unique Arg295 residue that may serve as the key residue for substrate specificity and regioselectivity in BaCYP106A6. This observation provides valuable background for further protein engineering to design commercially useful CYP steroid hydroxylases with different substrate specificities.
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Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Bacillus Idioma: En Revista: J Microbiol Biotechnol Ano de publicação: 2023 Tipo de documento: Article

Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Bacillus Idioma: En Revista: J Microbiol Biotechnol Ano de publicação: 2023 Tipo de documento: Article
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