8HG9

Cytochrome P450 steroid hydroxylase (BaCYP106A6) from Bacillus species

8HG9 の概要

• エントリーDOI: 10.2210/pdb8hg9/pdb
• 分子名称: cytochrome P450 steroid hydroxylase, PROTOPORPHYRIN IX CONTAINING FE (3 entities in total)
• 機能のキーワード: cytochrome p450, steroid hydroxylase, hormone
• 由来する生物種: Bacillus sp. (in: Bacteria)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 95609.79

構造登録者

Do, H.,Lee, J.H. (登録日: 2022-11-14, 公開日: 2023-07-26, 最終更新日: 2024-05-29)

主引用文献

Kim, K.H.,Do, H.,Lee, C.W.,Subedi, P.,Choi, M.,Nam, Y.,Lee, J.H.,Oh, T.J.
Crystal Structure and Biochemical Analysis of a Cytochrome P450 Steroid Hydroxylase ( Ba CYP106A6) from Bacillus Species.
J Microbiol Biotechnol., 33:387-397, 2023

PubMed 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 (CYP106A6) from the bacterium sp. and characterizes it using an in vitro enzyme assay and structural investigation. Bioconversion assays indicated that CYP106A1 catalyzes the hydroxylation of progesterone and androstenedione, whereas no or low conversion was observed with 11β-hydroxysteroids such as cortisol, corticosterone, dexamethasone, and prednisolone. In addition, the crystal structure of CYP106A6 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 CYP106A6. This observation provides valuable background for further protein engineering to design commercially useful CYP steroid hydroxylases with different substrate specificities.

PubMed: 36655276
DOI: 10.4014/jmb.2211.11031

実験手法

X-RAY DIFFRACTION (2.79 Å)