7DLS

Cytochrome P450 (CYP105D18) complex with papaverine

7DLS の概要

• エントリーDOI: 10.2210/pdb7dls/pdb
• 関連するPDBエントリー: 7DI3
• 分子名称: Cytochrome P450 hydroxylase, PROTOPORPHYRIN IX CONTAINING FE, 1-(3,4-DIMETHOXYBENZYL)-6,7-DIMETHOXYISOQUINOLINE, ... (4 entities in total)
• 機能のキーワード: papaverine n-oxide, eukaryotic cytochrome p450, chemical modification, heme oxidation, transferase
• 由来する生物種: Streptomyces laurentii
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 45359.14

構造登録者

Do, H.,Lee, J.H. (登録日: 2020-11-30, 公開日: 2021-07-14, 最終更新日: 2023-11-29)

主引用文献

Pardhe, B.D.,Do, H.,Jeong, C.S.,Kim, K.H.,Lee, J.H.,Oh, T.J.
Characterization of high-H 2 O 2 -tolerant bacterial cytochrome P450 CYP105D18: insights into papaverine N-oxidation.
Iucrj, 8:684-694, 2021

PubMed Abstract: The bacterial CYP105 family is involved in secondary metabolite biosynthetic pathways and plays essential roles in the biotransformation of xenobiotics. This study investigates the newly identified HO-mediated CYP105D18 from as the first bacterial CYP for N-oxidation. The catalytic efficiency of CYP105D18 for papaverine N-oxidation was 1.43 s µ . The heme oxidation rate () was low (<0.3 min) in the presence of 200 m HO. This high HO tolerance capacity of CYP105D18 led to higher turnover prior to heme oxidation. Additionally, the high-resolution papaverine complexed structure and substrate-free structure of CYP105D18 were determined. Structural analysis and activity assay results revealed that CYP105D18 had a strong substrate preference for papaverine because of its bendable structure. These findings establish a basis for biotechnological applications of CYP105D18 in the pharmaceutical and medicinal industries.

PubMed: 34258016
DOI: 10.1107/S2052252521005522

実験手法

X-RAY DIFFRACTION (2.06 Å)