8GTL

Crystal Structure of Cytochrome P450 (CYP101D5)

8GTL の概要

• エントリーDOI: 10.2210/pdb8gtl/pdb
• 分子名称: cytochrome P450 CYP101D5, PROTOPORPHYRIN IX CONTAINING FE (3 entities in total)
• 機能のキーワード: ionone, cytochrome p450, chemical modification, heme oxidation, transferase
• 由来する生物種: Sphingomonas echinoides
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 92937.56

構造登録者

Do, H.,Lee, J.H. (登録日: 2022-09-08, 公開日: 2022-12-28, 最終更新日: 2023-11-29)

主引用文献

Subedi, P.,Do, H.,Lee, J.H.,Oh, T.J.
Crystal Structure and Biochemical Analysis of a Cytochrome P450 CYP101D5 from Sphingomonas echinoides.
Int J Mol Sci, 23:-, 2022

PubMed Abstract: Cytochrome P450 enzymes (CYPs) are heme-containing enzymes that catalyze hydroxylation with a variety of biological molecules. Despite their diverse activity and substrates, the structures of CYPs are limited to a tertiary structure that is similar across all the enzymes. It has been presumed that CYPs overcome substrate selectivity with highly flexible loops and divergent sequences around the substrate entrance region. Here, we report the newly identified CYP101D5 from . CYP101D5 catalyzes the hydroxylation of β-ionone and flavonoids, including naringenin and apigenin, and causes the dehydrogenation of α-ionone. A structural investigation and comparison with other CYP101 families indicated that spatial constraints at the substrate-recognition site originate from the B/C loop. Furthermore, charge distribution at the substrate binding site may be important for substrate selectivity and the preference for CYP101D5.

PubMed: 36362105
DOI: 10.3390/ijms232113317

実験手法

X-RAY DIFFRACTION (3.2 Å)