6G5O

The structure of a carbohydrate active P450

6G5O の概要

• エントリーDOI: 10.2210/pdb6g5o/pdb
• 分子名称: Cytochrome P450, PROTOPORPHYRIN IX CONTAINING FE (3 entities in total)
• 機能のキーワード: p450, monooxygenase, carbohydrate-active enzyme, oxidoreductase
• 由来する生物種: Zobellia galactanivorans
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 92233.65

構造登録者

Robb, C.S.,Hehemann, J.H. (登録日: 2018-03-29, 公開日: 2018-11-21, 最終更新日: 2024-01-17)

主引用文献

Robb, C.S.,Reisky, L.,Bornscheuer, U.T.,Hehemann, J.H.
Specificity and mechanism of carbohydrate demethylation by cytochrome P450 monooxygenases.
Biochem. J., 475:3875-3886, 2018

PubMed Abstract: Degradation of carbohydrates by bacteria represents a key step in energy metabolism that can be inhibited by methylated sugars. Removal of methyl groups, which is critical for further processing, poses a biocatalytic challenge because enzymes need to overcome a high energy barrier. Our structural and computational analysis revealed how a member of the cytochrome P450 family evolved to oxidize a carbohydrate ligand. Using structural biology, we ascertained the molecular determinants of substrate specificity and revealed a highly specialized active site complementary to the substrate chemistry. Invariance of the residues involved in substrate recognition across the subfamily suggests that they are critical for enzyme function and when mutated, the enzyme lost substrate recognition. The structure of a carbohydrate-active P450 adds mechanistic insight into monooxygenase action on a methylated monosaccharide and reveals the broad conservation of the active site machinery across the subfamily.

PubMed: 30404923
DOI: 10.1042/BCJ20180762

実験手法

X-RAY DIFFRACTION (2.25 Å)