1FOH

PHENOL HYDROXYLASE FROM TRICHOSPORON CUTANEUM

1FOH の概要

• エントリーDOI: 10.2210/pdb1foh/pdb
• 分子名称: PHENOL HYDROXYLASE, FLAVIN-ADENINE DINUCLEOTIDE, PHENOL, ... (4 entities in total)
• 機能のキーワード: flavin, phenol hydroxylase, monooxygenase, oxidoreductase
• 由来する生物種: Trichosporon cutaneum
• 細胞内の位置: Cytoplasm: P15245
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 304309.21

構造登録者

Enroth, C.,Neujahr, H.,Schneider, G.,Lindqvist, Y. (登録日: 1998-03-26, 公開日: 1998-06-17, 最終更新日: 2024-02-07)

主引用文献

Enroth, C.,Neujahr, H.,Schneider, G.,Lindqvist, Y.
The crystal structure of phenol hydroxylase in complex with FAD and phenol provides evidence for a concerted conformational change in the enzyme and its cofactor during catalysis.
Structure, 6:605-617, 1998

PubMed Abstract: The synthesis of phenolic compounds as by-products of industrial reactions poses a serious threat to the environment. Understanding the enzymatic reactions involved in the degradation and detoxification of these compounds is therefore of much interest. Soil-living yeasts use flavin adenine dinucleotide (FAD)-containing enzymes to hydroxylate phenols. This reaction initiates a metabolic sequence permitting utilisation of the aromatic compound as a source of carbon and energy. The phenol hydroxylase from Trichosporon cutaneum hydroxylates phenol to catechol. Phenol is the best substrate, but the enzyme also accepts simple hydroxyl-, amino-, halogen- or methyl-substituted phenols.

PubMed: 9634698
DOI: 10.1016/S0969-2126(98)00062-8

実験手法

X-RAY DIFFRACTION (2.4 Å)