1W4X

Phenylacetone Monooxygenase, a Baeyer-Villiger Monooxygenase

1W4X の概要

• エントリーDOI: 10.2210/pdb1w4x/pdb
• 分子名称: PHENYLACETONE MONOOXYGENASE, FLAVIN-ADENINE DINUCLEOTIDE, SULFATE ION, ... (4 entities in total)
• 機能のキーワード: baeyer-villiger, monooxygenase, fad, oxygenase
• 由来する生物種: THERMOBIFIDA FUSCA
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 62073.06

構造登録者

Malito, E.,Alfieri, A.,Mattevi, A. (登録日: 2004-08-03, 公開日: 2004-09-02, 最終更新日: 2024-05-08)

主引用文献

Malito, E.,Alfieri, A.,Fraaije, M.W.,Mattevi, A.
Crystal Structure of a Baeyer-Villiger Monooxygenase
Proc.Natl.Acad.Sci.USA, 101:13157-, 2004

PubMed Abstract: Flavin-containing Baeyer-Villiger monooxygenases employ NADPH and molecular oxygen to catalyze the insertion of an oxygen atom into a carbon-carbon bond of a carbonylic substrate. These enzymes can potentially be exploited in a variety of biocatalytic applications given the wide use of Baeyer-Villiger reactions in synthetic organic chemistry. The catalytic activity of these enzymes involves the formation of two crucial intermediates: a flavin peroxide generated by the reaction of the reduced flavin with molecular oxygen and the "Criegee" intermediate resulting from the attack of the flavin peroxide onto the substrate that is being oxygenated. The crystal structure of phenylacetone monooxygenase, a Baeyer-Villiger monooxygenase from the thermophilic bacterium Thermobifida fusca, exhibits a two-domain architecture resembling that of the disulfide oxidoreductases. The active site is located in a cleft at the domain interface. An arginine residue lays above the flavin ring in a position suited to stabilize the negatively charged flavin-peroxide and Criegee intermediates. This amino acid residue is predicted to exist in two positions; the "IN" position found in the crystal structure and an "OUT" position that allows NADPH to approach the flavin to reduce the cofactor. Domain rotations are proposed to bring about the conformational changes involved in catalysis. The structural studies highlight the functional complexity of this class of flavoenzymes, which coordinate the binding of three substrates (molecular oxygen, NADPH, and phenylacetone) in proximity of the flavin cofactor with formation of two distinct catalytic intermediates.

PubMed: 15328411
DOI: 10.1073/PNAS.0404538101

実験手法

X-RAY DIFFRACTION (1.7 Å)