4D04

Structure of the Cys65Asp mutant of phenylacetone monooxygenase: reduced state

4D04 の概要

• エントリーDOI: 10.2210/pdb4d04/pdb
• 関連するPDBエントリー: 4CZZ 4D03
• 分子名称: PHENYLACETONE MONOOXYGENASE, FLAVIN-ADENINE DINUCLEOTIDE, NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE, ... (5 entities in total)
• 機能のキーワード: oxidoreductase, biocatalysis
• 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: 63297.00

構造登録者

Brondani, P.B.,Dudek, H.M.,Martinoli, C.,Mattevi, A.,Fraaije, M.W. (登録日: 2014-04-24, 公開日: 2014-12-10, 最終更新日: 2023-12-20)

主引用文献

Brondani, P.B.,Dudek, H.M.,Martinoli, C.,Mattevi, A.,Fraaije, M.W.
Finding the Switch: Turning a Baeyer-Villiger Monooxygenase Into a Nadph Oxidase.
J.Am.Chem.Soc., 136:16966-, 2014

PubMed Abstract: By a targeted enzyme engineering approach, we were able to create an efficient NADPH oxidase from a monooxygenase. Intriguingly, replacement of only one specific single amino acid was sufficient for such a monooxygenase-to-oxidase switch-a complete transition in enzyme activity. Pre-steady-state kinetic analysis and elucidation of the crystal structure of the C65D PAMO mutant revealed that the mutation introduces small changes near the flavin cofactor, resulting in a rapid decay of the peroxyflavin intermediate. The engineered biocatalyst was shown to be a thermostable, solvent tolerant, and effective cofactor-regenerating biocatalyst. Therefore, it represents a valuable new biocatalytic tool.

PubMed: 25423359
DOI: 10.1021/JA508265B

実験手法

X-RAY DIFFRACTION (1.75 Å)