4C74

Phenylacetone monooxygenase: Reduced enzyme in complex with APADP

4C74 の概要

• エントリーDOI: 10.2210/pdb4c74/pdb
• 分子名称: PHENYLACETONE MONOOXYGENASE, FLAVIN-ADENINE DINUCLEOTIDE, 3-ACETYLPYRIDINE ADENINE DINUCLEOTIDE, ... (5 entities in total)
• 機能のキーワード: oxidoreductase, flavin, baeyer-villiger, cofactor
• 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: 62998.72

構造登録者

Martinoli, C.,Fraaije, M.W.,Mattevi, A. (登録日: 2013-09-19, 公開日: 2014-02-05, 最終更新日: 2023-12-20)

主引用文献

Martinoli, C.,Dudek, H.M.,Orru, R.,Edmondson, D.E.,Fraaije, M.W.,Mattevi, A.
Beyond the Protein Matrix: Probing Cofactor Variants in a Baeyer-Villiger Oxygenation Reaction.
Acs Catal., 3:3058-, 2013

PubMed Abstract: A general question in biochemistry is the interplay between the chemical properties of cofactors and the surrounding protein matrix. Here, the functions of NADP and FAD are explored by investigation of a representative monooxygenase reconstituted with chemically-modified cofactor analogues. Like pieces of a jigsaw puzzle, the enzyme active site juxtaposes the flavin and nicotinamide rings, harnessing their H-bonding and steric properties to finely construct an oxygen-reacting center that restrains the flavin-peroxide intermediate in a catalytically-competent orientation. Strikingly, the regio- and stereoselectivities of the reaction are essentially unaffected by cofactor modifications. These observations indicate a remarkable robustness of this complex multi-cofactor active site, which has implications for enzyme design based on cofactor engineering approaches.

PubMed: 24443704
DOI: 10.1021/CS400837Z

実験手法

X-RAY DIFFRACTION (1.97 Å)