Oxidative maturation and structural characterization of prenylated FMN binding by UbiD, a decarboxylase involved in bacterial ubiquinone biosynthesis

Journal of Biological Chemistry

Volumn 292, Issue 11, 2017, Pages 4623-4637

  Marshall, Stephen A ^a   Fisher, Karl ^a   Cheallaigh, Aisling Ní ^a,c   White, Mark D ^a,d   Payne, Karl A P ^a   Parker, D A ^b   Rigby, Stephen E J ^a   Leys, David ^a  

^a UNIVERSITY OF MANCHESTER   (United Kingdom)

^b SHELL GLOBAL SOLUTIONS INTERNATIONAL B V   (United States)

^c ASTRAZENECA   (United Kingdom)

^d UNIVERSITY OF OXFORD   (United Kingdom)

Author keywords

[No Author keywords available]

Indexed keywords

ALKALINITY; BIOCHEMISTRY; BIOSYNTHESIS; CARBOXYLATION; ENZYMES; ESCHERICHIA COLI; FREE RADICAL REACTIONS; OXIDATION; SUBSTRATES;

1 ,3-DIPOLARCYCLOADDITION; DECARBOXYLASE ENZYMES; DECARBOXYLASES; DOMAIN MOTIONS; HYDROPHOBIC BINDING; HYDROXYBENZOIC ACIDS; PROTON COUPLED ELECTRON TRANSFERS; STRUCTURAL CHARACTERIZATION;

BINS;

4 HYDROXYBENZOIC ACID; APOENZYME; BACTERIAL ENZYME; FDC1 PROTEIN; FLAVINE MONONUCLEOTIDE; HOLOENZYME; PRENYLATED FLAVINE MONONUCLEOTIDE; PROTON; SULFITE; UBID PROTEIN; UBIQUINONE; UNCLASSIFIED DRUG; 3-OCTAPRENYL-4-HYDROXYBENZOATE CARBOXY-LYASE; CARBOXYLYASE;

ALKALINITY; ARTICLE; BINDING SITE; BIOSYNTHESIS; CONTROLLED STUDY; CRYSTAL STRUCTURE; ELECTRON TRANSPORT; ENZYME ACTIVATION; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME STRUCTURE; ENZYME SUBSTRATE; ESCHERICHIA COLI; IN VITRO STUDY; NONHUMAN; OXIDATION; PH; PROTEIN FAMILY; CHEMISTRY; ELECTRON SPIN RESONANCE; METABOLISM; MOLECULAR MODEL; OXIDATION REDUCTION REACTION; PRENYLATION; PROTEIN DOMAIN; X RAY CRYSTALLOGRAPHY;

BINDING SITES; CARBOXY-LYASES; CRYSTALLOGRAPHY, X-RAY; ELECTRON SPIN RESONANCE SPECTROSCOPY; ELECTRON TRANSPORT; ESCHERICHIA COLI; FLAVIN MONONUCLEOTIDE; MODELS, MOLECULAR; OXIDATION-REDUCTION; PRENYLATION; PROTEIN DOMAINS; UBIQUINONE;

EID: 85015310184     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M116.762732     Document Type: Article

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