Substrate binding modulates the activity of mycobacterium smegmatis G, a flavin-dependent monooxygenase involved in the biosynthesis of hydroxamate-containing siderophores

Biochemistry

Volumn 50, Issue 39, 2011, Pages 8489-8496

  Robinson, Reeder ^a   Sobrado, Pablo ^a,b  

^a VIRGINIA POLYTECHNIC INSTITUTE AND STATE UNIVERSITY   (United States)

^b Fralin Life Science Institute   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

BIOSYNTHETIC PATHWAY; COFACTORS; FLAVIN-DEPENDENT MONOOXYGENASE; IONIC EXCHANGE; L-LYSINE; METAL AFFINITY; MONOOXYGENASES; MYCOBACTERIUM SMEGMATIS; NAD(P)H; OXIDASE ACTIVITY; OXYGEN CONSUMPTION; POTENTIAL DRUG; SIDE-CHAINS; SIDEROPHORES; STEADY-STATE CONDITION; SUBSTRATE BINDING; SUPEROXIDES; TERMINAL AMINO GROUPS;

BACTERIA; BIOCHEMISTRY; BIOSYNTHESIS; ENZYMES; ESCHERICHIA COLI; HYDROGEN; HYDROGEN PEROXIDE; HYDROXYLATION; ION EXCHANGE; OXYGEN;

AMINO ACIDS;

BACTERIAL PROTEIN; HYDROGEN PEROXIDE; HYDROXAMIC ACID; LYSINE; MYCOBACTERIUM SMEGMATIS G; OXIDOREDUCTASE; QUERCETIN; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE; SIDEROPHORE; SUPEROXIDE; UNCLASSIFIED DRUG; UNSPECIFIC MONOOXYGENASE;

ARTICLE; BIOSYNTHESIS; ENZYME ACTIVITY; ENZYME ISOLATION; ENZYME SUBSTRATE COMPLEX; ESCHERICHIA COLI; HYDROXYLATION; IMMOBILIZED METAL AFFINITY CHROMATOGRAPHY; MYCOBACTERIUM SMEGMATIS; NONHUMAN; OXYGEN CONSUMPTION; PRIORITY JOURNAL; PROTEIN EXPRESSION; STEADY STATE;

FLAVIN-ADENINE DINUCLEOTIDE; HYDROXAMIC ACIDS; KINETICS; MIXED FUNCTION OXYGENASES; MYCOBACTERIUM SMEGMATIS; OXAZOLES; OXYGEN CONSUMPTION; SIDEROPHORES; SUBSTRATE SPECIFICITY;

ESCHERICHIA COLI; MAMMALIA; MYCOBACTERIUM; MYCOBACTERIUM SMEGMATIS;

EID: 80053401997     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi200933h     Document Type: Article

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