Tryptophan-47 in the active site of methylophaga sp. strain SK1 flavin-monooxygenase is important for hydride transfer

Archives of Biochemistry and Biophysics

Volumn 532, Issue 1, 2013, Pages 46-53

  Han, Andre ^a   Robinson, Reeder M ^a   Badieyan, Somayesadat ^a   Ellerbrock, Jacob ^a   Sobrado, Pablo ^a,b  

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

^b Fralin Life Science Institute   (United States)

Author keywords

Active site residue; Flavin; Flavin monooxygenases; Hydride transfer; Kinetic isotope effects

Indexed keywords

FLAVIN DEPENDENT MONOOXYGENASE; MUTANT PROTEIN; NICOTINAMIDE; NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE; OXYGEN; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE; THIAMAZOLE; TRIMETHYLAMINE; TRYPTOPHAN; UNCLASSIFIED DRUG; UNSPECIFIC MONOOXYGENASE;

AMINO ACID SEQUENCE; ARTICLE; BACTERIAL STRAIN; BACTERIUM; CONFORMATIONAL TRANSITION; CONTROLLED STUDY; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME CONFORMATION; ENZYME INACTIVATION; ENZYME KINETICS; ENZYME PURIFICATION; ENZYME STABILITY; METHYLOPHAGA; NONHUMAN; PRIORITY JOURNAL; PROTEIN EXPRESSION; SEQUENCE ALIGNMENT; SIMULATION; SITE DIRECTED MUTAGENESIS; SOLVENT EFFECT; STEADY STATE; WILD TYPE;

METHYLOPHAGA;

EID: 84874398900     PISSN: 00039861     EISSN: 10960384     Source Type: Journal    
DOI: 10.1016/j.abb.2013.01.004     Document Type: Article

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