An unprecedented NADPH domain conformation in lysine monooxygenase NbtG provides insights into uncoupling of oxygen consumption from substrate hydroxylation

Journal of Biological Chemistry

Volumn 290, Issue 20, 2015, Pages 12676-12688

  Binda, Claudia ^a   Robinson, Reeder M ^b   Martin Del Campo, Julia S ^b   Keul, Nicholas D ^b   Rodriguez, Pedro J ^b   Robinson, Howard H ^c   Mattevi, Andrea ^a   Sobrado, Pablo ^b  

^a UNIVERSITY OF PAVIA   (Italy)

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

^c BROOKHAVEN NATIONAL LABORATORY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS; BIOCHEMISTRY; HYDROXYLATION; OXYGEN;

BIOCHEMICAL PROPERTIES; BIOLOGICAL IMPLICATIONS; FLAVIN ADENINE DINUCLEOTIDE; NICOTINAMIDE COFACTOR; OXYGEN CONSUMPTION; PROTEIN CONFORMATION; STRUCTURAL CHARACTERIZATION; SUBSTRATE HYDROXYLATION;

CRYSTAL STRUCTURE;

FLAVINE ADENINE NUCLEOTIDE; HYDROGEN PEROXIDE; LYSINE MONOOXYGENASE NBTG; NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE; REACTIVE OXYGEN METABOLITE; SUPEROXIDE; UNCLASSIFIED DRUG; UNSPECIFIC MONOOXYGENASE; BACTERIAL PROTEIN; LYSINE; LYSINE MONOOXYGENASE; MIXED FUNCTION OXIDASE;

AMINO ACID SUBSTITUTION; AMINOHYDROXYLATION; ARTICLE; BINDING AFFINITY; BINDING SITE; CONTROLLED STUDY; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME BINDING; ENZYME MECHANISM; ENZYME METABOLISM; ENZYME STRUCTURE; HYDROGEN BOND; NOCARDIA FARCINICA; NONHUMAN; NUCLEIC ACID METABOLISM; OXYGEN CONSUMPTION; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN EXPRESSION; CHEMISTRY; ENZYMOLOGY; GENETICS; HYDROXYLATION; METABOLISM; NOCARDIA; PHYSIOLOGY; PROTEIN TERTIARY STRUCTURE; X RAY CRYSTALLOGRAPHY;

NOCARDIA FARCINICA;

BACTERIAL PROTEINS; CRYSTALLOGRAPHY, X-RAY; FLAVIN-ADENINE DINUCLEOTIDE; HYDROXYLATION; LYSINE; MIXED FUNCTION OXYGENASES; NADP; NOCARDIA; OXYGEN CONSUMPTION; PROTEIN STRUCTURE, TERTIARY;

EID: 84929378443     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M114.629485     Document Type: Article

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