Kinetic isotope effects on the noncovalent flavin mutant protein of pyranose 2-oxidase reveal insights into the flavin reduction mechanism

Biochemistry

Volumn 49, Issue 17, 2010, Pages 3753-3765

  Sucharitakul, Jeerus ^a   Wongnate, Thanyaporn ^b   Chaiyen, Pimchai ^b  

^a CHULALONGKORN UNIVERSITY   (Thailand)

^b MAHIDOL UNIVERSITY   (Thailand)

Author keywords

[No Author keywords available]

Indexed keywords

BINDING MODES; COFACTORS; COVALENT LINKAGE; D-GLUCOSE; FLAVIN ADENINE DINUCLEOTIDE; GAIN INSIGHT; H-BONDS; HALF-REACTIONS; KINETIC CONSTANT; KINETIC ISOTOPE EFFECTS; KINETIC MECHANISM; KINETIC SIMULATION; MICHAELIS COMPLEX; MUTANT PROTEINS; NONCOVALENT; OH GROUP; PRIMARY ISOTOPE EFFECT; PYRANOSE; REACTION MECHANISM; REDUCTION MECHANISMS; SOLVENT KINETIC ISOTOPE EFFECTS; STEADY-STATE KINETICS; TRANSIENT KINETIC DATA; TRANSIENT KINETICS; WILD TYPES; WILD-TYPE ENZYMES;

BINDING ENERGY; CARRIER MOBILITY; ENZYMES; ISOTOPES; MOLECULAR OXYGEN; OXIDATION; RATE CONSTANTS; REACTION INTERMEDIATES;

GLUCOSE;

1,2,3,4,5,6,6 DELTA7 DEXTRO GLUCOSE; 2 DELTA DEXTRO GLUCOSE; 3 DELTA DEXTRO GLUCOSE; 8A N 3 HISTIDYL FLAVIN ADENINE DINUCLEOTIDE; ALANINE; CARBON; ENZYME; FLAVINE ADENINE NUCLEOTIDE; FLAVINE NUCLEOTIDE; FLAVOPROTEIN; GLUCOSE; GLUCOSE DERIVATIVE; HISTIDINE; HYDROGEN PEROXIDE; HYDROXYL GROUP; OXIDOREDUCTASE; OXYGEN; PYRANOSE 2 OXIDASE; SOLVENT; UNCLASSIFIED DRUG;

AMINO ACID SUBSTITUTION; ARTICLE; BINDING AFFINITY; CATALYSIS; CHEMICAL BOND; COMPLEX FORMATION; CONTROLLED STUDY; CROSS LINKING; DEPROTONATION; ENZYME KINETICS; ENZYME SPECIFICITY; ISOTOPE ANALYSIS; KINETIC ISOTOPE EFFECT; MICHAELIS CONSTANT; MUTANT; OXIDATION REDUCTION REACTION; PRIORITY JOURNAL; PROTEIN CLEAVAGE; PROTON TRANSPORT; WILD TYPE;

AMINO ACID SUBSTITUTION; BINDING SITES; CARBOHYDRATE DEHYDROGENASES; CATALYSIS; CATALYTIC DOMAIN; FLAVINS; GLUCOSE; KINETICS; MODELS, MOLECULAR; MOLECULAR STRUCTURE; MUTAGENESIS, SITE-DIRECTED; MUTANT PROTEINS; MUTATION; OXIDATION-REDUCTION; TRAMETES;

TRAMETES OCHRACEA;

EID: 77951683048     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi100187b     Document Type: Article

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