A single mutation in a tunnel to the active site changes the mechanism and kinetics of product release in haloalkane dehalogenase LinB

Journal of Biological Chemistry

Volumn 287, Issue 34, 2012, Pages 29062-29074

  Biedermannová, Lada ^a,b   Prokop, Zbyněk ^b   Gora, Artur ^b   Chovancová, Eva ^b   Kovács, Mihály ^c   Damborský, Jiří ^b   Wade, Rebecca C ^a,d  

^a HEIDELBERG INSTITUTE FOR THEORETICAL STUDIES   (Germany)

^b MASARYK UNIVERSITY   (Czech Republic)

^c INSTITUTE OF EXPERIMENTAL MEDICINE   (Hungary)

^d UNIVERSITY OF HEIDELBERG   (Germany)

Author keywords

[No Author keywords available]

Indexed keywords

ACTIVE SITE; BROMIDE IONS; BULK SOLVENTS; CATALYTIC CYCLES; CATALYTIC PROPERTIES; DEHALOGENASE; LIGAND BINDING; MECHANISM AND KINETICS; MOLECULAR DYNAMICS SIMULATIONS; ONE-STEP PROCESS; POTENTIAL OF MEAN FORCE; PRODUCT RELEASE; RATE-LIMITING STEPS; SAMPLING TECHNIQUE; SINGLE MUTATION; TRANSIENT KINETICS; TUNNEL DETECTION; TURNOVER RATE; TWO-STEP PROCESS; WILD-TYPE ENZYMES;

AMINO ACIDS; ENERGY BARRIERS; ENZYMES; EXPERIMENTS; FREE ENERGY; IONS; LIGANDS; MOLECULAR DYNAMICS; RATE CONSTANTS; REACTION KINETICS;

KINETICS;

BROMIDE ION; HYDROLASE; LEUCINE; LINB PROTEIN; TRYPTOPHAN; UNCLASSIFIED DRUG;

AMINO ACID SUBSTITUTION; ARTICLE; BINDING AFFINITY; CATALYSIS; CONTROLLED STUDY; CRYSTAL STRUCTURE; DOWN REGULATION; ENZYME ACTIVE SITE; ENZYME ASSAY; ENZYME MECHANISM; FLUORESCENCE ANALYSIS; LIGAND BINDING; MATHEMATICAL MODEL; MOLECULAR DYNAMICS; MOLECULAR INTERACTION; MUTATIONAL ANALYSIS; PHYSICAL CHEMISTRY; PRIORITY JOURNAL; STATIC ELECTRICITY; STEADY STATE;

AMINO ACID SUBSTITUTION; BACTERIAL PROTEINS; CATALYSIS; CATALYTIC DOMAIN; HYDROLASES; KINETICS; MOLECULAR DYNAMICS SIMULATION; MUTATION, MISSENSE; PROTEIN STRUCTURE, TERTIARY; SPHINGOMONADACEAE;

EID: 84865201962     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M112.377853     Document Type: Article

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