A phenylalanine clamp controls substrate specificity in the quorum-quenching metallo-γ-lactonase from Bacillus thuringiensis

Biochemistry

Volumn 52, Issue 9, 2013, Pages 1603-1610

  Liu, Ce Feng ^a,d   Liu, Dali ^b   Momb, Jessica ^c   Thomas, Pei W ^c   Lajoie, Ashley ^a   Petsko, Gregory A ^a   Fast, Walter ^c   Ringe, Dagmar ^a  

^a BRANDEIS UNIVERSITY   (United States)

^b LOYOLA UNIVERSITY CHICAGO   (United States)

^c UNIVERSITY OF TEXAS AT AUSTIN   (United States)

^d WEILL CORNELL MEDICAL COLLEGE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

AROMATIC RESIDUES; BACILLUS THURINGIENSIS; BINDING INTERACTION; BINDING POCKETS; HOMOSERINE; HYDROPHOBIC BINDING; HYDROPHOBIC CAVITIES; LACTONASE; LIGAND BINDING; METAL CENTERS; MUTATION RESULTS; N-ACYL HOMOSERINE LACTONES; REDOX SENSITIVES; RING-OPENED PRODUCTS; STEADY-STATE KINETICS; SUBSTRATE SPECIFICITY;

AMINO ACIDS; BACTERIOLOGY; BINDING ENERGY; HYDROPHOBICITY; QUENCHING;

SUBSTRATES;

BACTERIAL ENZYME; CARBON; CYSTEINE; METALLO GAMMA LACTONASE; PHENYLALANINE; SERINE DERIVATIVE; UNCLASSIFIED DRUG;

ARTICLE; BACILLUS THURINGIENSIS; BACTERIAL MUTATION; BACTERIUM MUTANT; BINDING SITE; CONTROLLED STUDY; CRYSTAL STRUCTURE; CRYSTALLIZATION; ENZYME SPECIFICITY; HYDROLYSIS; HYDROPHOBICITY; LIGAND BINDING; MOLECULAR INTERACTION; NONHUMAN; OXIDATION REDUCTION REACTION; PRIORITY JOURNAL; PROTEIN LOCALIZATION; QUORUM SENSING; STEADY STATE; WILD TYPE;

AMIDOHYDROLASES; BACILLUS THURINGIENSIS; CRYSTALLOGRAPHY, X-RAY; HOMOSERINE; KINETICS; MODELS, MOLECULAR; MUTAGENESIS, SITE-DIRECTED; PHENYLALANINE; POINT MUTATION; PROTEIN CONFORMATION; QUORUM SENSING; SUBSTRATE SPECIFICITY;

EID: 84874639991     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi400050j     Document Type: Article

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