Evolution in the amidohydrolase superfamily: Substrate-assisted gain of function in the E183K mutant of a phosphotriesterase-like metal-carboxylesterase

Biochemistry

Volumn 48, Issue 24, 2009, Pages 5602-5612

  Mandrich, Luigi ^a   Manco, Giuseppe ^a  

^a INSTITUTE OF PROTEIN BIOCHEMISTRY   (Italy)

Author keywords

[No Author keywords available]

Indexed keywords

AMIDOHYDROLASE SUPERFAMILY; BINUCLEAR METAL CENTER; BIOCHEMICAL CHARACTERIZATION; CARBOXYLESTERASE; DIVALENT CATION; GAIN-OF FUNCTION; IN-SILICO; KINETIC DATA; LACTONASE; MESORHIZOBIUM LOTI; PHOSPHODIESTERASE; PHOSPHODIESTERASE ACTIVITY; PHOSPHOTRIESTERASE; PSEUDOMONAS DIMINUTA; SEQUENCE SIMILARITY;

AMINO ACIDS; CATALYSTS; ENZYMES; ESCHERICHIA COLI; PHASE LOCKED LOOPS;

ENZYME ACTIVITY;

4 NITROPHENYLPHOSPHATASE; CARBOXYLESTERASE; GLUTAMIC ACID; HYDROLASE; LYSINE; PHOSPHOTRIESTERASE;

ARTICLE; BIOCHEMISTRY; CHEMICAL ANALYSIS; COMPUTER MODEL; ENZYME ACTIVITY; ENZYME SPECIFICITY; ESCHERICHIA COLI; KINETICS; MESORHIZOBIUM; MOLECULAR EVOLUTION; MUTANT; NONHUMAN; PREDICTION; PRIORITY JOURNAL;

ALPHAPROTEOBACTERIA; AMIDOHYDROLASES; AMINO ACID SEQUENCE; BINDING SITES; CARBOXYLESTERASE; ESCHERICHIA COLI; EVOLUTION, MOLECULAR; KINETICS; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MUTATION; NITROPHENOLS; PHOSPHORIC TRIESTER HYDROLASES; PROTEIN CONFORMATION; PSEUDOMONAS; SEQUENCE ALIGNMENT; SEQUENCE HOMOLOGY, AMINO ACID; STRUCTURE-ACTIVITY RELATIONSHIP; SUBSTRATE SPECIFICITY;

BREVUNDIMONAS DIMINUTA; ESCHERICHIA COLI; MESORHIZOBIUM LOTI;

EID: 67649213710     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi801932x     Document Type: Article

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