Evolution of a new function in an esterase: Simple amino acid substitutions enable the activity present in the larger paralog, BioH

Protein Engineering, Design and Selection

Volumn 25, Issue 8, 2012, Pages 387-395

  Flores, Humberto ^a   Lin, Steven ^b   Contreras Ferrat, Gabriel ^a   Cronan, John E ^b   Morett, Enrique ^a  

^a INSTITUTO DE BIOTECNOLOGÍA   (Mexico)

^b UNIVERSITY OF ILLINOIS AT URBANA CHAMPAIGN   (United States)

Author keywords

BioH activity; biotin; catalytic promiscuity; directed evolution of enzyme catalysis; esterase; PA3859

Indexed keywords

BIOTIN; CATALYTIC PROMISCUITY; ENZYME CATALYSIS; ESTERASE; PA3859;

AMINO ACIDS; BIOCHEMISTRY; COENZYMES; ENZYME ACTIVITY; ESTERS; GENES; PROTEINS;

CATALYST ACTIVITY;

BIOTIN; CARBOXYLESTERASE; ESTERASE;

AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; ARTICLE; AUXOTROPHY; BIOH GENE; CATALYSIS; CONTROLLED STUDY; ENZYME ACTIVITY; GENE; GENE DUPLICATION; GENE FUNCTION; GENETIC VARIABILITY; IN VITRO STUDY; IN VIVO STUDY; MOLECULAR EVOLUTION; MUTAGENESIS; NONHUMAN; PARALOGY; PRIORITY JOURNAL; PROTEIN FUNCTION; PROTEIN MODIFICATION; PSEUDOMONAS AERUGINOSA;

AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; CARBOXYLIC ESTER HYDROLASES; ESCHERICHIA COLI; ESCHERICHIA COLI PROTEINS; GENETIC COMPLEMENTATION TEST; MOLECULAR SEQUENCE DATA; PHENOTYPE; PLASMIDS; SEQUENCE ALIGNMENT;

PSEUDOMONAS AERUGINOSA;

EID: 84863655274     PISSN: 17410126     EISSN: 17410134     Source Type: Journal    
DOI: 10.1093/protein/gzs035     Document Type: Article

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