How does an enzyme evolved in vitro compare to naturally occurring homologs possessing the targeted function? Tyrosine aminotransferase from aspartate aminotransferase

Journal of Molecular Biology

Volumn 327, Issue 3, 2003, Pages 593-608

  Rothman, Steven C ^a   Kirsch, Jack F ^a  

^a UNIVERSITY OF CALIFORNIA   (United States)

Author keywords

Aminotransferase; DNA shuffling; Enzyme evolution; Substrate specificity; Venn diagrams

Indexed keywords

AMINO ACID; ASPARTATE AMINOTRANSFERASE; ENZYME VARIANT; HYDROCINNAMIC ACID; PHENYL GROUP; TYROSINE AMINOTRANSFERASE;

AMINO ACID SUBSTITUTION; ARTICLE; CLONE; CONTROLLED STUDY; CRYSTAL STRUCTURE; ENZYME ACTIVITY; ESCHERICHIA COLI; EVOLUTIONARY HOMOLOGY; GENE MUTATION; IN VITRO STUDY; METHODOLOGY; MOLECULAR EVOLUTION; NONHUMAN; PRIORITY JOURNAL; PROTEIN FUNCTION; SEQUENCE HOMOLOGY; SITE DIRECTED MUTAGENESIS; STATISTICAL SIGNIFICANCE; THEORY; WILD TYPE;

ESCHERICHIA COLI;

EID: 0037470619     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0022-2836(03)00095-0     Document Type: Article

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