Replacement of Tryptophan Residues in Haloalkane Dehalogenase Reduces Halide Binding and Catalytic Activity

European Journal of Biochemistry

Volumn 228, Issue 2, 1995, Pages 403-407

  Kennes, Christian ^a   Pries, Frens ^a   Krooshof, Geja H ^a   Bokma, Evert ^a   Kingma, Jaap ^a   Janssen, Dick B ^a  

^a UNIVERSITY OF GRONINGEN   (Netherlands)

Author keywords

1,2 dichloroethane; Haloalkane dehalogenase; hydrolase; site directed mutagenesis; tryptophan

Indexed keywords

HALOALKANE DEHALOGENASE; HYDROLASE; UNCLASSIFIED DRUG;

ARTICLE; BACTERIUM; ENZYME ACTIVE SITE; ENZYME ACTIVITY; PRIORITY JOURNAL; SITE DIRECTED MUTAGENESIS; STRUCTURE ACTIVITY RELATION;

AMINO ACID SEQUENCE; BASE SEQUENCE; BINDING SITES; BROMIDES; CHLORIDES; DEUTERIUM OXIDE; HYDROLASES; KINETICS; MOLECULAR SEQUENCE DATA; MUTAGENESIS, SITE-DIRECTED; STRUCTURE-ACTIVITY RELATIONSHIP; SUPPORT, NON-U.S. GOV'T; TRYPTOPHAN;

BACTERIA (MICROORGANISMS); FELIS CATUS;

EID: 0028942983     PISSN: 00142956     EISSN: 14321033     Source Type: Journal    
DOI: 10.1111/j.1432-1033.1995.00403.x     Document Type: Article

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