Hydroxyl groups in the ββ sandwich of metallo-β-lactamases favor enzyme activity: A computational protein design study

Journal of Molecular Biology

Volumn 350, Issue 3, 2005, Pages 395-401

  Oelschlaeger, Peter ^a,c   Mayo, Stephen L ^b  

^a California Institute of Technology HHMI   (United States)

^b HOWARD HUGHES MEDICAL INSTITUTE   (United States)

^c UNIVERSITY OF SOUTHERN CALIFORNIA   (United States)

Author keywords

Catalytic efficiency; Metallo lactamase; Protein design; Substrate specificity; Zinc lactamase

Indexed keywords

BETA LACTAMASE; HYDROXYL GROUP; IMIPENEMASE; MUTANT PROTEIN; UNCLASSIFIED DRUG;

AMINO ACID SEQUENCE; ARTICLE; CALCULATION; CATALYSIS; DRUG HYDROLYSIS; ENZYME ACTIVITY; ENZYME MECHANISM; ENZYME SPECIFICITY; ENZYME SUBSTRATE; MATHEMATICAL ANALYSIS; PREDICTION; PRIORITY JOURNAL;

EID: 20444440035     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2005.04.044     Document Type: Article

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