Increase of the deacylation rate of PBP2x from Streptococcus pneumoniae by single point mutations mimicking the class A β-lactamases

European Journal of Biochemistry

Volumn 269, Issue 6, 2002, Pages 1678-1683

  Chesnel, Laurent ^a   Zapun, André ^a   Mouz, Nicolas ^b   Dideberg, Otto ^b   Vernet, Thierry ^a,b  

^a Laboratoire d'Ingénierie des Macromolécules LIM   (France)

^b INSTITUT DE BIOLOGIE STRUCTURALE   (France)

Author keywords

lactamase; Antibiotic resistance protein engineering; Deacylation; Penicillin binding protein

Indexed keywords

AMINO ACID; BETA LACTAM ANTIBIOTIC; BETA LACTAMASE; CEPHALOSPORIN DERIVATIVE; GAMMA GLUTAMYLTRANSFERASE; PENICILLIN BINDING PROTEIN;

ANTIBIOTIC RESISTANCE; ANTIMICROBIAL ACTIVITY; ARTICLE; CONTROLLED STUDY; DEACYLATION; ENZYME ACTIVITY; ENZYME INHIBITION; HYDROLYSIS; NONHUMAN; PH; POINT MUTATION; PRIORITY JOURNAL; PROTEIN DOMAIN; REGULATORY MECHANISM; STREPTOCOCCUS PNEUMONIAE;

ACYLATION; BETA-LACTAMASES; CARRIER PROTEINS; HYDROLYSIS; KINETICS; PENICILLIN-BINDING PROTEINS; POINT MUTATION; STREPTOCOCCUS PNEUMONIAE;

BACTERIA (MICROORGANISMS); ESCHERICHIA COLI; POSIBACTERIA; STREPTOCOCCUS; STREPTOCOCCUS PNEUMONIAE;

EID: 0036227417     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1432-1327.2002.02815.x     Document Type: Article

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