Substitution of Arg-244 by Cys or Ser in SHV-1 and SHV-5 β-lactamases confers resistance to mechanism-based inhibitors and reduces catalytic efficiency of the enzymes

FEMS Microbiology Letters

Volumn 160, Issue 1, 1998, Pages 49-54

  Giakkoupi, Panagiota ^a   Tzelepi, Eva ^a   Legakis, Nicholas J ^b   Tzouvelekis, Leonidas S ^a,b  

^a HELLENIC PASTEUR INSTITUTE   (Greece)

^b UNIVERSITY OF ATHENS MEDICAL SCHOOL   (Greece)

Author keywords

Arginine 244; Clavulanate resistance; SHV lactamase

Indexed keywords

AMOXICILLIN; AMOXICILLIN PLUS CLAVULANIC ACID; ARGININE; AZTREONAM; BETA LACTAMASE; BETA LACTAMASE INHIBITOR; CEFACLOR; CEFALOTIN; CEFOTAXIME; CEFPROZIL; CEFTAZIDIME; CEFTRIAXONE; CLAVULANIC ACID; CYSTEINE; PENICILLIN G; PIPERACILLIN; PIPERACILLIN PLUS TAZOBACTAM; SERINE; SULBACTAM; SULTAMICILLIN; TAZOBACTAM; TICARCILLIN;

AMINO ACID SUBSTITUTION; ANTIBIOTIC RESISTANCE; ARTICLE; BINDING AFFINITY; CONTROLLED STUDY; ENZYME ACTIVE SITE; ENZYME ACTIVITY; MINIMUM INHIBITORY CONCENTRATION; NONHUMAN; POLYMERASE CHAIN REACTION; PRIORITY JOURNAL; SITE DIRECTED MUTAGENESIS;

AMINO ACID SUBSTITUTION; ANTI-BACTERIAL AGENTS; ARGININE; BETA-LACTAMASES; CLAVULANIC ACID; CLONING, MOLECULAR; CYSTEINE; ESCHERICHIA COLI; MICROBIAL SENSITIVITY TESTS; PENICILLIN RESISTANCE; SERINE;

NEGIBACTERIA;

EID: 0032031376     PISSN: 03781097     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0378-1097(98)00009-3     Document Type: Article

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