PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 19736945-1 2009 Extended-spectrum beta-lactamases (ESBLs) are derivatives of enzymes such as SHV-1 and TEM-1 that have undergone site-specific mutations that enable them to hydrolyze, and thus inactivate, oxyimino-cephalosporins, such as cefotaxime and ceftazidime. Cefotaxime 222-232 CD248 molecule Homo sapiens 87-92 29527530-4 2018 Oxyimino-cephalosporins, such as cefotaxime and ceftazidime, however, are poor substrates for TEM-1 and were introduced, in part, to circumvent beta-lactamase-mediated resistance. Cefotaxime 33-43 CD248 molecule Homo sapiens 94-99 12183265-1 2002 In an early example of DNA shuffling, Stemmer (W. P. C. Stemmer, Nature 370:389-390, 1994) demonstrated a dramatic improvement in the activity of the TEM-1 beta-lactamase toward cefotaxime as the consequence of six amino acid substitutions. Cefotaxime 178-188 CD248 molecule Homo sapiens 150-155 9878443-4 1999 Here we report the results of an experiment in which we have hypermutated the bacterial enzyme TEM-1 beta-lactamase and selected small pools (<1.5x10(5)) of clones for enzymatic activity against the beta-lactam antibiotic cefotaxime. Cefotaxime 225-235 CD248 molecule Homo sapiens 95-100 9878443-5 1999 The experiment resulted in the isolation of a number of TEM-1 mutants with greatly improved activity against cefotaxime. Cefotaxime 109-119 CD248 molecule Homo sapiens 56-61 9878443-6 1999 Among these, clone 3D.5 (E104K:M182T:G238S) exhibited a minimum inhibitory concentration for cefotaxime 20,000-fold higher than wild-type TEM-1 and a catalytic efficiency (kcat/Km) 2383 times higher than the wild-type enzyme. Cefotaxime 93-103 CD248 molecule Homo sapiens 138-143 7547898-0 1995 Mass spectral kinetic study of acylation and deacylation during the hydrolysis of penicillins and cefotaxime by beta-lactamase TEM-1 and the G238S mutant. Cefotaxime 98-108 CD248 molecule Homo sapiens 127-132 7547898-1 1995 The G238S substitution found in extended-spectrum natural mutants of TEM-1 beta-lactamase induces a new capacity to hydrolyze cefotaxime and a large loss of activity against the good substrates of TEM-1. Cefotaxime 126-136 CD248 molecule Homo sapiens 69-74 7547898-1 1995 The G238S substitution found in extended-spectrum natural mutants of TEM-1 beta-lactamase induces a new capacity to hydrolyze cefotaxime and a large loss of activity against the good substrates of TEM-1. Cefotaxime 126-136 CD248 molecule Homo sapiens 197-202 7547898-3 1995 The hydrolysis of penicillins and cefotaxime by TEM-1 and the G238S mutant shows that the behavior of penicillins and cefotaxime is very different. Cefotaxime 34-44 CD248 molecule Homo sapiens 48-53 7547898-3 1995 The hydrolysis of penicillins and cefotaxime by TEM-1 and the G238S mutant shows that the behavior of penicillins and cefotaxime is very different. Cefotaxime 118-128 CD248 molecule Homo sapiens 48-53 7785992-5 1995 These three strains produced two beta-lactamases with pIs of 5.4 (TEM-1) and 7.6. beta-Lactamase assays revealed that the pI 7.6 enzyme hydrolyzed cefotaxime faster (at a relative hydrolysis rate of 30% compared with that of benzylpenicillin) than either ceftazidime or aztreonam (relative hydrolysis rates of 13 and 3.3%, respectively). Cefotaxime 147-157 CD248 molecule Homo sapiens 66-71 2550326-2 1989 The TEM-4 enzyme, which confers high-level resistance to cefotaxime (Ctx) and ceftazidime (Caz), differed from the TEM-1 penicillinase by four amino acid substitutions. Cefotaxime 57-67 CD248 molecule Homo sapiens 115-120 30501088-9 2018 A more exhaustive dynamic analysis, using a selection pressure for ampicillin and cefotaxime resistance on all possible types of substitutions in the amino acid sequence of TEM-1, further demonstrated the observed mechanism. Cefotaxime 82-92 CD248 molecule Homo sapiens 173-178 27173379-4 2016 We measured the effect on ampicillin resistance of ~12,500 unique single amino acid mutants of the TEM-1, TEM-17, TEM-19, and TEM-15 beta-lactamase alleles, which constitute an adaptive path in the evolution of cefotaxime resistance. Cefotaxime 211-221 CD248 molecule Homo sapiens 99-104 25489790-3 2015 Many of the active site residues are conserved between the CTX-M family and non-ESBL beta-lactamases such as TEM-1, but the residues Ser237 and Arg276 are specific to the CTX-M family, suggesting that they may help to define the increased specificity for cefotaxime hydrolysis. Cefotaxime 255-265 CD248 molecule Homo sapiens 109-114 25489790-5 2015 Substitutions of Ser237 and Arg276 with their TEM-1 counterparts, Ala237 and Asn276, had a modest effect on cefotaxime hydrolysis, as did removal of the Arg276 side chain in an R276A mutant. Cefotaxime 108-118 CD248 molecule Homo sapiens 46-51