{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"omics_type":["Unknown"],"volume":["44(9)"],"submitter":["Giakkoupi P"],"pubmed_abstract":["A transferable beta-lactamase produced by a multidrug-resistant clinical isolate of Enterobacter cloacae was studied. The bla gene was carried by a large (>80-kb) transmissible plasmid. Nucleotide sequence analysis of cloned fragments revealed that it was part of a gene cassette carried by a class 1 integron along with other resistance genes, including aac(6')-Ib. The encoded beta-lactamase, designated IBC-1, was a novel class A enzyme that hydrolyzed ceftazidime and cefotaxime and was inhibited by tazobactam and, to a lesser extent, by clavulanate. Also, imipenem exhibited potent inhibitory activity against IBC-1. The enzyme consisted of 287 amino acid residues, including Ser-237, cysteines at positions 69 and 237a, and Arg-244, which may be implicated in its interaction with beta-lactams. In amino acid sequence comparisons, IBC-1 displayed the highest similarity with the chromosomal penicillinase of Yersinia enterocolitica, a carbenicillinase from Proteus mirabilis GN79, the species-specific beta-lactamases of Klebsiella oxytoca, and the carbapenemase Sme-1. However, a phylogenetic association with established beta-lactamase clusters could not be conclusively shown."],"journal":["Antimicrobial agents and chemotherapy"],"pagination":["2247-53"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC90053"],"repository":["biostudies-literature"],"pubmed_title":["IBC-1, a novel integron-associated class A beta-lactamase with extended-spectrum properties produced by an Enterobacter cloacae clinical strain."],"pmcid":["PMC90053"],"pubmed_authors":["Loukova V","Tzouvelekis LS","Tsakris A","Giakkoupi P","Sofianou D","Tzelepi E"],"additional_accession":[]},"is_claimable":false,"name":"IBC-1, a novel integron-associated class A beta-lactamase with extended-spectrum properties produced by an Enterobacter cloacae clinical strain.","description":"A transferable beta-lactamase produced by a multidrug-resistant clinical isolate of Enterobacter cloacae was studied. The bla gene was carried by a large (>80-kb) transmissible plasmid. Nucleotide sequence analysis of cloned fragments revealed that it was part of a gene cassette carried by a class 1 integron along with other resistance genes, including aac(6')-Ib. The encoded beta-lactamase, designated IBC-1, was a novel class A enzyme that hydrolyzed ceftazidime and cefotaxime and was inhibited by tazobactam and, to a lesser extent, by clavulanate. Also, imipenem exhibited potent inhibitory activity against IBC-1. The enzyme consisted of 287 amino acid residues, including Ser-237, cysteines at positions 69 and 237a, and Arg-244, which may be implicated in its interaction with beta-lactams. In amino acid sequence comparisons, IBC-1 displayed the highest similarity with the chromosomal penicillinase of Yersinia enterocolitica, a carbenicillinase from Proteus mirabilis GN79, the species-specific beta-lactamases of Klebsiella oxytoca, and the carbapenemase Sme-1. However, a phylogenetic association with established beta-lactamase clusters could not be conclusively shown.","dates":{"release":"2000-01-01T00:00:00Z","publication":"2000 Sep","modification":"2024-11-15T22:42:04.9Z","creation":"2019-03-27T00:18:25Z"},"accession":"S-EPMC90053","cross_references":{"pubmed":["10952563"],"doi":["10.1128/AAC.44.9.2247-2253.2000"]}}