Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UMLS:C0276640 (TEM)
 20,729 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Resistance to oxyimino cephalosporins was originally highlighted by the emergence of plasmid-encoded extended-spectrum beta-lactamases deriving by mutation from TEM-1, TEM-2 and SHV type enzymes (class A). The broader spectrum of resistance produced by these enzymes is related to more amino acid substitutions, but susceptibility to seven alpha-methoxyimino cephalosporins and carbapenems was preserved until recently. Clavulanate-sensitive extended-spectrum beta-lactamases are distributed worldwide, mainly among Klebsiella pneumoniae isolates. Novel clavulanate-sensitive extended-spectrum beta-lactamases deriving from other class A enzymes (e.g. MEN-1 from beta la OXY, OXA-11 in Pseudomonas aeruginosa from PSE-2) have been reported. Recently, clavulanate-resistant extended-spectrum beta-lactamases (class C) were encountered amongst single isolates, mostly Klebsiella pneumoniae. These cephalosporinases or cefamycinases (usually chromosomally mediated) have expanded the spectrum of plasmid-encoded resistance to include seven alpha-methoxyimino cephalosporins. Thus far, only two isolates (1 Pseudomonas aeruginosa, 1 Bacteroides fragilis), both recovered in Japan, with plasmid-mediated resistance to carbapenems have been found.
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PMID:Origin and impact of plasmid-mediated extended-spectrum beta-lactamases. 782

The interactions of cefdinir, a new orally-active third-generation cephalosporin, with cell-free beta-lactamase preparations were studied in comparison with some other beta-lactams. Cefdinir was very resistant to narrow-spectrum Ambler's class A beta-lactamases, as it was for other oximino beta-lactams: cefotaxime, ceftazidime, cefixime and cefuroxime. Cefaclor showed a low but significant hydrolysis by these beta-lactamases. These class-A enzymes include the widespread plasmid mediated TEM-1, TEM-2, SHV-1 and also the enzymes of Gram-positive penicillinases, such as that produced by S. aureus. The hydrolysis of cefdinir was hardly detectable by the Ambler's class C beta-lactamases (cephalosporinases) produced by E. coli, E. cloacae and M. morganii. A similar conclusion is shown for cefotaxime, ceftazidime, cefixime and cefuroxime: for these beta-lactamases, the hydrolysis of cefaclor was high. The P. vulgaris cephalosporinase differs from the previous cephalosporinases in that it hydrolyses cefotaxime, cefuroxime and cefaclor efficiently. However, the hydrolysis of cefdinir remains too low to be detected. Cefdinir, as other third-generation cephalosporins, showed some hydrolysis by the novel extended-spectrum beta-lactamases (ESBL): SHV-2, TEM-3, TEM-5, MEN-1 and other ESBL.
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PMID:Interaction of cefdinir with beta-lactamases. 792 95

We have determined the nucleotide sequence (EMBL accession number, Z 21957) of the cloned chromosomal PER-1 extended-spectrum beta-lactamase gene from a Pseudomonas aeruginosa RNL-1 clinical isolate, blaPER-1 corresponds to a 924-bp open reading frame which encodes a polypeptide of 308 amino acids. This open reading frame is preceded by a -10 and a -35 region consistent with a putative P. aeruginosa promoter. Primer extension analysis of the PER-1 mRNA start revealed that this promoter was active in P. aeruginosa but not in Escherichia coli, in which PER-1 expression was driven by vector promoter sequences. N-terminal sequencing identified the PER-1 26-amino-acid leader peptide and enabled us to calculate the molecular mass (30.8 kDa) of the PER-1 mature form. Analysis of the percent GC content of blaPER-1 and of its 5' upstream sequences, as well as the codon usage for blaPER-1, indicated that blaPER-1 may have been inserted into P. aeruginosa genomic DNA from a nonpseudomonad bacterium. The PER-1 gene showed very low homology with other beta-lactamase genes at the DNA level. By using computer methods, assessment of the extent of identity between PER-1 and 10 beta-lactamase amino acid sequences indicated that PER-1 is a class A beta-lactamase. PER-1 shares around 27% amino acid identity with the sequenced extended-spectrum beta-lactamases of the TEM-SHV series and MEN-1 from Enterobacteriaceae species. The use of parsimony methods showed that PER-1 is not more closely related to gram-negative than to gram-positive bacterial class A beta-lactamases. Surprisingly, among class A beta-lactamases, PER-1 was most closely related to the recently reported CFXA from Bacteroides vulgatus, with which it shared 40% amino acid identity. This work indicates that non-Enterobacteriaceae species such as P. aeruginosa may possess class A extended-spectrum beta-lactamase genes possibly resulting from intergeneric DNA transfer.
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PMID:Sequence analysis of PER-1 extended-spectrum beta-lactamase from Pseudomonas aeruginosa and comparison with class A beta-lactamases. 814 62

Escherichia coli TUH12191, which is resistant to piperacillin, cefazolin, cefotiam, ceftizoxime, cefuzonam, and aztreonam but is susceptible to cefoxitin, latamoxef, flomoxef, and imipenem, was isolated from the urine of a patient treated with beta-lactam antibiotics. The beta-lactamase (Toho-1) purified from the bacteria had a pI of 7.8, had a molecular weight of about 29,000, and hydrolyzed beta-lactam antibiotics such as penicillin G, ampicillin, oxacillin, carbenicillin, piperacillin, cephalothin, cefoxitin, cefotaxime, ceftazidime, and aztreonam. Toho-1 was markedly inhibited by beta-lactamase inhibitors such as clavulanic acid and tazobactam. Resistance to beta-lactams, streptomycin, spectinomycin, sulfamethoxazole, and trimethoprim was transferred by conjugational transfer from E. coli TUH12191 to E. coli ML4903, and the transferred plasmid was about 58 kbp, belonging to incompatibility group M. The cefotaxime resistance gene for Toho-1 was subcloned from the 58-kbp plasmid by transformation of E. coli MV1184. The sequence of the gene for Toho-1 was determined, and the open reading frame of the gene consisted of 873 or 876 bases (initial sequence, ATGATG). The nucleotide sequence of the gene (DDBJ accession number D37830) was found to be about 73% homologous to the sequence of the gene encoding a class A beta-lactamase produced by Klebsiella oxytoca E23004. According to the amino acid sequence deduced from the DNA sequence, the precursor consisted of 290 or 291 amino acid residues, which contained amino acid motifs common to class A beta-lactamases (70SXXK, 130SDN, and 234KTG). Toho-1 was about 83% homologous to the beta-lactamase mediated by the chromosome of K. oxytoca D488 and the beta-lactamase mediated by the plasmid of E. coli MEN-1. Therefore, the newly isolated beta-lactamase Toho-1 produced by E. coli TUH12191 is similar to beta-lactamases produced by K. oxytoca D488, K. oxytoca E23004, and E. coli MEN-1 rather than to mutants of TEM or SHV enzymes. Toho-1 has shown the highest degree of similarity to K. oxytoca class A beta-lactamase. Detailed comparison of Toho-1 with other beta-lactamases implied that replacement of Asn-276 by Arg with the concomitant substitution of Thr for Arg-244 is an important mutation in the extension of the substrate specificity.
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PMID:Cloning and sequence of the gene encoding a cefotaxime-hydrolyzing class A beta-lactamase isolated from Escherichia coli. 1118 30

Amino acid sequences determined either by protein sequencing or by DNA sequencing are identical for cefotaximases CTX-M-1 and MEN-1, whereas CTX-M-2 is 84% identical to CTX-M-1/MEN-1. Both beta-lactamases are distantly related to other plasmidic class A enzymes (homology to TEM-1 is 38.1% for CTX-M-1/MEN-1 and 36.5% for CTX-M-2); the closest relationship was with the chromosomal beta-lactamase of Klebsiella oxytoca E23004 (homologies of 74.5% for CTX-M-1/MEN-1 and 77.9% for CTX-M-2). The cefotaximases CTX-M-1/MEN-1 and CTX-M-2 represent two members of a new subgroup of plasmidic class A beta-lactamases.
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PMID:Sequences of beta-lactamase genes encoding CTX-M-1 (MEN-1) and CTX-M-2 and relationship of their amino acid sequences with those of other beta-lactamases. 883 13

Serratia fonticola CUV produces two isoenzymes (forms I and II) with beta-lactamase activity which were purified by a five-step procedure. The isoenzymes had identical kinetic parameters and isoelectric point (pI = 8.12). They were characterized by a specific activity towards benzylpenicillin of 1650 U/mg. The beta-lactamase hydrolyzed benzylpenicillin, amoxycillin, ureidopenicillins, first- and second-generation cephalosporins. Carboxypenicillins and isoxazolylpenicillins were hydrolyzed to a lesser extent. Towards cefotaxime and ceftriaxone (third-generation cephalosporins), the S. fonticola enzyme exhibited catalytic efficiencies much higher than those of MEN-1 and extended-spectrum TEM derivative beta-lactamases. The beta-lactamase from S. fonticola was markedly inhibited by beta-lactamase inhibitors such as clavulanic acid, sulbactam and tazobactam. The purified isoenzymes were digested by trypsin, endoproteinase Asp-N and chymotrypsin. Amino acid sequence determinations of the resulting peptides allowed the alignment of 267 amino acid residues (Swiss-Prot, accession number P 80545) for form I beta-lactamase. Form II is five residues shorter than form I at its N-terminus. From amino acid sequence comparisons, S. fonticola CUV beta-lactamase was found to share more than 69.3% identity with the chromosomally encoded beta-lactamases of Klebsiella oxytoca, Proteus vulgaris, Citrobacter diversus and the plasmid-mediated enzymes MEN-1 and Toho-1. Therefore, the oxyimino cephalosporin-hydrolyzing beta-lactamase of S. fonticola belongs to Ambler's class A. Contribution of the serine at ABL 237 in the broad-spectrum activity of these beta-lactamases is discussed.
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PMID:Characterization and amino acid sequence analysis of a new oxyimino cephalosporin-hydrolyzing class A beta-lactamase from Serratia fonticola CUV. 930 Aug 9

beta-Lactam resistance among Enterobacteriaceae is related primarily to the emergence of novel beta-lactamases. The class A extended-spectrum beta-lactamases hydrolyze extended-spectrum beta-lactams and are inhibited by clavulanic acid. These beta-lactamases are divided in two groups: TEM and SHV derivatives and non-TEM and non-SHV extended-spectrum beta-lactamases (CTX-M1, CTX-M2, MEN-1, PER-1, PER-2, TOHO-1, and VEB-1). The plasmid-mediated cephalosporinases (MIR-1, FOX-1, MOX-1, BIL-1, CMY-1, CMY-2, and LAT-1) hydrolyze extended-spectrum cephalosporins and cephamycins and are not inhibited by clavulanic acid. They have been reported in Europe and in the United States. The 15 inhibitor-resistant penicillinases are TEM derivatives (except for SHV-10) and plasmid mediated, and they are mainly from Escherichia coli isolates. The carbapenemases noted among Enterobacteriaceae are either the chromosomally located penicillinases (Sme-1, NmcA, IMI-1) found in rare Enterobacter cloacae or Serratia marcescens isolates or the plasmid-mediated metalloenzyme IMP-1 that is widespread in Japan. The incidence of resistance among Enterobacteriaceae related to the other more common beta-lactam-resistance mechanisms has continued to rise worldwide.
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PMID:Trends in beta-lactam resistance among Enterobacteriaceae. 971 Jun 78

A robust and fast DNA chip method was developed in order to detect the various beta-lactam antibiotic-resistance genes in one slide. These genes included PSE, OXA, FOX, MEN, CMY, TEM, SHV, OXY, and AmpC. beta-lactam antibiotic-resistance genes were labeled with a fluorescent nucleotide by a multiplex polymerase chain reaction using a mixture of specific primer sets for each gene. This labeled target was hybridized with a DNA chip that contained the spots of the specific probe DNAs for each beta-lactam antibiotic-resistance gene. This technique made it possible to detect the specific resistance gene, even in a single bacterium.
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PMID:Development of DNA chip for the simultaneous detection of various beta-lactam antibiotic-resistant genes. 1244 90

Enterobacteria produce elementary chromosomal enzymes, Beta-lactamases of class A: TEM and SHV (Escherichia coli, Klebsiella pneumoniae). These can give rise to plasmid-coded broad-spectrum Beta-lactamases (ESBL) discovered in 1980 (E. coli, K. pneumoniae, Enterobacter cloacae). The first cefotaximase (CTX-M, MEN-1) was reported in Europe in 1990. This enzyme is far more active against cefotaxime than against ceftazidime and aztreonam. Chromosomal hyperpoduction of K1 Beta-lactamase differs from all other ESBLs due its sensitivity to ceftazidime (Klebsiella oxytoca). However, not all enterobacteria are resistant only because of ESBLs, but also as a result of the action of chromosomally or plasmid coded AmpC Beta-lactamase of class C (MIR-1, CMY-1, BIL-1, FOX-1, MOX-1, DHA-1, ACC-1), resistant to Beta-lactamase inhibitors and to cefoxitin (Enterobacter spp., Proteus vulgaris, Citrobacter freundii, Morganelle spp., Serratia spp.). With the loss of outside-membrane porins (OMP) they can become resistant to carbapenem an tibiotics. The 100% resistance of enterobacteria to carbapenems that so far exists in this country is elsewhere in the world compromised by the incidence of carbapenem-hydrolysing plasmid-determined Beta-lactamase of class B (IMP-1, VIM-1) and of class A (KPC-1) in K. pneumoniae, (SME-1) in Serratia marcescens and (IMI-1, NMC-A) in E. clocae. Carbapenemases in enterobacteria are only effective in the presence of impermeability and other resistance mechanisms.
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PMID:[Development of Beta-lactamase resistance in enterobacteria]. 1705 71

Adsorption/desorption in a new Zn(II)-TiO2 adsorption system was investigated at different particle concentrations (Cp). TEM, SEM and XRD analyses revealed that the TiO2 particles were an aggregation of nano-sized (approximately 10 nm) pure anatase-type TiO2. Adsorption experiments were carried out with particle concentrations of 100, 400 and 1000 mg/L, and their adsorption isotherms were found to decline successively, showing an obvious Cp effect. Desorption experiments indicated that adsorption in this system was irreversible, and the irreversibility increased with increasing Cp. These phenomena could be explained by the MEA (metastable equilibrium adsorption) theory and the Cp effect could be modeled well with an MEA-Freundlich-type Cp effect isotherm equation. This study may help understand environmental behavior of contaminants on ultrafine natural particles.
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PMID:Particle concentration effect in adsorption/desorption of Zn(II) on anatase type nano TiO2. 1827 47


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