Browse
Submit Data
Databases
API
Help

Dataset Information

0 Views

0 Connections

0 Citations

0 Reanalyses

0 Downloads

Omics score: 0

TEM-28 from an Escherichia coli clinical isolate is a member of the His-164 family of TEM-1 extended-spectrum beta-lactamases.

ABSTRACT: TEM-28 (pI 6.1), expressed by an Escherichia coli clinical isolate, is a novel beta-lactamase which hydrolyzed ceftazidime, cefotaxime, and aztreonam with rates of 25, 1.1, and 5.6, respectively, relative to that for benzylpenicillin (100). The nucleotide sequence of blaTEM-28 differed from that of blaTEM-1 by two base changes, resulting in amino acid substitutions of Arg-164 to His and Glu-240 to Lys.

SUBMITTER: Bradford PA

PROVIDER: S-EPMC163097 | biostudies-other | 1996 Jan

REPOSITORIES: biostudies-other

ACCESS DATA

Json Xml

Publications

TEM-28 from an Escherichia coli clinical isolate is a member of the His-164 family of TEM-1 extended-spectrum beta-lactamases.

Bradford P A PA Jacobus N V NV Bhachech N N Bush K K

Antimicrobial agents and chemotherapy 19960101 1

TEM-28 (pI 6.1), expressed by an Escherichia coli clinical isolate, is a novel beta-lactamase which hydrolyzed ceftazidime, cefotaxime, and aztreonam with rates of 25, 1.1, and 5.6, respectively, relative to that for benzylpenicillin (100). The nucleotide sequence of blaTEM-28 differed from that of blaTEM-1 by two base changes, resulting in amino acid substitutions of Arg-164 to His and Glu-240 to Lys. ...[more]

PMID: 8787920

Similar Datasets

TEM-158 (CMT-9), a new member of the CMT-type extended-spectrum beta-lactamases.

Project description:TEM-158 was found to include the substitutions previously observed for TEM-12 and TEM-35. This enzyme presented hydrolytic activity against ceftazidime and a high level of resistance against clavulanate, which can alter its detection. Its discovery highlights the need for accurate detection methods.

| S-EPMC2151416 | biostudies-literature

Evolution of TEM-related extended-spectrum beta-lactamases in Korea.

Project description:TEM-52, differing from TEM-1 by having the substitutions Glu-104-->Lys, Met-182-->Thr, and Gly-238-->Ser, has previously been described as the most prevalent extended-spectrum beta-lactamase (ESBL) in Korea. In a further survey, we discovered the ESBLs TEM-15, which is like TEM-52 but lacks the substitution at residue 182, and TEM-88, which is like TEM-52 with an additional Gly-196-->Asp substitution. TEM-88 retained the activity of TEM-52 against moxalactam. Otherwise, the kinetic properties of the three ESBLs failed to show an advantage to this evolution.

| S-EPMC90891 | biostudies-literature

Sequences of the genes for the TEM-20, TEM-21, TEM-22, and TEM-29 extended-spectrum beta-lactamases.

Project description:The sequences of the blaTEM genes encoding TEM-20, TEM-21, TEM-22, and TEM-29 extended-spectrum beta-lactamases were determined. Analysis of the deduced amino acid sequences indicated that TEM-20 and TEM-29 were derived from TEM-1 and that TEM-21 and TEM-22 were derived from TEM-2. The substitutions involved were Ser-238 and Thr-182 for TEM-20; His-164 for TEM-29; Lys-104, Arg-153, and Ser-238 for TEM-21; and Lys-104, Gly-237, and Ser-238 for TEM-22. The promoter region of the blaTEM-22 gene was identical to that of blaTEM-3. High-level production of TEM-20 could result from a 135-bp deletion which combined the -35 region of the Pa promoter with the -10 region of the P3 promoter and a G-->T transition in the latter motif.

| S-EPMC89239 | biostudies-literature

Extended-spectrum beta-lactamases in Ireland, including a novel enzyme, TEM-102.

Project description:Organisms producing extended-spectrum beta-lactamases (ESBLs) have been reported in many countries, but there is no information on the prevalence of ESBL-producing members of the family Enterobacteriaceae in Ireland. A total of 925 isolates of ampicillin-resistant members of the Enterobacteriaceae were received from six hospitals in Ireland over a 3-year period from September 1996 to September 1999. Isolates were screened for ESBL production by the double-disk diffusion (DDD) method. DDD-positive isolates that were (i) confirmed as ESBL producers by National Committee for Clinical Laboratory Standards (NCCLS) confirmatory testing and (ii) susceptible to cefoxitin by disk diffusion were considered ESBL producers. By these criteria, 27 (3%) of the ampicillin-resistant members of the Enterobacteriaceae studied were categorized as ESBL producers. Molecular typing suggested that some intra- and interhospital spread of ESBL-producing isolates had occurred. DNA sequencing of amplified bla(TEM) and bla(SHV) genes resulted in the detection of a novel bla(TEM) ESBL gene, bla(TEM-102) in two isolates (Klebsiella pneumoniae and Enterobacter cloacae) received from the same hospital but isolated from different patients. The study suggests dissemination of ESBL-producing bacteria within the health care system in Ireland and emphasizes the need for measures to control such spread.

| S-EPMC166109 | biostudies-literature

Novel TEM-type extended-spectrum beta-lactamase, TEM-134, in a Citrobacter koseri clinical isolate.

Project description:A new natural TEM derivative with extended-spectrum beta-lactamase activity, TEM-134, was identified in a ceftazidime-resistant clinical isolate of Citrobacter koseri. Compared to TEM-1, TEM-134 contains the following mutations: Q39K, E104K, R164H, and G238S. The bla(TEM-134) gene was not transferable by conjugation and, apparently, was chromosomally encoded. Expression studies with Escherichia coli revealed efficient cefotaximase and ceftazidimase activity for TEM-134.

| S-EPMC1068604 | biostudies-literature

Evolution of TEM-type extended-spectrum beta-lactamases in clinical Enterobacteriaceae strains in Poland.

Project description:Seventeen extended-spectrum beta-lactamase (ESBL)-producing isolates of the family Enterobacteriaceae recovered from 1998 to 2000 in hospitals of five different cities in Poland were analyzed. They expressed several TEM-type ESBLs, TEM-4, TEM-29, TEM-85, TEM-86, TEM-93, and TEM-94. TEM-85 (L21F, R164S, E240K, T265M), TEM-86 (L21F, R164S, A237T, E240K, T265M), TEM-93 (M182T, G238S, E240K), and TEM-94 (L21F, E104K, M182T, G238S, T265M) were identified for the first time. Including the enzymes described earlier, TEM-47, TEM-48, TEM-49, and TEM-68, the group of known ESBLs of the TEM family produced by enterobacteria in Polish hospitals has increased to 10 variants. Comparative sequence analysis of the genes coding for all these beta-lactamases revealed a view of their possible evolution, which, apart from the gradual acquisition of various mutations, could also have involved recombination events. Two different bla(TEM-1) gene alleles were precursors of the ESBL genes: bla(TEM-1A), which was the ancestor of bla(TEM-93), and bla(TEM-1F), from which all the remaining genes originated. The evolution of the bla(TEM-1F)-related genes most probably consisted of three major separate lineages, one of which, including bla(TEM-4), bla(TEM-47), bla(TEM-48), bla(TEM-49), bla(TEM-68), and bla(TEM-94), was highly structured itself and could have been initiated by the bla(TEM-25) gene, identified exclusively in France so far. Plasmid fingerprinting analysis revealed a high degree of diversity of plasmids carrying related bla(TEM) genes, which suggested either the intense diversification or transposition of bla(TEM) genes between different plasmids or some contribution of convergent evolution. The results of this study clearly demonstrate that the environment of Polish hospitals has been highly favorable for the rapid evolution of ESBLs.

| S-EPMC1087658 | biostudies-literature

Multiple global suppressors of protein stability defects facilitate the evolution of extended-spectrum TEM ?-lactamases.

Project description:The introduction of extended-spectrum cephalosporins and ?-lactamase inhibitors has driven the evolution of extended-spectrum ?-lactamases (ESBLs) that possess the ability to hydrolyze these drugs. The evolved TEM ESBLs from clinical isolates of bacteria often contain substitutions that occur in the active site and alter the catalytic properties of the enzyme to provide an increased hydrolysis of extended-spectrum cephalosporins or an increased resistance to inhibitors. These active-site substitutions often result in a cost in the form of reduced enzyme stability. The evolution of TEM ESBLs is facilitated by mutations that act as global suppressors of protein stability defects in that they allow the enzyme to absorb multiple amino acid changes despite incremental losses in stability associated with the substitutions. The best-studied example is the M182T substitution, which corrects protein stability defects and is commonly found in TEM ESBLs or inhibitor-resistant variants from clinical isolates. In this study, a genetic selection for second-site mutations that could partially restore function to a severely destabilized primary mutant enabled the identification of A184V, T265M, R275Q, and N276D, which are known to occur in TEM ESBLs from clinical isolates, as suppressors of TEM-1 protein stability defects. Further characterization demonstrated that these substitutions increased the thermal stability of TEM-1 and were able to correct the stability defects of two different sets of destabilizing mutations. The acquisition of compensatory global suppressors of stability costs associated with active-site mutations may be a common mechanism for the evolution of novel protein function.

| S-EPMC3032993 | biostudies-literature

The Prevalence of TEM and SHV Genes among Extended-Spectrum Beta-Lactamases Producing Escherichia Coli and Klebsiella Pneumoniae.

Project description:ObjectivesProduction of extended-spectrum beta-lactamases (ESBLs) by enteric bacteria continues to be a major problem in hospitals and community. ESBLs producing bacteria cause many serious infections including urinary tract infections, peritonitis, cholangitis and intra-abdominal abscess. The aim of this study was to determine the prevalence of ESBLs producing Escherichia coli and Klebsiella pneumoniae bacteria isolated from clinical samples of patients attending Imam Reza and Ghaem University Hospitals, Mashhad, Northeast of Iran.Materials and methodsDuring 2009 and 2010, 82 strains of E. coli and 78 strains of K. pneumoniae were isolated from out-patients and hospitalized patients and they were examined by Oxoid combination disk test and PCR methods.ResultsWe found that 43.9% of E. coli and 56.1% of K. pneumoniae produced ESBLs. The frequency of SHV and TEM among the ESBLs producing isolates were 14.4% and 20.6%, respectively. Ratios of ESBLs positive isolates from out-patients to hospitalized patients were 24/33.ConclusionThis study shows that the prevalence of ESBLs producing E. coli and K. pneumoniae is high in both study groups (out-patients and hospitalized patients). Therefore it seems that continuous surveillance is essential to monitor the ESBLs producing microorganisms in hospitals and community.

| S-EPMC3586863 | biostudies-literature

Biochemical characterization of the TEM-107 extended-spectrum ?-lactamase in a Klebsiella pneumoniae isolate from South Korea.

Project description:The TEM-107 extended-spectrum ?-lactamase detected in a Klebsiella pneumoniae clinical isolate had a Gly238Ser substitution compared to the TEM-43 ?-lactamase. The MIC of ceftazidime was higher (64 ?g/ml) than that of cefotaxime (2 ?g/ml) for the isolate. Clavulanic acid reduced the MIC of ceftazidime 64-fold.

| S-EPMC3232759 | biostudies-literature

TEM-71, a novel plasmid-encoded, extended-spectrum beta-lactamase produced by a clinical isolate of Klebsiella pneumoniae.

Project description:TEM-71, a novel extended-spectrum beta-lactamase from a Klebsiella pneumoniae clinical isolate, had an isoelectric point of 6.0 and a substrate profile showing preferential hydrolysis of cefotaxime over ceftazidime. It differed from TEM-1 by two substitutions, Gly238Ser and Glu240Lys, and was under the control of the strong P4 promoter.

| S-EPMC127224 | biostudies-literature

OmicsDI is part of the ELIXIR infrastructure

OmicsDI is an Elixir interoperability service. Learn more ›

Tweets

OmicsDI Databases

PRIDE
PeptideAtlas
MassIVE
JPOST Repository
Physiome Model Repository

EGA
EVA
ENA
LINCS
PAXDB
Cell Collective

MetaboLights
Metabolomics Workbench
MetabolomeExpress
GNPS
BioModels
FAIRDOMHub

ArrayExpress
dbGaP
ExpressionAtlas
GEO
NODE

Information

Databases
Help
API
Contact us
Code on GitHub
Terms of use
Submit Data