Target intelligence / Profile preview

TEM-1 beta-lactamase (TEM-1)

Target
TEM-1
Molecular classification
Enzyme, Beta-lactamase, Hydrolase, Serine beta-lactamase (Class A)
01

Overview

TEM-1 beta-lactamase is a **Class A serine hydrolase enzyme** produced primarily by Gram-negative bacteria such as *Escherichia coli* and *Klebsiella pneumoniae* that acts by hydrolyzing the beta-lactam ring of penicillin and early cephalosporin antibiotics, conferring bacterial resistance. Discovered in 1963, it is the most common beta-lactamase responsible for ampicillin resistance in *E. coli* and is widely distributed among Enterobacteriaceae and other pathogens. Over 170 variants of TEM-1 have evolved, expanding resistance to additional antibiotics (extended-spectrum beta-lactamases, ESBLs) through amino acid substitutions mostly around the active site loop, though original TEM-1 remains highly efficient against penicillins but less so against third-generation cephalosporins. Remediation of TEM-1-mediated resistance involves the clinical use of beta-lactamase inhibitors (such as clavulanic acid), though continued mutation poses a challenge to therapy.

Other names
TEM-1TEM beta-lactamaseBeta-lactamase TEM-1Class A beta-lactamase
02

Mechanism of action

Enzymatic hydrolysis of the beta-lactam ring in antibiotics, rendering them inactive

03

Biological functions

Hydrolysis of beta-lactam antibioticsAntibiotic resistance
04

Disease associations

InfectionAntimicrobial resistance
05

Safety considerations

Rapid dissemination of resistance among Gram-negative pathogensCompromised efficacy of many first- and second-line antibiotics
06

Interacting drugs

Penicillins (e.g., ampicillin)

3 more in the full profile.

07

Biomarkers

Presence of TEM-1 gene or protein as a marker for resistance to penicillins and some cephalosporins in bacterial isolates

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