Browse AMR Genes
Explore antimicrobial resistance genes from the literature
Explore antimicrobial resistance genes from the literature
beta-lactamase
Overview
| Protein Change | Nucleotide Change | Mechanism | Organism | Resistance To | Database | Validation Status |
|---|---|---|---|---|---|---|
| G238A | - | conferred the most resistance to penicillins and cephalosporins | Escherichia coli | penicillin|cephalosporins | Reslit | Candidate |
| G238S | - | conferred resistance to penicillins and cephalosporins | Escherichia coli | penicillin|cephalosporinscefotaxime|ceftazidime | Reslit | Candidate |
| G238P | - | demonstrated lower levels of resistance | Escherichia coli | penicillin|cephalosporins | Reslit | Candidate |
| G238C | - | demonstrated lower levels of resistance | Escherichia coli | penicillin|cephalosporins | Reslit | Candidate |
| G238Q | - | demonstrated lower levels of resistance | Escherichia coli | penicillin|cephalosporins | Reslit | Candidate |
| G238D | - | demonstrated lower levels of resistance | Escherichia coli | penicillin|cephalosporins | Reslit | Candidate |
| D104K | - | - | Escherichia coli | cefotaxime|ceftazidime | Reslit | Candidate |
| D104R | - | - | Escherichia coli | cefotaxime|ceftazidime | Reslit | Candidate |
| R164A | - | - | Escherichia coli | ceftazidime | Reslit | Candidate |
| L138P | - | reduced role in penicillin and ampicillin hydrolyzing properties | Escherichia coli, Klebsiella pneumoniae | penicillin|ampicillin | Reslit | Candidate |
| - | - | Klebsiella pneumoniae | ceftazidime|piperacillin tazobactam | Reslit | Candidate |
Amino acid substitutions at Ambler position Gly238 in the SHV-1 beta-lactamase: exploring sequence requirements for resistance to penicillins and cephalosporins.
Mutations at Ambler position Gly238 in SHV-1 beta-lactamase confer resistance to penicillins and cephalosporins.
Role of Asp104 in the SHV beta-lactamase.
Mutations at Ambler position 104 and 238 contribute to resistance
Activity of ceftazidime/avibactam against isogenic strains of Escherichia coli containing KPC and SHV β-lactamases with single amino acid substitutions in the Ω-loop.
Enzymatic analysis of the effect of naturally occurring Leu138Pro mutation identified in SHV β-lactamase on hydrolysis of penicillin and ampicillin.
High-level expression of chromosomally encoded SHV-1 beta-lactamase and an outer membrane protein change confer resistance to ceftazidime and piperacillin-tazobactam in a clinical isolate of Klebsiella pneumoniae.
The A→C change in the second position of the −10 region of the blaSHV-1 promoter leads to reduced β-lactamase expression and lower resistance.