Generic enzyme-class and ring-context orientation for beta-lactamase. This reconstruction does not identify an enzyme subclass, antibiotic, resistance gene, bacterial species, susceptibility result, or treatment outcome.
Scientific media record2 verified identifiers
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- Beta-lactamasebiological-process
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- WikiBiome:beta-lactamaseEC:3.5.2.6
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- Editorial review completeIdentifiers authority-verified · Accessibility validated · · beta-lactamase|beta-lactamase-mechanism-v2.webp
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- Trained-algorithmic mediaCreated with a trained generative algorithm and reviewed by WikiBiome for subject identity, scientific framing, identifiers, provenance, and accessibility.
- Scientific basis
- Beta-lactamase — EC 3.5.2.6EC 3.5.2.6 reactionsBeta-Lactamase
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- CC BY-SA 4.0Created
Beta-lactamases are bacterial enzymes that hydrolyze the beta-lactam ring of penicillins, cephalosporins, and carbapenems, rendering them inactive. They are the most common mechanism of antibiotic resistance and a central concern in the Antimicrobial Resistance crisis. Extended-spectrum beta-lactamases (ESBLs) and carbapenemases (KPC, NDM, OXA-48) confer resistance to last-resort antibiotics.
Evidence map1 cited passagesInspect provenance +
Beta-lactamase genes frequently co-locate with metal resistance genes on the same plasmids and mobile genetic elements—meaning environmental metal exposure selects for beta-lactamase-producing bacteria without antibiotic exposure. This is documented in CKD gut microbiome.
Co-Selection with Metal Resistance#
Beta-lactamase genes frequently co-locate with metal resistance genes on the same plasmids and mobile genetic elements—meaning environmental metal exposure selects for beta-lactamase-producing bacteria without antibiotic exposure.[1]Baker-Austin 2006 — Co-selection of Antibiotic and Metal ResistanceBaker-Austin C, Wright MS, Stepanauskas R et al. · 2006Open reference 1 ↓[2]Understanding the Development of Environmental Resistance Among Microbes: A ReviewSrivastava J, Chandra H, Singh N et al. · 2016Open reference 2 ↓
This is documented in CKD Gut Microbiome.[3]Miranda 2022 — Characterization of Metal(loid)s and Antibiotic Resistance in Bacteria of Human Gut Microbiota from CKD SubjectsMaría V. Miranda, Fernanda C. González, Osvaldo S. Paredes-Godoy et al. · 2022Open reference 3 ↓
WikiBiome Relevance#
The beta-lactamase → Co-Selection → metal resistance connection is a core WikiBiome insight: heavy metal pollution in agriculture, water, and food is an unrecognized driver of antibiotic resistance in the human gut microbiome.
Cross-References#
- Antimicrobial Resistance—AMR context
- Co-Selection—metal-antibiotic co-resistance on shared plasmids
- Cephalosporins—beta-lactam antibiotic class
- Vancomycin—alternative when beta-lactams fail
- Klebsiella—major carbapenemase-producing genus
References 3
Numbered by first appearance in the article, then reconciled with its declared source list.
- 1
Baker-Austin C, Wright MS, Stepanauskas R et al. (2006). Baker-Austin 2006 — Co-selection of Antibiotic and Metal Resistance. Trends in Microbiology.
- 2
Srivastava J, Chandra H, Singh N et al. (2016). Understanding the Development of Environmental Resistance Among Microbes: A Review. Clean - Soil, Air, Water.
- 3
María V. Miranda, Fernanda C. González, Osvaldo S. Paredes-Godoy et al. (2022). Miranda 2022 — Characterization of Metal(loid)s and Antibiotic Resistance in Bacteria of Human Gut Microbiota from CKD Subjects. Biological Research.
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Created “Beta-Lactamase”: Beta-lactamases are bacterial enzymes that hydrolyze the beta-lactam ring of penicillins, cephalosporins, and carbapenems, rendering them inactive. They are the most common mechanism of antibiotic…
Created “Beta-Lactamase”: Beta-lactamases are bacterial enzymes that hydrolyze the beta-lactam ring of penicillins, cephalosporins, and carbapenems, rendering them inactive. They are the most common mechanism of antibiotic… Published sections: Beta-Lactamase; Co-Selection with Metal Resistance; WikiBiome Relevance; Cross-References. · WikiBiome Deploy Bot · +36 −0
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