Updated Functional Classification of β-Lactamases
Open accessAbstract
Two classification schemes for β-lactamases are currently in use. The molecular classification is based on the amino acid sequence and divides β-lactamases into class A, C, and D enzymes which utilize serine for β-lactam hydrolysis and class B metalloenzymes which require divalent zinc ions for substrate hydrolysis. The functional classification scheme updated herein is based on the 1995 proposal by Bush et al. (K. Bush, G. A. Jacoby, and A. A. Medeiros, Antimicrob. Agents Chemother. 39:1211-1233, 1995). It takes into account substrate and inhibitor profiles in an attempt to group the enzymes in ways that can be correlated with their phenotype in clinical isolates. Major groupings generally correlate with the more broadly based molecular classification. The updated system includes group 1 (class C) cephalosporinases; group 2 (classes A and D) broad-spectrum, inhibitor-resistant, and extended-spectrum β-lactamases and serine carbapenemases; and group 3 metallo-β-lactamases. Several new subgroups of each of the major groups are described, based on specific attributes of individual enzymes. A list of attributes is also suggested for the description of a new β-lactamase, including the requisite microbiological properties, substrate and inhibitor profiles, and molecular sequence data that provide an adequate characterization for a new β-lactam-hydrolyzing enzyme.
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The Bush-Jacoby classification divides β-lactamases into 4 categories according to their biochemical function, mainly based on substrate specificity.
“On the other hand, the Bush-Jacoby classification divides β-lactamases into 4 categories (each with several subgroups) according to their biochemical function, mainly based on substrate specificity (19, 20).”
From Mechanisms of Antibiotic Resistance (2016) · cites this paper as [20]
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- Authors
- Bush, K., & Jacoby, G. A.
- Affiliations
- Indiana University Bloomington (US)
- Lahey Hospital and Medical Center (US)
- Corresponding author
- Bush, Karen
- Venue
- Antimicrobial Agents and Chemotherapy
- Publisher
- American Society for Microbiology
- Published
- 2010-03
- Volume
- 54
- Issue
- 3
- Pages
- 969-976
- ISSN
- 0066-4804 (ISSN-L)
- 1098-6596
- PMC
- PMC2825993
- OpenAlex
- W2152127318
- Cited by
- 2,367
- References
- 73
- Citations by year
- 2026: 141 · 2025: 159 · 2024: 168 · 2023: 149 · 2022: 196 · 2021: 184 · 2020: 190 · 2019: 208 · 2018: 169 · 2017: 156 · 2016: 126 · 2015: 123 · 2014: 110 · 2013: 99 · 2012: 68
- FWCI
- 3.13
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Antimicrobial Agents and Chemotherapy (publishedVersion, public-domain)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Medicine › Antibiotic Resistance in Bacteria
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Clinical Biochemistry › Bacterial Identification and Susceptibility Testing
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Biotechnology › Enzyme Production and Characterization
- Keywords
- beta-lactamase, functional classification, molecular classification, class A beta-lactamase, class C beta-lactamase, class D beta-lactamase, metallo-beta-lactamase, serine carbapenemases, extended-spectrum beta-lactamase, inhibitor resistance, cephalosporinase, clinical isolates
- MeSH terms
- Anti-Bacterial Agents, beta-Lactamases, Gram-Negative Bacteria, Humans, Drug Resistance, Bacterial, beta-Lactams
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