What is the molecular classification of carbapenemase enzymes according to the Bush/Jacoby classification?

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From the Guidelines

Carbapenemase enzymes are primarily classified into three main molecular classes: Class A, Class B, and Class D, according to the Ambler classification system, which is crucial for guiding antibiotic therapy. The main classes of carbapenemases include:

  • Class A: KPC (Klebsiella pneumoniae carbapenemase) 1
  • Class B: metallo-β-lactamases (MBLs), such as NDM, VIM, and IMP 1
  • Class D: OXA-48-like β-lactamases 1 Understanding the molecular mechanism responsible for the carbapenem-resistant phenotype is essential because each class of enzymes confers variable susceptibility profiles that require different treatment strategies 1. Rapid testing strategies to identify specific carbapenemases are strongly recommended to guide antibiotic therapy and improve patient outcomes 1. The ability to hydrolyse all classes of β-lactams, except monobactams (aztreonam), and the inability of classic serine β-lactamase inhibitors to inhibit MBLs, make them particularly worrisome 1. Key considerations in the treatment of infections caused by carbapenemase-producing Enterobacteriaceae include the use of newer beta-lactam/beta-lactamase inhibitor combinations, such as ceftazidime-avibactam, which are active against Class A and some Class D carbapenemases, but not against Class B metallo-beta-lactamases 1.

From the Research

Molecular Classification of Carbapenemase Enzymes

The molecular classification of carbapenemase enzymes is based on their amino acid sequence and divides them into four classes: A, B, C, and D.

  • Class A carbapenemases are serine-based enzymes that hydrolyze penicillins, cephalosporins, monobactams, and carbapenems, and are inhibited by clavulanate and tazobactam 2, 3.
  • Class B carbapenemases are metallo-beta-lactamases that contain zinc in the active site and hydrolyze all beta-lactams except aztreonam 2, 4.
  • Class D carbapenemases are serine-based enzymes that hydrolyze penicillins, cephalosporins, and carbapenems, and are often detected in Acinetobacter baumannii 2, 4.

Bush/Jacoby Classification

The Bush/Jacoby classification system is a functional classification scheme that groups beta-lactamases based on their substrate and inhibitor profiles 5.

  • Group 1 includes class C cephalosporinases.
  • Group 2 includes classes A and D broad-spectrum, inhibitor-resistant, and extended-spectrum beta-lactamases and serine carbapenemases, which are divided into four phenotypically different groups: 2br, 2be, 2e, and 2f 3.
  • Group 3 includes metallo-beta-lactamases, which belong to class B.

Carbapenemase Enzymes

Carbapenemase enzymes are beta-lactamases that hydrolyze carbapenems, which are often used as last-resort antibiotics to treat serious infections 2, 6, 4.

  • The emergence of carbapenemase-producing bacteria has limited the options for treatment and poses a significant threat to public health 6.
  • The horizontal transfer of resistant determinants through mobile genetic elements has increased the incidence of multidrug-resistant bacteria 6.

References

Guideline

Guideline Directed Topic Overview

Dr.Oracle Medical Advisory Board & Editors, 2025

Research

Class A carbapenemases.

The Journal of antimicrobial chemotherapy, 2007

Research

Carbapenemases: the versatile beta-lactamases.

Clinical microbiology reviews, 2007

Research

Updated functional classification of beta-lactamases.

Antimicrobial agents and chemotherapy, 2010

Professional Medical Disclaimer

This information is intended for healthcare professionals. Any medical decision-making should rely on clinical judgment and independently verified information. The content provided herein does not replace professional discretion and should be considered supplementary to established clinical guidelines. Healthcare providers should verify all information against primary literature and current practice standards before application in patient care. Dr.Oracle assumes no liability for clinical decisions based on this content.

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