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Chapter 7 : β-Lactams, Penicillin-Binding Proteins, and β-Lactamases
Author:
Oreste A. Mascaretti1
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Affiliations:
1: Department of Organic Chemistry, Faculty of Biochemistry and Pharmacy, Universidad Nacional de Rosario, Rosario, Argentina
Content Type: Textbook
Publication Year:
2003
Category: Bacterial Pathogenesis
Book DOI:
10.1128/9781555817794
Chapter DOI:
10.1128/9781555817794.ch7
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Abstract:
Several properties shared by some of the β-lactam antibiotics are spectral characteristics of the β-lactam group; however, in other cases the properties are very different, and it is difficult to give a clear picture of properties of the individual members and how they differ from each other. Penicillin-binding protein (PBPs) are a group of bacterial membrane-bound enzymes whose active sites are available in the periplasmic space. The production of β-lactamases is considered to be the most common mechanism of bacterial resistance to β-lactam antibiotics. According to Ambler, β-lactamases are also grouped into four molecular classes based on their primary sequence homology. Serine β-lactamases differ from serine DD-transpeptidases in that they catalyze the deacylation step very efficiently only with β-lactams that have an aromatic (planar) substituent joined to the secondary amide side chain. The amino acid alignments reveal several conserved boxes that consist of strict identities or homologous amino acids. The significance of the homologies and differences is highlighted by the recent results of X-ray crystallography and site-directed mutagenesis experiments that have demonstrated the three-dimensional structural similarities between representatives of β-lactamases enzymes. Structural studies suggested that the conserved residue Tyr150 is the catalytic base that activates the hydrolytic water for its attack on the acyl intermediate.
Citation:
Mascaretti O.
2003.
β-Lactams, Penicillin-Binding Proteins, and β-Lactamases,
p 107-128.
In
Bacteria versus Antibacterial Agents.
ASM Press, Washington, DC.
doi: 10.1128/9781555817794.ch7
Figures
β-Lactams, Penicillin-Binding Proteins, and β-Lactamases
Citation:
Mascaretti O.
2003.
β-Lactams, Penicillin-Binding Proteins, and β-Lactamases,
p 107-128.
In
Bacteria versus Antibacterial Agents.
ASM Press, Washington, DC.
doi: 10.1128/9781555817794.ch7
/content/10.1128/9781555817794.chap7.fig7-1
Figure 7.1
Structures of representative classical and nonclassical β-lactam antibiotics.
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10.1128/9781555817794/fig7-1.gif
Figure 7.1
Structures of representative classical and nonclassical β-lactam antibiotics.
Citation:
Mascaretti O.
2003.
β-Lactams, Penicillin-Binding Proteins, and β-Lactamases,
p 107-128.
In
Bacteria versus Antibacterial Agents.
ASM Press, Washington, DC.
doi: 10.1128/9781555817794.ch7
/content/10.1128/9781555817794.chap7.fig7-2
Figure 7.2
Basic skeleton and nomenclature systems of penicillins.
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10.1128/9781555817794/fig7-2.gif
Figure 7.2
Basic skeleton and nomenclature systems of penicillins.
Citation:
Mascaretti O.
2003.
β-Lactams, Penicillin-Binding Proteins, and β-Lactamases,
p 107-128.
In
Bacteria versus Antibacterial Agents.
ASM Press, Washington, DC.
doi: 10.1128/9781555817794.ch7
/content/10.1128/9781555817794.chap7.fig7-3
Figure 7.3
Conformation of the sodium salt of benzylpenicillin in the solid state. R is –NHCOCH2C6H5. The absolute configuration of chiral centers and the α and β positions below or above the plane are shown.
10.1128/9781555817794/fig7-3_thmb.gif
10.1128/9781555817794/fig7-3.gif
Figure 7.3
Conformation of the sodium salt of benzylpenicillin in the solid state. R is –NHCOCH2C6H5. The absolute configuration of chiral centers and the α and β positions below or above the plane are shown.
Citation:
Mascaretti O.
2003.
β-Lactams, Penicillin-Binding Proteins, and β-Lactamases,
p 107-128.
In
Bacteria versus Antibacterial Agents.
ASM Press, Washington, DC.
doi: 10.1128/9781555817794.ch7
/content/10.1128/9781555817794.chap7.fig7-4
Figure 7.4
Chemical structure of 6-β-aminopenicillanic acid in its nonionized and zwitterionic forms.
10.1128/9781555817794/fig7-4_thmb.gif
10.1128/9781555817794/fig7-4.gif
Figure 7.4
Chemical structure of 6-β-aminopenicillanic acid in its nonionized and zwitterionic forms.
Citation:
Mascaretti O.
2003.
β-Lactams, Penicillin-Binding Proteins, and β-Lactamases,
p 107-128.
In
Bacteria versus Antibacterial Agents.
ASM Press, Washington, DC.
doi: 10.1128/9781555817794.ch7
/content/10.1128/9781555817794.chap7.fig7-5
FIGURE 7.5
(a to c) Basic skeleton of cephalosporins and cephamycins (a), carbapenems (b), and clavulanic acid (c). (d and e) Chemical structures of cephalosporanic acid (d) and desacetylcephalosporanic acid (e).
10.1128/9781555817794/fig7-5_thmb.gif
10.1128/9781555817794/fig7-5.gif
FIGURE 7.5
(a to c) Basic skeleton of cephalosporins and cephamycins (a), carbapenems (b), and clavulanic acid (c). (d and e) Chemical structures of cephalosporanic acid (d) and desacetylcephalosporanic acid (e).
Citation:
Mascaretti O.
2003.
β-Lactams, Penicillin-Binding Proteins, and β-Lactamases,
p 107-128.
In
Bacteria versus Antibacterial Agents.
ASM Press, Washington, DC.
doi: 10.1128/9781555817794.ch7
/content/10.1128/9781555817794.chap7.fig7-6
FIGURE 7.6
Resonance in secondary amides, unstrained monocyclic β-lactams, and strained β-lactams.
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10.1128/9781555817794/fig7-6.gif
FIGURE 7.6
Resonance in secondary amides, unstrained monocyclic β-lactams, and strained β-lactams.
Citation:
Mascaretti O.
2003.
β-Lactams, Penicillin-Binding Proteins, and β-Lactamases,
p 107-128.
In
Bacteria versus Antibacterial Agents.
ASM Press, Washington, DC.
doi: 10.1128/9781555817794.ch7
/content/10.1128/9781555817794.chap7.fig7-7
FIGURE 7.7
Hydrogen atoms in penicillins and cephalosporins and coupling signals in the 1H NMR spectra.
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10.1128/9781555817794/fig7-7.gif
FIGURE 7.7
Hydrogen atoms in penicillins and cephalosporins and coupling signals in the 1H NMR spectra.
Citation:
Mascaretti O.
2003.
β-Lactams, Penicillin-Binding Proteins, and β-Lactamases,
p 107-128.
In
Bacteria versus Antibacterial Agents.
ASM Press, Washington, DC.
doi: 10.1128/9781555817794.ch7
/content/10.1128/9781555817794.chap7.fig7-8
FIGURE 7.8
Penicillanic acid derivative structure showing some positions where chemical transformations are made. Chemical mapping of the different positions and orientation of the molecule is very useful for structure-activity relationships.
10.1128/9781555817794/fig7-8_thmb.gif
10.1128/9781555817794/fig7-8.gif
FIGURE 7.8
Penicillanic acid derivative structure showing some positions where chemical transformations are made. Chemical mapping of the different positions and orientation of the molecule is very useful for structure-activity relationships.
Citation:
Mascaretti O.
2003.
β-Lactams, Penicillin-Binding Proteins, and β-Lactamases,
p 107-128.
In
Bacteria versus Antibacterial Agents.
ASM Press, Washington, DC.
doi: 10.1128/9781555817794.ch7
/content/10.1128/9781555817794.chap7.fig7-9
FIGURE 7.9
Carboxypeptidase and transpeptidase reactions (pathways I and II). These reactions are catalyzed by bacterial PBPs. Pathway III shows the action of a penicillin. The penicilloyl-transpeptidase is more stable than the acyl-d-alanyl-transpeptidase, and consequently the transfer of the acyl group to an amino group does not take place (pathway III).
10.1128/9781555817794/fig7-9_thmb.gif
10.1128/9781555817794/fig7-9.gif
FIGURE 7.9
Carboxypeptidase and transpeptidase reactions (pathways I and II). These reactions are catalyzed by bacterial PBPs. Pathway III shows the action of a penicillin. The penicilloyl-transpeptidase is more stable than the acyl-d-alanyl-transpeptidase, and consequently the transfer of the acyl group to an amino group does not take place (pathway III).
Citation:
Mascaretti O.
2003.
β-Lactams, Penicillin-Binding Proteins, and β-Lactamases,
p 107-128.
In
Bacteria versus Antibacterial Agents.
ASM Press, Washington, DC.
doi: 10.1128/9781555817794.ch7
/content/10.1128/9781555817794.chap7.fig7-10
FIGURE 7.10
Dreiding stereomodels of penicillin and of the acyl-d-alanyl-d-alanine end of the nascent peptidoglycan. Arrows indicate the position of the OC—N bond in the β-lactam ring of the penicillin and of the OC—N peptide bond joining the two d-alanine residues. Reprinted from D. J. Tipper and J. L. Strominger, Proc. Natl. Acad. Sci. USA 54:1133, 1965, with permission from the publisher.
10.1128/9781555817794/fig7-10_thmb.gif
10.1128/9781555817794/fig7-10.gif
FIGURE 7.10
Dreiding stereomodels of penicillin and of the acyl-d-alanyl-d-alanine end of the nascent peptidoglycan. Arrows indicate the position of the OC—N bond in the β-lactam ring of the penicillin and of the OC—N peptide bond joining the two d-alanine residues. Reprinted from D. J. Tipper and J. L. Strominger, Proc. Natl. Acad. Sci. USA 54:1133, 1965, with permission from the publisher.
Citation:
Mascaretti O.
2003.
β-Lactams, Penicillin-Binding Proteins, and β-Lactamases,
p 107-128.
In
Bacteria versus Antibacterial Agents.
ASM Press, Washington, DC.
doi: 10.1128/9781555817794.ch7
/content/10.1128/9781555817794.chap7.fig7-11
FIGURE 7.11
Opening of the β-lactam ring by catalysis with a β-lactamase enzyme.
10.1128/9781555817794/fig7-11_thmb.gif
10.1128/9781555817794/fig7-11.gif
FIGURE 7.11
Opening of the β-lactam ring by catalysis with a β-lactamase enzyme.
Citation:
Mascaretti O.
2003.
β-Lactams, Penicillin-Binding Proteins, and β-Lactamases,
p 107-128.
In
Bacteria versus Antibacterial Agents.
ASM Press, Washington, DC.
doi: 10.1128/9781555817794.ch7
/content/10.1128/9781555817794.chap7.fig7-12
FIGURE 7.12
Inactivation of penicillin by active-site serine β-lactamases.
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10.1128/9781555817794/fig7-12.gif
FIGURE 7.12
Inactivation of penicillin by active-site serine β-lactamases.
Citation:
Mascaretti O.
2003.
β-Lactams, Penicillin-Binding Proteins, and β-Lactamases,
p 107-128.
In
Bacteria versus Antibacterial Agents.
ASM Press, Washington, DC.
doi: 10.1128/9781555817794.ch7
/content/10.1128/9781555817794.chap7.fig7-13
FIGURE 7.13
The penicillin-interactive, serine-active-site PBPs and β-lactamases. Enz, enzyme; C, antibiotic; Enz-C, noncovalent Michaelis complex; Enz-C*, covalent acyl-enzyme; P, inactive degradation product(s) of the antibiotic.
10.1128/9781555817794/fig7-13_thmb.gif
10.1128/9781555817794/fig7-13.gif
FIGURE 7.13
The penicillin-interactive, serine-active-site PBPs and β-lactamases. Enz, enzyme; C, antibiotic; Enz-C, noncovalent Michaelis complex; Enz-C*, covalent acyl-enzyme; P, inactive degradation product(s) of the antibiotic.
Citation:
Mascaretti O.
2003.
β-Lactams, Penicillin-Binding Proteins, and β-Lactamases,
p 107-128.
In
Bacteria versus Antibacterial Agents.
ASM Press, Washington, DC.
doi: 10.1128/9781555817794.ch7
/content/10.1128/9781555817794.chap7.fig7-14
FIGURE 7.14
Schematic drawing of a possible catalytic mechanism for class A β-lactamases. Through an electrostatic interaction between the ammonium group of Lys234 and the C-3 carboxylate the substrate is recognized by the enzyme in both ground-state binding and transition-state binding. Reprinted from H. Adachi, T. Ohta, and H. Matsuzawa, J. Biol. Chem. 266:3186–3191, 1991, with permission from the publisher.
10.1128/9781555817794/fig7-14_thmb.gif
10.1128/9781555817794/fig7-14.gif
FIGURE 7.14
Schematic drawing of a possible catalytic mechanism for class A β-lactamases. Through an electrostatic interaction between the ammonium group of Lys234 and the C-3 carboxylate the substrate is recognized by the enzyme in both ground-state binding and transition-state binding. Reprinted from H. Adachi, T. Ohta, and H. Matsuzawa, J. Biol. Chem. 266:3186–3191, 1991, with permission from the publisher.
Citation:
Mascaretti O.
2003.
β-Lactams, Penicillin-Binding Proteins, and β-Lactamases,
p 107-128.
In
Bacteria versus Antibacterial Agents.
ASM Press, Washington, DC.
doi: 10.1128/9781555817794.ch7
/content/10.1128/9781555817794.chap7.fig7-15
FIGURE 7.15
Simplified mechanism of β-lactam hydrolysis by group C β-lactamases. Enz, enzyme.
10.1128/9781555817794/fig7-15_thmb.gif
10.1128/9781555817794/fig7-15.gif
FIGURE 7.15
Simplified mechanism of β-lactam hydrolysis by group C β-lactamases. Enz, enzyme.
Citation:
Mascaretti O.
2003.
β-Lactams, Penicillin-Binding Proteins, and β-Lactamases,
p 107-128.
In
Bacteria versus Antibacterial Agents.
ASM Press, Washington, DC.
doi: 10.1128/9781555817794.ch7
/content/10.1128/9781555817794.chap7.fig7-16
FIGURE 7.16
Proposed catalytic mechanism of benzylpenicillin hydrolysis by the mononuclear metallo-β-lactamase from B. cereus. H, histidine; Asp, aspartate. Adapted from S. Bounaga, A. P. Laws, M. Galleni, and M. I. Page, Biochem. J. 331:703–711, 1998, with permission from the publisher.
10.1128/9781555817794/fig7-16_thmb.gif
10.1128/9781555817794/fig7-16.gif
FIGURE 7.16
Proposed catalytic mechanism of benzylpenicillin hydrolysis by the mononuclear metallo-β-lactamase from B. cereus. H, histidine; Asp, aspartate. Adapted from S. Bounaga, A. P. Laws, M. Galleni, and M. I. Page, Biochem. J. 331:703–711, 1998, with permission from the publisher.
Citation:
Mascaretti O.
2003.
β-Lactams, Penicillin-Binding Proteins, and β-Lactamases,
p 107-128.
In
Bacteria versus Antibacterial Agents.
ASM Press, Washington, DC.
doi: 10.1128/9781555817794.ch7
/content/10.1128/9781555817794.chap7.fig7-17
FIGURE 7.17
Catalytic mechanism of nitrocefin hydrolysis by the dizinc metallo-β-lactamase from B. fragilis. H, histidine; C, cysteine; Asp, aspartate; Asn, asparaginamide. Adapted from Z. Wang, W. Fast, and S. J. Benkovic, Biochemistry 38:10013–10023, 1999, with permission from the publisher.
10.1128/9781555817794/fig7-17_thmb.gif
10.1128/9781555817794/fig7-17.gif
FIGURE 7.17
Catalytic mechanism of nitrocefin hydrolysis by the dizinc metallo-β-lactamase from B. fragilis. H, histidine; C, cysteine; Asp, aspartate; Asn, asparaginamide. Adapted from Z. Wang, W. Fast, and S. J. Benkovic, Biochemistry 38:10013–10023, 1999, with permission from the publisher.
Citation:
Mascaretti O.
2003.
β-Lactams, Penicillin-Binding Proteins, and β-Lactamases,
p 107-128.
In
Bacteria versus Antibacterial Agents.
ASM Press, Washington, DC.
doi: 10.1128/9781555817794.ch7
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Tables
β-Lactams, Penicillin-Binding Proteins, and β-Lactamases
Citation:
Mascaretti O.
2003.
β-Lactams, Penicillin-Binding Proteins, and β-Lactamases,
p 107-128.
In
Bacteria versus Antibacterial Agents.
ASM Press, Washington, DC.
doi: 10.1128/9781555817794.ch7
/content/10.1128/9781555817794.chap7.tab7-1
Table 7.1
Properties of the PBPs of E. coli K-12 a
Table 7.1
Properties of the PBPs of E. coli K-12 a
Citation:
Mascaretti O.
2003.
β-Lactams, Penicillin-Binding Proteins, and β-Lactamases,
p 107-128.
In
Bacteria versus Antibacterial Agents.
ASM Press, Washington, DC.
doi: 10.1128/9781555817794.ch7
/content/10.1128/9781555817794.chap7.tab7-2
Table 7.2
β-Lactamase classification a
Table 7.2
β-Lactamase classification a
Citation:
Mascaretti O.
2003.
β-Lactams, Penicillin-Binding Proteins, and β-Lactamases,
p 107-128.
In
Bacteria versus Antibacterial Agents.
ASM Press, Washington, DC.
doi: 10.1128/9781555817794.ch7