Specificity Profiles of the Membrane‐Bound γ‐<scp>d</scp>‐Glutamyl‐(<scp>l</scp>)<i>meso</i>‐diaminopimelate Endopeptidase and <scp>ld</scp>‐Carboxypeptidase from <i>Bacillus sphaericus</i> 9602

Arminjon, F.; Guinand, Micheline; Vacheron, Marie‐Jeanne; Michel, Georges

doi:10.1111/j.1432-1033.1977.tb11351.x

Cited by 24 publications

(10 citation statements)

References 11 publications

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“…Though tripeptides are found in many bacteria, very few of the corresponding LD-carboxypeptidases have been identified. Membrane preparations of B. subtilis have shown strong LD-carboxypeptidase activity against cell-wall-derived tetrapeptides (Arminjon et al., 1977), though the specific enzyme involved has not been isolated. The best characterized LD-carboxypeptidase is LD-carboxypeptidase A (LdcA), a cytoplasmic, penicillin-insensitive member of the S66 family of serine peptidases that is involved in PG recycling and is essential for cells entering the stationary phase (Metz et al., 1986; Templin et al., 1999).…”

Section: Introductionmentioning

confidence: 99%

Structure of the LdcB LD-Carboxypeptidase Reveals the Molecular Basis of Peptidoglycan Recognition

et al. 2014

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SummaryPeptidoglycan surrounds the bacterial cytoplasmic membrane to protect the cell against osmolysis. The biosynthesis of peptidoglycan, made of glycan strands crosslinked by short peptides, is the target of antibiotics like β-lactams and glycopeptides. Nascent peptidoglycan contains pentapeptides that are trimmed by carboxypeptidases to tetra- and tripeptides. The well-characterized DD-carboxypeptidases hydrolyze the terminal D-alanine from the stem pentapeptide to produce a tetrapeptide. However, few LD-carboxypeptidases that produce tripeptides have been identified, and nothing is known about substrate specificity in these enzymes. We report biochemical properties and crystal structures of the LD-carboxypeptidases LdcB from Streptococcus pneumoniae, Bacillus anthracis, and Bacillus subtilis. The enzymes are active against bacterial cell wall tetrapeptides and adopt a zinc-carboxypeptidase fold characteristic of the LAS superfamily. We have also solved the structure of S. pneumoniae LdcB with a product mimic, elucidating the residues essential for peptidoglycan recognition and the conformational changes that occur on ligand binding.

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Section: Introductionmentioning

confidence: 99%

Structure of the LdcB LD-Carboxypeptidase Reveals the Molecular Basis of Peptidoglycan Recognition

et al. 2014

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“…Bacillus sphaericus contains a sporulation-related ␥-D-GluDap amidase named ENP1 (2,32). The catalytic domain of ENP1 contains a zinc binding site, suggesting that a zinc ion is essential for its activity (51 (120).…”

Section: Mpaa: ␥-D-glutamyl-meso-diaminopimelate Amidasementioning

confidence: 99%

How Bacteria Consume Their Own Exoskeletons (Turnover and Recycling of Cell Wall Peptidoglycan)

Park

Uehara

2008

Microbiol Mol Biol Rev

385

498

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SUMMARY The phenomenon of peptidoglycan recycling is reviewed. Gram-negative bacteria such as Escherichia coli break down and reuse over 60% of the peptidoglycan of their side wall each generation. Recycling of newly made peptidoglycan during septum synthesis occurs at an even faster rate. Nine enzymes, one permease, and one periplasmic binding protein in E. coli that appear to have as their sole function the recovery of degradation products from peptidoglycan, thereby making them available for the cell to resynthesize more peptidoglycan or to use as an energy source, have been identified. It is shown that all of the amino acids and amino sugars of peptidoglycan are recycled. The discovery and properties of the individual proteins and the pathways involved are presented. In addition, the possible role of various peptidoglycan degradation products in the induction of β-lactamase is discussed.

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“…A sporulation-related enzyme, ENP1 from Bacillus sphaericus NCTC 9602, that cleaves the ␥-D-Glu-Dap amide bond has been reported (1,6,10). It has two domains: a 100-amino-acid N-terminal domain consisting of two tandem LysM motif sequences involved in binding to peptidoglycan, and a 296-amino-acid C-terminal catalytic domain with a zinc binding site.…”

Section: One Such Example N-acetylglucosamine-anhydro-n-acetylmuramymentioning

confidence: 99%

Identification of MpaA, an Amidase in Escherichia coli That Hydrolyzes the γ- d -Glutamyl- meso- Diaminopimelate Bond in Murein Peptides

Uehara

Park

2003

J Bacteriol

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MpaA amidase was identified in Escherichia coli by its amino acid sequence homology with the ENP1 endopeptidase from Bacillus sphaericus. The enzymatic activity of MpaA, i.e., hydrolysis of the ␥-D-glutamyl-diaminopimelic acid bond in the murein tripeptide L-alanyl-␥-D-glutamyl-meso-diaminopimelic acid, was demonstrated in the cell extract of a strain expressing mpaA from a multicopy plasmid. An mpaA mpl (murein peptide ligase) double mutant accumulated large amounts of murein tripeptide in its cytoplasm, consistent with the premise that MpaA degrades the tripeptide if its recycling via the peptidoglycan biosynthetic pathway is blocked.About 40% of Escherichia coli cell wall murein is degraded each generation by lytic transglycosylases and endopeptidases (7,11,18). The resulting anhydro-muropeptides are efficiently recycled (11). One such example,is transported into the cytoplasm via AmpG, a permease specific for muropeptides containing 11). It is rapidly broken down to yield GlcNAc, anhMurNAc, D-Ala, and murein tripeptide (L-Ala-␥-D-Glu-Dap), by NagZ, a ␤-N-acetylglucosamidase (3, 20), AmpD, an anhMurNAc-L-Ala amidase (9, 12), and LdcA, an L,D-carboxypeptidase (19). Murein tripeptide is then ligated to UDPMurNAc by Mpl, a murein peptide ligase (13), and thus free tripeptide reenters the biosynthetic pathway for murein synthesis. The two amino sugars are also recycled for murein and lipopolysaccharide synthesis (15).Over the course of our studies on cell wall recycling, two observations together strongly suggested that significant hydrolysis of murein tripeptide by an amidase must be taking place in the cytoplasm: (i) an mpl mutant accumulates an amount of murein tripeptide that is only a little more than 2-fold that of UDP-MurNAc-pentapeptide (13), while in an ampD deletion mutant, the amount of anhMurNAc-tripeptide present in the cytoplasm is about 40-fold more than the amount of UDPMurNAc-pentapeptide (11); (ii) the amount of the murein dipeptide L-Ala-D-Glu present in the cytoplasm of the mpl mutant is much greater than in the wild type (13). Another indication of the presence of a ␥-D-Glu-Dap amidase activity was the earlier demonstration of small amounts of Dap-D-Ala in the cytoplasm of E. coli (8). We therefore searched for the putative amidase, and here we report the identification of a gene, mpaA, and demonstrate that MpaA cleaves the ␥-D-GluDap amide bond in murein peptides.Homology-based identification of a ␥-D-Glu-Dap amidase in E. coli. A sporulation-related enzyme, ENP1 from Bacillus sphaericus NCTC 9602, that cleaves the ␥-D-Glu-Dap amide bond has been reported (1, 6, 10). It has two domains: a 100-amino-acid N-terminal domain consisting of two tandem LysM motif sequences involved in binding to peptidoglycan, and a 296-amino-acid C-terminal catalytic domain with a zinc binding site. In a search of the E. coli database, regions of the YcjI amino acid sequence displayed significant homology with the catalytic domain of ENP1 although the overall identity between the two sequences was low (13% (Fig. ...

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Specificity Profiles of the Membrane‐Bound γ‐d‐Glutamyl‐(l)meso‐diaminopimelate Endopeptidase and ld‐Carboxypeptidase from Bacillus sphaericus 9602

Cited by 24 publications

References 11 publications

Structure of the LdcB LD-Carboxypeptidase Reveals the Molecular Basis of Peptidoglycan Recognition

Structure of the LdcB LD-Carboxypeptidase Reveals the Molecular Basis of Peptidoglycan Recognition

How Bacteria Consume Their Own Exoskeletons (Turnover and Recycling of Cell Wall Peptidoglycan)

Identification of MpaA, an Amidase in Escherichia coli That Hydrolyzes the γ- d -Glutamyl- meso- Diaminopimelate Bond in Murein Peptides

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