Treatment of peptidoglycan monomer with aqueous ammonia: Formation of lactoylpeptide and a saturated disaccharide

Klaić, Branimir

doi:10.1016/0008-6215(85)85223-x

Cited by 5 publications

(3 citation statements)

References 22 publications

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“…Preparation of Lactoyl Peptides-The ether link internal to MurNAc was cleaved under alkaline conditions (23) to produce lactoyl peptide peptidoglycan fragments. To the solution of unreduced disaccharide peptides (200 l), 32% ammonium hydroxide (64 l) was added, and the mixture was incubated for 5 h at 37°C.…”

Section: Methodsmentioning

confidence: 99%

Synthesis of Mosaic Peptidoglycan Cross-bridges by Hybrid Peptidoglycan Assembly Pathways in Gram-positive Bacteria

Arbeloa

Hugonnet

Sentilhes

et al. 2004

Journal of Biological Chemistry

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The peptidoglycan cross-bridges of Staphylococcus aureus, Enterococcus faecalis, and Enterococcus faecium consist of the sequences Gly 5 , L-Ala 2 , and D-Asx, respectively. Expression of the fmhB, femA, and femB genes of S. aureus in E. faecalis led to the production of peptidoglycan precursors substituted by mosaic side chains that were efficiently used by the penicillin-binding proteins for cross-bridge formation. The Fem transferases were specific for incorporation of glycyl residues at defined positions of the side chains in the absence of any additional S. aureus factors such as tRNAs used for amino acid activation. The PBPs of E. faecalis displayed a broad substrate specificity because mosaic side chains containing from 1 to 5 residues and Gly instead of L-Ala at the N-terminal position were used for peptidoglycan cross-linking. Low affinity PBP2a of S. aureus conferred ␤-lactam resistance in E. faecalis and E. faecium, thereby indicating that there was no barrier to heterospecific expression of resistance caused by variations in the structure of peptidoglycan precursors. Thus, conservation of the structure of the peptidoglycan cross-bridges in members of the same species reflects the high specificity of the enzymes for side chain synthesis, although this is not essential for the activity of the PBPs.

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Section: Methodsmentioning

confidence: 99%

Synthesis of Mosaic Peptidoglycan Cross-bridges by Hybrid Peptidoglycan Assembly Pathways in Gram-positive Bacteria

Arbeloa

Hugonnet

Sentilhes

et al. 2004

Journal of Biological Chemistry

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“…The most abundant compounds, 10A and 10B, did not contain Mur; their NMR and mass spectra showed that they corresponded to [L-1-(D-lactoylamino)ethyl]phosphonic acid [(M-H)-= 1961 and its monomethyl ester [(M-H)-= 2101, respectively. They were certainly produced during the lithium hydroxide step, by @-elimination [18] or C -0 cleavage [19] of MurNAc derivatives whose anomeric position was unsubstituted.…”

Section: Methodsmentioning

confidence: 99%

Synthesis ofN-acetylmuramic acid derivatives as potential inhibitors of the D-glutamic acid-adding enzyme

et al. 1995

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Compounds containing N-acetyl-D-muramic acid and (L-1-aminoethy1)phosphonic acid were designed as potential inhibitors of the D-glutamic acid-adding enzyme of the biosynthesis of bacterial peptidoglycan.)phosphonic acid dimethyl ester]-c~,P-D-glucopyranose (9) was also prepared and was submitted to the MacDonald reaction in order to introduce a phosphate group on the anomeric position. A complex mixture of phosphorylated orland methylated derivatives of 3 was obtained. They were purified by h.p.1.c. and characterized by analyses of hexosamine, amino acid and labile phosphate, and by plasma desorption mass spectrometry. Neither 3 nor its derivatives inhibited the Dglutamic acid-adding enzyme from Escherichia coli.

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“…Nevertheless, peaks corresponding to the non-reduced forms of compounds I, II, III, and IV could be easily purified and characterized (data not shown). The corresponding lactoyl peptides, compounds IЈ, IIЈ, IIIЈ, and IVЈ, were obtained after a treatment with ammonium hydroxide, which cleaves the ether link internal to MurNAc (18), and were submitted to tandem mass spectrometry ( Fig. 4A and supplemental Fig.…”

Section: Purification and Chemical Composition Of The Peptidoglycan Omentioning

confidence: 99%

The Elucidation of the Structure of Thermotoga maritima Peptidoglycan Reveals Two Novel Types of Cross-link

Boniface

Parquet

Arthur

et al. 2009

Journal of Biological Chemistry

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Thermotoga maritima is a Gram-negative, hyperthermophilic bacterium whose peptidoglycan contains comparable amounts of L-and D-lysine. We have determined the fine structure of this cell-wall polymer. The muropeptides resulting from the digestion of peptidoglycan by mutanolysin were separated by high-performance liquid chromatography and identified by amino acid analysis after acid hydrolysis, dinitrophenylation, enzymatic determination of the configuration of the chiral amino acids, and mass spectrometry. The high-performance liquid chromatography profile contained four main peaks, two monomers, and two dimers, plus a few minor peaks corresponding to anhydro forms. Peptidoglycan (or murein) is a giant macromolecule whose main function is the protection of the cytoplasmic membrane against the internal osmotic pressure. It is composed of alternating residues of N-acetylglucosamine (GlcNAc) and N-acetylmuramic acid (MurNAc) 2 cross-linked by short peptides (1). The composition of the peptide stem in nascent peptidoglycan is L-Ala 1 -␥-D-Glu 2 -X 3 -D-Ala 4 -D-Ala 5 , where X is most often meso-diaminopimelic acid (meso-A 2 pm) or L-lysine in Gram-negative and Gram-positive species, respectively (2, 3). In the mature macromolecule, the last D-Ala residue is removed. Cross-linking of the glycan chains generally occurs between the carboxyl group of D-Ala at position 4 of a donor peptide stem and the side-chain amino group of the diamino acid at position 3 of an acceptor peptide stem (433 cross-links). Cross-linking is either direct or through a short peptide bridge such as pentaglycine in Staphylococcus aureus (2, 3). The enzymes for the formation of the 433 cross-links are active-site serine DDtranspeptidases that belong to the penicillin-binding protein (PBP) family and are the essential targets of ␤-lactam antibiotics in pathogenic bacteria (4). Catalysis involves the cleavage of the D-Ala 4 -D-Ala 5 bond of a donor peptide stem and the formation of an amide bond between the carboxyl of D-Ala 4 and the side chain amine at the third position of an acceptor stem. Transpeptidases of the LD specificity are active-site cysteine enzymes that were shown to act as surrogates of the PBPs in mutants of Enterococcus faecium resistant to ␤-lactam antibiotics (5). They cleave the X 3 -D-Ala 4 bond of a donor stem peptide to form 333 cross-links. This alternate mode of crosslinking is usually marginal, although it has recently been shown to predominate in non-replicative "dormant" forms of Mycobacterium tuberculosis (6).Thermotoga maritima is a Gram-negative, extremely thermophilic bacterium isolated from geothermally heated sea floors by Huber et al. (7). A morphological characteristic is the presence of an outer sheath-like envelope called "toga." Although the organism has received considerable attention for its biotechnological potential, studies about its peptidoglycan are scarce (8 -11), and in particular the fine structure of the macromolecule is still unknown. In their initial work, Huber et al. (7) showed that the comp...

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Treatment of peptidoglycan monomer with aqueous ammonia: Formation of lactoylpeptide and a saturated disaccharide

Cited by 5 publications

References 22 publications

Synthesis of Mosaic Peptidoglycan Cross-bridges by Hybrid Peptidoglycan Assembly Pathways in Gram-positive Bacteria

Synthesis of Mosaic Peptidoglycan Cross-bridges by Hybrid Peptidoglycan Assembly Pathways in Gram-positive Bacteria

Synthesis ofN-acetylmuramic acid derivatives as potential inhibitors of the D-glutamic acid-adding enzyme

The Elucidation of the Structure of Thermotoga maritima Peptidoglycan Reveals Two Novel Types of Cross-link

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