PMID:14750804
| Citation |
Hesek, D, Suvorov, M, Morio, K, Lee, M, Brown, S, Vakulenko, SB and Mobashery, S (2004) Synthetic peptidoglycan substrates for penicillin-binding protein 5 of Gram-negative bacteria. J. Org. Chem. 69:778-84 |
|---|---|
| Abstract |
The major constituent of the bacterial cell wall, peptidoglycan, is comprised of repeating units of N-acetylglucosamine (NAG) and N-acetylmuramic acid (NAM) with an appended peptide. Penicillin-binding proteins (PBPs) are involved in the final stages of bacterial cell wall assembly. Two activities for PBPs are the cross-linking of the cell wall, carried out by dd-transpeptidases, and the dd-peptidase activity, that removes the terminal d-Ala residue from peptidoglycan. The dd-peptidase activity moderates the extent of the cell wall cross-linking. There exists a balance between the two activities that is critical for the well-being of bacterial cells. We have cloned and purified PBP5 of Escherichia coli. The membrane anchor of this protein was removed, and the enzyme was obtained as a soluble protein. Two fragments of the polymeric cell wall of Gram-negative bacteria (compounds 5 and 6) were synthesized. These molecules served as substrates for PBP5. The products of the reactions of PBP5 and compounds 5 and 6 were isolated and were shown to be d-Ala and the fragments of the substrates minus the terminal d-Ala. The kinetic parameters for these enzymic reactions were evaluated. PBP5 would appear to have the potential for turnover of as many as 1.4 million peptidoglycan strands within a single doubling time (i.e., generation) of E. coli. |
| Links |
PubMed Online version:10.1021/jo035397e |
| Keywords |
Bacterial Proteins/genetics; Bacterial Proteins/metabolism; Carrier Proteins/genetics; Carrier Proteins/metabolism; Escherichia coli/enzymology; Escherichia coli/metabolism; Escherichia coli Proteins/genetics; Escherichia coli Proteins/metabolism; Hexosyltransferases/genetics; Hexosyltransferases/metabolism; Muramoylpentapeptide Carboxypeptidase/genetics; Muramoylpentapeptide Carboxypeptidase/metabolism; Nuclear Magnetic Resonance, Biomolecular; Penicillin-Binding Proteins; Peptide Fragments/chemical synthesis; Peptide Fragments/metabolism; Peptidoglycan/chemistry; Peptidoglycan/metabolism; Peptidyl Transferases/genetics; Peptidyl Transferases/metabolism; Recombinant Proteins/genetics; Recombinant Proteins/metabolism; Substrate Specificity |
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