Chapter 771 Actinomadura R39 d-Ala d Ala Carboxypeptidase
نویسندگان
چکیده
bacterial penicillin-binding proteins and beta-lactamases. Antimicrob. Agents Chemother. 42(1), 1 17. [41] Davies, C., White, S.W., Nicholas, R.A. (2001). Crystal structure of a deacylation-defective mutant of penicillin-binding protein 5 at 2.3-Å resolution. J. Biol. Chem. 276(1), 616 623. [42] Nicola, G., Tomberg, J., Pratt, R.F., Nicholas, R.A., Davies, C. (2010). Crystal structures of covalent complexes of beta-lactam antibiotics with Escherichia coli penicillin-binding protein 5: toward an understanding of antibiotic specificity. Biochemistry 49(37), 8094 8104. [43] Pratt, R.F., McLeish, M.J. (2010). Structural relationship between the active sites of beta-lactam-recognizing and amidase signature enzymes: convergent evolution? Biochemistry 49(45), 9688 9697. [44] Blumberg, P.M., Strominger, J.L. (1972). Isolation by covalent affinity chromatography of the penicillin-binding components from membranes of Bacillus subtilis. Proc. Natl. Acad. Sci. USA 69(12), 3751 3755. [45] Kawai, F., Clarke, T.B., Roper, D.I., Han, G.J., Hwang, K.Y., Unzai, S., Obayashi, E., Park, S.Y., Tame, J.R. (2010). Crystal structures of penicillin-binding proteins 4 and 5 from Haemophilus influenzae. J. Mol. Biol. 396(3), 634 645. [46] Broome-Smith, J.K., Ioannidis, I., Edelman, A., Spratt, B.G. (1988). Nucleotide sequences of the penicillin-binding protein 5 and 6 genes of Escherichia coli. Nucleic Acids Res. 16(4), 1617. [47] Chowdhury, C., Ghosh, A.S. (2011). Differences in active-site microarchitecture explain the dissimilar behaviors of PBP5 and 6 in Escherichia coli. J. Mol. Graph. Model. 29(5), 650 656. [48] Nicola, G., Fedarovich, A., Nicholas, R.A., Davies, C. (2005). A large displacement of the SXN motif of Cys115-modified penicillin-binding protein 5 from Escherichia coli. Biochem. J. 392(Pt. 1), 55 63. [49] Morlot, C., Pernot, L., Le Gouellec, A., Di Guilmi, A.M., Vernet, T., Dideberg, O., Dessen, A. (2005). Crystal structure of a peptidoglycan synthesis regulatory factor (PBP3) from Streptococcus pneumonia. J. Biol. Chem. 280(16), 15984 15991. [50] Pratt, R.F. (2002). Functional evolution of the serine β-lactamase active site. J. Chem. Soc. Perkin Transactions 2(5), 851 861.
منابع مشابه
Inhibition of Streptococcus pneumoniae penicillin-binding protein 2x and Actinomadura R39 DD-peptidase activities by ceftaroline.
Although the rate of acylation of a penicillin-resistant form of Streptococcus pneumoniae penicillin-binding protein 2x (PBP2x) by ceftaroline is 80-fold lower than that of its penicillin-sensitive counterpart, it remains sufficiently high (k(2)/K = 12,600 M(-1) s(-1)) to explain the sensitivity of the penicillin-resistant strain to this new cephalosporin. Surprisingly, the Actinomadura R39 DD-...
متن کاملSite-directed mutagenesis of the Actinomadura R39 DD-peptidase.
The role of various residues in the conserved structural elements of the Actinomadura R39 penicillin-sensitive dd-peptidase has been studied by site-directed mutagenesis. Replacement of Ser-298 of the 'SDN loop' by Ala or Gly significantly decreased the kcat/Km value for the peptide substrate, but only by a factor of 15 and had little effect on the other catalytic properties. Mutations of Asn-3...
متن کاملPrimary and predicted secondary structure of the Actinomadura R39 extracellular DD-peptidase, a penicillin-binding protein (PBP) related to the Escherichia coli PBP4.
As derived from gene cloning and sequencing, the 489-amino-acid DD-peptidase/penicillin-binding protein (PBP) produced by Actinomadura R39 has a primary structure very similar to that of the Escherichia coli PBP4 [Mottl, Terpstra & Keck (1991) FEMS Microbiol. Lett. 78, 213-220]. Hydrophobic-cluster analysis of the two proteins shows that, providing that a large 174-amino-acid stretch is exclude...
متن کاملThe penicillin-binding site in the exocellular DD-carboxypeptidase-transpeptidase of Actinomadura R39.
Heat denaturation and Pronase degradation of the complex previously formed between benzylpenicillin and the exocellular DD-carboxypeptidase-transpeptidase of Actinomadura R39 yields a heptapeptide H-Leu-Pro-Ala-Ser-Asn-Gly-Val-OH, where the benzylpenicilloyl group is ester-linked to the serine residue. This linkage is very labile and its hydrolysis causes the release of benzylpenicilloate. In c...
متن کاملCrystal structure of the Actinomadura R39 DD-peptidase reveals new domains in penicillin-binding proteins.
Actinomadura sp. R39 produces an exocellular DD-peptidase/penicillin-binding protein (PBP) whose primary structure is similar to that of Escherichia coli PBP4. It is characterized by a high beta-lactam-binding activity (second order rate constant for the acylation of the active site serine by benzylpenicillin: k2/K = 300 mm(-1) s(-1)). The crystal structure of the DD-peptidase from Actinomadura...
متن کاملSPR Biosensor Analysis of -Lactam Antibiotics in Milk Development and use of assays based on a -lactam receptor protein
The aim of this study was to investigate the applicability of an SPR biosensor in combination with a -lactam receptor protein for generic detection of -lactam antibiotics in milk. β-Lactam antibiotics constitute the group of antimicrobials most commonly used for treatment of bacterial infections in dairy cows. Consequently, they are also the most common type of drug residue found in milk and, a...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
عنوان ژورنال:
دوره شماره
صفحات -
تاریخ انتشار 2012