Literature DB >> 9614972

X-ray studies of enzymes that interact with penicillins.

J A Kelly1, A P Kuzin, P Charlier, E Fonzé.   

Abstract

The technique of X-ray diffraction has been successfully applied to enzymes associated with peptidoglycan biosynthesis. The technique has taught us a great deal about the structures and catalytic mechanisms of penicillin-binding proteins and beta-lactamases. An insight into the structural basis for antibiotic resistance is given.

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Year:  1998        PMID： 9614972     DOI： 10.1007/s000180050163

Source DB:  PubMed          Journal:  Cell Mol Life Sci        ISSN： 1420-682X            Impact factor:   9.261


  5 in total

1.  A 1.2-A snapshot of the final step of bacterial cell wall biosynthesis.

Authors:  W Lee; M A McDonough; L Kotra; Z H Li; N R Silvaggi; Y Takeda; J A Kelly; S Mobashery
Journal:  Proc Natl Acad Sci U S A       Date:  2001-02-13       Impact factor: 11.205

Review 2.  Biochemistry and comparative genomics of SxxK superfamily acyltransferases offer a clue to the mycobacterial paradox: presence of penicillin-susceptible target proteins versus lack of efficiency of penicillin as therapeutic agent.

Authors:  Colette Goffin; Jean-Marie Ghuysen
Journal:  Microbiol Mol Biol Rev       Date:  2002-12       Impact factor: 11.056

Review 3.  Multimodular penicillin-binding proteins: an enigmatic family of orthologs and paralogs.

Authors:  C Goffin; J M Ghuysen
Journal:  Microbiol Mol Biol Rev       Date:  1998-12       Impact factor: 11.056

4.  Critical involvement of a carbamylated lysine in catalytic function of class D beta-lactamases.

Authors:  D Golemi; L Maveyraud; S Vakulenko; J P Samama; S Mobashery
Journal:  Proc Natl Acad Sci U S A       Date:  2001-11-27       Impact factor: 11.205

5.  Induction of beta-lactamase influences the course of development in Myxococcus xanthus.

Authors:  K A O'Connor; D R Zusman
Journal:  J Bacteriol       Date:  1999-10       Impact factor: 3.490
  5 in total

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