Literature DB >> 7926678

Site-directed mutagenesis of penicillin-binding protein 3 of Escherichia coli: role of Val-545.

J Ayala1, C Goffin, M Nguyen-Distèche, J M Ghuysen.   

Abstract

Val545 of the Escherichia coli penicillin-binding protein 3 is essential to the acyl transfer mechanism through which the active-site serine 307 is acylated by benzylpenicillin and cephalexin and to the mechanism through which the protein allows rapidly growing cells to divide.

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Year:  1994        PMID： 7926678     DOI： 10.1111/j.1574-6968.1994.tb07106.x

Source DB:  PubMed          Journal:  FEMS Microbiol Lett        ISSN： 0378-1097            Impact factor:   2.742


  2 in total

1.  Deciphering morphological determinants of the helix-shaped Leptospira.

Authors:  Leyla Slamti; Miguel A de Pedro; Emilande Guichet; Mathieu Picardeau
Journal:  J Bacteriol       Date:  2011-09-16       Impact factor: 3.490

2.  Cell division inhibition in Salmonella typhimurium histidine-constitutive strains: an ftsI-like defect in the presence of wild-type penicillin-binding protein 3 levels.

Authors:  D A Cano; C Mouslim; J A Ayala; F García-del Portillo; J Casadesús
Journal:  J Bacteriol       Date:  1998-10       Impact factor: 3.490
  2 in total

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