Literature DB >> 12946254

Specificity of the action of lysoamidase on Staphylococcus aureus 209P cell walls.

E A Begunova1, O A Stepnaya, V Ya Lysanskaya, I S Kulaev.   

Abstract

Specificity of Staphylococcus aureus 209P cell wall hydrolysis by the L1 and L2-bacteriolytic enzymes from lysoamidase lytic complex was studied. L1-peptidase was shown to display both glycyl-glycine endopeptidase and N-acetylmuramyl-L-alanine amidase enzymatic activities on the S. aureus peptidoglycan molecule, whereas L2-peptidase acts as N-acetylmuramyl-L-alanine amidase.

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Year:  2003        PMID: 12946254     DOI: 10.1023/a:1025074714910

Source DB:  PubMed          Journal:  Biochemistry (Mosc)        ISSN: 0006-2979            Impact factor:   2.487


  2 in total

1.  Structural Studies of Component of Lysoamidase Bacteriolytic Complex from Lysobacter sp. XL1.

Authors:  Svetlana Tishchenko; Azat Gabdulkhakov; Bogdan Melnik; Irina Kudryakova; Oleg Latypov; Natalya Vasilyeva; Alexey Leontievsky
Journal:  Protein J       Date:  2016-02       Impact factor: 2.371

2.  Cloning and expression analysis of genes encoding lytic endopeptidases L1 and L5 from Lysobacter sp. strain XL1.

Authors:  Y S Lapteva; O E Zolova; M G Shlyapnikov; I M Tsfasman; T A Muranova; O A Stepnaya; I S Kulaev; I E Granovsky
Journal:  Appl Environ Microbiol       Date:  2012-08-03       Impact factor: 4.792

  2 in total

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