VSE knjižnice (vzajemna bibliografsko-kataložna baza podatkov COBIB.SI)
  • Purification and biochemical characterization of Mur ligases from Staphylococcus aureus
    Patin, Delphine ...
    The Mur ligases (MurC, MurD, MurE and MurF) catalyze the stepwise synthesis ofthe UDP-N-acetylmuramoyl-pentapeptide precursor of peptidoglycan. The murC, murD, murE and murF genes from Staphylococcus ... aureus, a major pathogen, were cloned and the corresponding proteins were overproduced in Escherichia coli and purified as His(6)-tagged forms. Their biochemical properties were investigated and compared to those of the E. coli enzymes. Staphylococcal MurCaccepted L-Ala, L-Ser and Gly as substrates, as the E. coli enzyme does, with a strong preference for L-Ala. S. aureus MurE was very specific for L-lysine and in particular did not accept meso-diaminopimelic acid as a substrate. This mirrors the E. coli MurE specificity, for which meso-diaminopimelic acid is the preferred substrate and L-lysine a very poor one. S. aureus MurF appeared less specific and accepted both forms (L-lysine and meso-diaminopimelic acid) of UDP-MurNAc-tripeptide, as the E. coli MurF does. The inverse and strict substrate specificities of the two MurE orthologues is thus responsible for the presence of exclusively meso-diaminopimelic acid and L-lysine at the third position of the peptide in the peptidoglycans of E. coli and S. aureus, respectively. The specific activities of the four Mur ligases were also determined in crude extracts of S. aureus and compared to cell requirements for peptidoglycan biosynthesis.
    Vir: Biochimie. - ISSN 0300-9084 (Vol. 92, no. 12, 2010, str. 1793-1800)
    Vrsta gradiva - članek, sestavni del
    Leto - 2010
    Jezik - angleški
    COBISS.SI-ID - 2965105

    Povezava(-e):

    http://www.sciencedirect.com/science?_ob=ArticleURL&_udi=B6VRJ-50M1S02-1&_user=4776866&_coverDate=12%2F31%2F2010&_rdoc=1&_fmt=high&_orig=gateway&_origin=gateway&_sort=d&_docanchor=&view=c&_acct=C000033658&_version=1&_urlVersion=0&_userid=4776866&md5=0fe01aa87d3b56989c9f4256ea1ecb83&searchtype=a
    DOI

vir: Biochimie. - ISSN 0300-9084 (Vol. 92, no. 12, 2010, str. 1793-1800)
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