<abstract xmlns="http://www.w3.org/1999/xhtml"> Adenylat kinase is an ubiquitous enzyme found in prokaryotes and eukaryotes. In the present study we examined the inhibition of Streptococcus pneumoniae adenylate kinase (AKSP) by six 5-arylidene-thiazolidin-4- on-2-thione derivates using 2, 4-dinitrophenylhydrazine colorimetric assay. Inhibition of AKSP activity with synthetic compounds was performed against recombinant enzyme over-expressed in E. coli. The compound C10H6BrNOS2 with the bromine atom in -ortho position has shown the most efficient inhibitory activity; I50 value (the inhibitor concentration that leads to 50% activity inhibition) was 0.067mM.</abstract>

Adenylat kinase is an ubiquitous enzyme found in prokaryotes and eukaryotes. In the present study we examined the inhibition of Streptococcus pneumoniae adenylate kinase (AKSP) by six 5-arylidene-thiazolidin-4- on-2-thione derivates using 2, 4-dinitrophenylhydrazine colorimetric assay. Inhibition of AKSP activity with synthetic compounds was performed against recombinant enzyme over-expressed in E. coli. The compound C10H6BrNOS2 with the bromine atom in -ortho position has shown the most efficient inhibitory activity; I50 value (the inhibitor concentration that leads to 50% activity inhibition) was 0.067mM.

Inhibition of Streptococcus pneumoniae adenylate kinase by some 5-arylidene-thiazolidin-4-on-2-thione derivates

“Iuliu Haţieganu” University of Medicine and Pharmacy, Cluj-Napoca Microbiology Department, Str. Louis Pasteur, Nr.6, Cluj-Napoca, Romania, 400349, Tel: 0740-859281

Cantacuzino Institute, Enzymology and Applied Microbiology Laboratory, Bucharest

“Iuliu Haţieganu” University of Medicine and Pharmacy, Cluj-Napoca

Revista Romana de Medicina de Laborator

Adenylat kinase is an ubiquitous enzyme found in prokaryotes and eukaryotes. In the present study we examined the inhibition of Streptococcus pneumoniae...

Inhibition of Streptococcus pneumoniae adenylate kinase by some 5-arylidene-thiazolidin-4-on-2-thione derivates

Publié en ligne: 08 août 2013

Pages: 93 - 99

DOI: https://doi.org/10.2478/rrlm-2013-0022

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