| Literature DB >> 4945198 |
N Krymkiewicz, E Diéguez, U D Rekarte, N Zwaig.
Abstract
A lethal product (BPG) produced by a glycerol kinase mutant of Escherichia coli was purified, and its mode of action on E. coli was studied. At concentrations where BPG strongly inhibits in vivo deoxyribonucleic acid, ribonucleic acid, and protein synthesis, it produces small effects on other functions: slight inhibition of respiration and small changes in intracellular pools of substrates, nucleic acids degradation, and adenosine triphosphate levels. BPG also inhibits in vitro protein synthesis and produces inactivation of bacteriophage T4. The bactericidal product has been identified in another laboratory as methylglyoxal (MG). By comparing BPG and MG, we confirmed this observation and concluded that the activity found in our BPG preparation is due to its MG content. We also observed that MG is able to react with guanosine triphosphate. According to these results, it is interpreted that MG could act directly on macromolecular synthesis by reacting with the guanine residues of nucleic acids and its precursors.Entities:
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Year: 1971 PMID: 4945198 PMCID: PMC247224 DOI: 10.1128/jb.108.3.1338-1347.1971
Source DB: PubMed Journal: J Bacteriol ISSN: 0021-9193 Impact factor: 3.490