Publications by authors named "Pometun A"

The problem of antibiotic resistance is currently very acute. Numerous research and development of new antibacterial drugs are being carried out that could help cope with various infectious agents. One of the promising directions for the search for new antibacterial drugs is the search among the probiotic strains present in the human gastrointestinal tract.

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Ribonucleoside hydrolases are enzymes that catalyze the cleavage of ribonucleosides to nitrogenous bases and ribose. These enzymes are found in many organisms: bacteria, archaea, protozoa, metazoans, yeasts, fungi and plants. Despite the simple reaction catalyzed by these enzymes, their physiological role in most organisms remains unclear.

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The expression of multifunctional proteins can facilitate the setup of a biotechnology process that requires multiple functions absolved by different proteins. Herein the functional and conformational characterization of a formate dehydrogenase-monooxygenase chimera enzyme is presented. The fused enzyme (FDH-PAMO) was prepared by linking the C-terminus of the mutant NADP-dependent formate dehydrogenase from Pseudomonas sp.

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In order to accelerate Sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE), here we propose an optimized version of the technique enabled by experimental tuning reinforced by theoretical description. In the resulting system, the gel buffer was diluted twofold and supplemented with glycine at a low concentration, whereas a higher voltage was applied. This approach reduced runtime from 90 to 18 min.

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Article Synopsis
  • Oxidized nicotinamide adenine dinucleotide (NAD) is crucial for cellular metabolism and signaling, and this research develops a reliable enzymatic assay to measure NAD levels in human blood.
  • The study compares NAD concentrations between healthy individuals and patients with cardiac or neurological diseases, finding significant reductions in NAD levels among these patient groups.
  • The assay not only confirms expected NAD levels in healthy subjects but also highlights its potential as a diagnostic tool by offering better differentiation between cardiac and neurological patients through NAD ratio comparisons with other blood markers.
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Article Synopsis
  • Researchers fused genes from cytochrome P450 BM3 and formate dehydrogenase to create multifunctional enzymes aimed at improving stability and activity.
  • The study varied the arrangement of the genes and linkers and compared the fused enzymes with individual ones in terms of substrate conversion and stability.
  • A significant increase in activity (up to threefold) was noted for the fusion constructs, indicating that the fusion may cause conformational changes in P450 BM3, although no NADPH channeling was observed.
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# These authors contributed equally to the work. NAD+-dependent formate dehydrogenase from Staphylococcus aureus (SauFDH) is one of the key enzymes responsible for the survival of this pathogen in the form of biofilms. 3D structure of the enzyme might be helpful in the search for highly specific SauFDH inhibitors that can be used as antibacterial agents exactly against S.

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Article Synopsis
  • - The increasing importance of NAD in medical research necessitates efficient methods for quantifying it in complex samples.
  • - A novel fluorometric assay using formate dehydrogenase allows for specific and straightforward measurement of NAD without needing complicated separation techniques.
  • - This method has been successfully tested on rat brain cortex and mitochondria extracts, demonstrating its reliability and stability in various conditions.
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