Microbial 5′-nucleotidases: their characteristics, roles in cellular metabolism, and possible practical applications

Abstract

Abstract5′-Nucleotidases (EC 3.1.3.5) are enzymes that catalyze the hydrolytic dephosphorylation of 5′-ribonucleotides and 5′-deoxyribonucleotides to their respective nucleosides and phosphate. Most 5′-nucleotidases have broad substrate specificity and are multifunctional enzymes capable of cleaving phosphorus from not only mononucleotide phosphate molecules but also a variety of other phosphorylated metabolites. 5′-Nucleotidases are widely distributed throughout all kingdoms of life and found in different cellular locations. The well-studied vertebrate 5′-nucleotidases play an important role in cellular metabolism. These enzymes are involved in purine and pyrimidine salvage pathways, nucleic acid repair, cell-to-cell communication, signal transduction, control of the ribo- and deoxyribonucleotide pools, etc. Although the first evidence of microbial 5′-nucleotidases was obtained almost 60 years ago, active studies of genetic control and the functions of microbial 5′-nucleotidases started relatively recently. The present review summarizes the current knowledge about microbial 5′-nucleotidases with a focus on their diversity, cellular localizations, molecular structures, mechanisms of catalysis, physiological roles, and activity regulation and approaches to identify new 5′-nucleotidases. The possible applications of these enzymes in biotechnology are also discussed.Key points• Microbial 5′-nucleotidases differ in molecular structure, hydrolytic mechanism, and cellular localization.• 5′-Nucleotidases play important and multifaceted roles in microbial cells.• Microbial 5′-nucleotidases have wide range of practical applications. Graphical abstract

In silico biotechnological potential of Bacillus sp. strain MHSD_37 bacterial endophyte

“…5’-nucleotidase have a broad substrate specificity and catalyse the hydrolytic dephosphorylation of 5′-ribonucleotides and 5′-deoxyribonucleotides to their respective nucleosides and phosphate [ 54 ]. Nucleotidase are also involved in cell-to-cell communication, nucleic acid repair, and signal transduction, and control of the ribo- and deoxyribonucleotide pools [ 55 ]. Therefore, the prevalence of cell wall anchored 5’-nucleotidase in most human bacterial pathogens as well as such roles in cell-to-cell communication and signal transduction [ 56 ], make nucleotidase potential targets for vaccine development.…”

Clostridium perfringens phospholipase C, an archetypal bacterial virulence factor, induces the formation of extracellular traps by human neutrophils

“…They are homologous to enzymes relevant for pathogenicity in different streptococcal species ( Soh et al., 2020 ). 5´-nucleotidases catalyze the hydrolytic dephosphorylation of nucleotides and deoxynucleotides to their respective nucleosides and deoxynucleosides ( Zakataeva, 2021 ). Cell wall-anchored or secreted bacterial 5´-nucleotidases could be virulence factors that disturb the host inflammatory response ( Zakataeva, 2021 ).…”

Quantifying the effect of water quality on eDNA degradation using microcosm and bioassay experiments

“…One major reservoir of organic phosphorus is dissolved DNA, which is one form of eDNA (Grzyb & Fraczek, 2012), and was the form of DNA used in this study. eDNA that is dissolved in the water can be targeted by the 5′-nucleotidase enzymes that are secreted by many bacteria and cyanobacteria found throughout the water column (Zakataeva, 2021). In our filtered treatment in the bioassays, we used a 0.22 μm pore size filter, which would remove aquatic bacteria (which are 0.4-1.0 mm in diameter (Button & Robertson, 1999)).…”