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Microbial 5′-nucleotidases: their characteristics, roles in cellular metabolism, and possible practical applications
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Microbial 5′-nucleotidases: their characteristics, roles in cellular metabolism, and possible practical applications
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Journal Article
Microbial 5′-nucleotidases: their characteristics, roles in cellular metabolism, and possible practical applications
2021
Overview
5′-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.
Publisher
Springer Nature B.V
Subject
/ Enzymes
