Microbial 5\u2032-nucleotidases: their characteristics, roles in cellular metabolism, and possible practical applications

Natalia P. Zakataeva

doi:10.1007/s00253-021-11547-w

Natalia P. Zakataeva

Open Access

https://doi.org/10.1007/s00253-021-11547-w

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Abstract

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.Graphical abstract

Highlights

5′-Nucleotidases (EC 3.1.3.5) are enzymes that catalyze the hydrolytic dephosphorylation of 5′-ribonucleotides and 5′-deoxyribonucleotides to their corresponding nucleosides plus phosphate [5′-(deoxy) ribonucleotide + H2O < = >ribonucleoside + phosphate]
By influencing the level of proinflammatory extracellular ATP and anti-inflammatory extracellular adenosine, ecto-5′-nucleotidases are involved in cell–matrix or cell–cell interactions and transmembrane signaling and play important roles in immune and inflammatory responses (Zimmermann et al 2012)
The present review summarizes the current knowledge about microbial 5′-nucleotidases, with a focus on their diversity, cellular localizations, molecular structures, mechanisms of catalysis, activity regulation, and physiological roles; approaches to identify these enzymes; and their possible applications in biotechnology

Summary

Introduction

Depending on their molecular structure, type of hydrolytic mechanism, and cellular location, microbial 5′-nucleotidases hydrolyze a certain substrate range, exhibit a specific pattern of activity regulation, and play a certain physiological role Despite differences in their localization and their attachment to the cell surface or presence in a soluble form, all secreted (surface-located, periplasmic and extracellular) microbial 5′-nucleotidases that utilize the type I catalytic mechanism characterized to date show low but significant sequence identity with the mammalian ecto-5′-nucleotidase CD73 (Zimmermann 1992; Colgan et al 2006), indicating their common ancestry and similar structures (Volknandt et al 1991; Sträter 2006) (Fig. 1a). C. glutamicum UshA has demonstrated activity against guanosine monophosphate (GMP), inosine monophosphate

Metal ion requirement

UDP sugars

Expression regulation

Posttranslational regulation

Findings

Conclusions and future prospects