GlcNAc De- N -Acetylase from the Hyperthermophilic Archaeon Sulfolobus solfataricus

Author:

Iacono Roberta12,Strazzulli Andrea13,Maurelli Luisa2,Curci Nicola12,Casillo Angela4,Corsaro Maria Michela4,Moracci Marco123,Cobucci-Ponzano Beatrice2ORCID

Affiliation:

1. Department of Biology, University of Naples Federico II, Naples, Italy

2. Institute of Biosciences and BioResources, National Research Council of Italy, Naples, Italy

3. Task Force on Microbiome Studies, University of Naples Federico II, Naples, Italy

4. Department of Chemical Sciences, University of Naples Federico II, Naples, Italy

Abstract

In this study, a preliminary screening of cellular extracts of S. solfataricus allowed the identification of an α- N -acetylglucosaminidase activity. However, the characterization of the corresponding recombinant enzyme revealed a novel GlcNAc de- N -acetylase, which, in cooperation with the α-glucosidase, catalyzed the hydrolysis of O-α-GlcNAc glycosides. In addition, we show that the product of a gene flanking the one encoding the de- N -acetylase is a putative glycosyltransferase, suggesting the involvement of the two enzymes in the metabolism of GlcNAc. The discovery and functional analysis of novel enzymatic activities involved in the modification of this essential sugar represent a powerful strategy to shed light on the physiology and metabolism of Archaea .

Funder

Italian Space Agency - ASI

Publisher

American Society for Microbiology

Subject

Ecology,Applied Microbiology and Biotechnology,Food Science,Biotechnology

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