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Hypoxanthine-Guanine Phosphoribosyltransferase/adenylate Kinase From Zobellia galactanivorans: A Bifunctional Catalyst for the Synthesis of Nucleoside-5′-Mono-, Di- and Triphosphates

dc.contributor.authorAcosta, Javierspa
dc.contributor.authorDel Arco, Jonspa
dc.contributor.authorDel Pozo, Maria Luisaspa
dc.contributor.authorHerrera, Beliñaspa
dc.contributor.authorClemente-Suárez, Vicente Javierspa
dc.contributor.authorBerenguer, Joséspa
dc.contributor.authorHidalgo, Aureliospa
dc.contributor.authorFernández-Lucas, Jesússpa
dc.date.accessioned2020-07-07T19:25:59Z
dc.date.available2020-07-07T19:25:59Z
dc.date.issued2020-06-24
dc.identifier.issn2296-4185spa
dc.identifier.urihttps://hdl.handle.net/11323/6477spa
dc.description.abstractIn our search for novel biocatalysts for the synthesis of nucleic acid derivatives, we found a good candidate in a putative dual-domain hypoxanthine-guanine phosphoribosyltransferase (HGPRT)/adenylate kinase (AMPK) from Zobellia galactanivorans (ZgHGPRT/AMPK). In this respect, we report for the first time the recombinant expression, production, and characterization of a bifunctional HGPRT/AMPK. Biochemical characterization of the recombinant protein indicates that the enzyme is a homodimer, with high activity in the pH range 6-7 and in a temperature interval from 30 to 80°C. Thermal denaturation experiments revealed that ZgHGPRT/AMPK exhibits an apparent unfolding temperature (Tm) of 45°C and a retained activity of around 80% when incubated at 40°C for 240 min. This bifunctional enzyme shows a dependence on divalent cations, with a remarkable preference for Mg2+ and Co2+ as cofactors. More interestingly, substrate specificity studies revealed ZgHGPRT/AMPK as a bifunctional enzyme, which acts as phosphoribosyltransferase or adenylate kinase depending upon the nature of the substrate. Finally, to assess the potential of ZgHGPRT/AMPK as biocatalyst for the synthesis of nucleoside-5′-mono, di- and triphosphates, the kinetic analysis of both activities (phosphoribosyltransferase and adenylate kinase) and the effect of water-miscible solvents on enzyme activity were studied.spa
dc.language.isoeng
dc.publisherFrontiers in Bioengineering and Biotechnologyspa
dc.rightsCC0 1.0 Universalspa
dc.rights.urihttp://creativecommons.org/publicdomain/zero/1.0/spa
dc.subjectEnzymatic synthesisspa
dc.subjectNucleotidesspa
dc.subjectPhosphoribosyltransferasespa
dc.subjectNucleoside-5cpsdummy′-monophosphate kinasespa
dc.subjectDual domain proteinspa
dc.titleHypoxanthine-Guanine Phosphoribosyltransferase/adenylate Kinase From Zobellia galactanivorans: A Bifunctional Catalyst for the Synthesis of Nucleoside-5′-Mono-, Di- and Triphosphatesspa
dc.typeArtículo de revistaspa
dc.rights.accessrightsinfo:eu-repo/semantics/openAccessspa
dc.identifier.doihttps://doi.org/10.3389/fbioe.2020.00677spa
dc.identifier.instnameCorporación Universidad de la Costaspa
dc.identifier.reponameREDICUC - Repositorio CUCspa
dc.identifier.repourlhttps://repositorio.cuc.edu.co/spa
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