Diversification of the kinetic properties of yeast NADP‐glutamate‐dehydrogenase isozymes proceeds independently of their evolutionary origin

dc.creatorJOSE CARLOS CAMPERO BASALDUA
dc.creatorHector Quezada
dc.creatorLINA RAQUEL RIEGO RUIZ
dc.creatorDARIEL MARQUEZ GUTIERREZ
dc.creatorJames González
dc.creatorMOHAMMED EL HAFIDI BENTLAKDER
dc.creatorMARIA ALICIA GONZALEZ MANJARREZ
dc.date2017-04
dc.date.accessioned2022-10-12T19:56:29Z
dc.date.available2022-10-12T19:56:29Z
dc.identifierhttp://ipicyt.repositorioinstitucional.mx/jspui/handle/1010/1631
dc.identifier.urihttps://repositorioslatinoamericanos.uchile.cl/handle/2250/4125351
dc.description"In the yeast Saccharomyces cerevisiae, the ScGDH1 and ScGDH3 encoded glutamate dehydrogenases (NADP‐GDHs) catalyze the synthesis of glutamate from ammonium and α‐ketoglutarate (α‐KG). Previous kinetic characterization showed that these enzymes displayed different allosteric properties and respectively high or low rate of α‐KG utilization. Accordingly, the coordinated action of ScGdh1 and ScGdh3, regulated balanced α‐KG utilization for glutamate biosynthesis under either fermentative or respiratory conditions, safeguarding energy provision. Here, we have addressed the question of whether there is a correlation between the regulation and kinetic properties of the NADP‐GDH isozymes present in S. cerevisiae (ScGdh1 and ScGdh3), Kluyveromyces lactis (KlGdh1), and Lachancea kluyveri (LkGdh1) and their evolutionary history. Our results show that the kinetic properties of K. lactis and L. kluyveri single NADP‐GDHs are respectively similar to either ScGDH3 or ScGDH1, which arose from the whole genome duplication event of the S. cerevisiae lineage, although, KlGDH1 and LkGDH1 originated from a GDH clade, through an ancient interspecies hybridization event that preceded the divergence between the Saccharomyces clade and the one containing the genera Kluyveromyces, Lachancea, and Eremothecium. Thus, the kinetic properties which determine the NADP‐GDHs capacity to utilize α‐KG and synthesize glutamate do not correlate with their evolutionary origin."
dc.formatapplication/pdf
dc.publisherJohn Wiley & Sons
dc.relationinfo:eu-repo/semantics/altIdentifier/DOI/https://doi.org/10.1002/mbo3.419
dc.relationcitation:Campero‐Basaldua, C., Quezada, H., Riego‐Ruíz, L., Márquez, D., Rojas, E., González, J., El‐Hafidi, M. and González, A. Diversification of the kinetic properties of yeast NADP‐glutamate‐dehydrogenase isozymes proceeds independently of their evolutionary origin. MicrobiologyOpen. 2017;6:e00419. https://doi.org/10.1002/mbo3.419
dc.rightsinfo:eu-repo/semantics/openAccess
dc.rightshttp://creativecommons.org/licenses/by-nc-nd/4.0
dc.subjectinfo:eu-repo/classification/Autor/Functional diversification
dc.subjectinfo:eu-repo/classification/Autor/Glutamate dehydrogenase
dc.subjectinfo:eu-repo/classification/Autor/Kinetics
dc.subjectinfo:eu-repo/classification/Autor/Paralogous enzymes
dc.subjectinfo:eu-repo/classification/Autor/Phylogeny
dc.subjectinfo:eu-repo/classification/Autor/Yeast gene duplication
dc.subjectinfo:eu-repo/classification/cti/2
dc.subjectinfo:eu-repo/classification/cti/24
dc.subjectinfo:eu-repo/classification/cti/2414
dc.titleDiversification of the kinetic properties of yeast NADP‐glutamate‐dehydrogenase isozymes proceeds independently of their evolutionary origin
dc.typeinfo:eu-repo/semantics/article
dc.typeinfo:eu-repo/semantics/publishedVersion


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