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- W2554285063 abstract "Abstract In the yeast Saccharomyces cerevisiae , the Sc GDH 1 and Sc GDH 3 encoded glutamate dehydrogenases ( NADP ‐ GDH s) 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 Sc Gdh1 and Sc Gdh3, 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 ( Sc Gdh1 and Sc Gdh3), Kluyveromyces lactis ( Kl Gdh1), and Lachancea kluyveri ( Lk Gdh1) and their evolutionary history. Our results show that the kinetic properties of K. lactis and L. kluyveri single NADP ‐ GDH s are respectively similar to either Sc GDH 3 or Sc GDH 1 , which arose from the whole genome duplication event of the S. cerevisiae lineage, although, Kl GDH 1 and Lk GDH 1 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 ‐ GDH s capacity to utilize α‐ KG and synthesize glutamate do not correlate with their evolutionary origin." @default.
- W2554285063 created "2016-11-30" @default.
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- W2554285063 date "2016-11-19" @default.
- W2554285063 modified "2023-10-05" @default.
- W2554285063 title "Diversification of the kinetic properties of yeast NADP-glutamate-dehydrogenase isozymes proceeds independently of their evolutionary origin" @default.
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- W2554285063 doi "https://doi.org/10.1002/mbo3.419" @default.
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