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Identification of cofactor discrimination sites in NAD-isocitrate dehydrogenase from Pyrococcus furiosus

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Abstract.

The role of Asp-328 and Ile-329 as a cofactor discrimination site of the NAD-dependent isocitrate dehydrognase (NAD-IDH) from Pyrococcus furiosus has been verified by replacing these residues with Lys and Tyr, respectively, which are the corresponding residues in NADP-IDH from Escherichia coli. The Asp-328–Lys mutant showed dual coenzyme specificity, whereas introduction of the double mutation, Asp-328–Lys/Ile-329–Tyr shifted the cofactor preference from NAD to NADP. NADP-dependent P. furiosus IDH retained thermostability and thermoactivity compared with NAD-IDH.

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Authors and Affiliations

  1. Department of Microbiology, University of Bergen, P.O. Box 7800, Jahnebakken 5, 5020 Bergen, Norway, , , , ,

    Ida Steen, Torleiv Lien, Marit Madsen & Nils-Kåre Birkeland

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  1. Ida Steen
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  2. Torleiv Lien
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  3. Marit Madsen
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  4. Nils-Kåre Birkeland
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Steen, I., Lien, T., Madsen, M. et al. Identification of cofactor discrimination sites in NAD-isocitrate dehydrogenase from Pyrococcus furiosus. Arch Microbiol 178, 297–300 (2002). https://doi.org/10.1007/s00203-002-0439-x

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  • DOI: https://doi.org/10.1007/s00203-002-0439-x

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