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Comparison of isocitrate dehydrogenase from three hyperthermophiles reveals differences in thermostability, cofactor specificity, oligomeric state, and phylogenetic affiliation.
J Biol Chem. 2001 Nov 23; 276(47):43924-31.JB

Abstract

With the aim of gaining insight into the molecular and phylogenetic relationships of isocitrate dehydrogenase (IDH) from hyperthermophiles, we carried out a comparative study of putative IDHs identified in the genomes of the eubacterium Thermotoga maritima and the archaea Aeropyrum pernix and Pyrococcus furiosus. An optimum for activity at 90 degrees C or above was found for each IDH. PfIDH and ApIDH were the most thermostable with a melting temperature of 103.7 and 109.9 degrees C, respectively, compared with 98.3 and 98.5 degrees C for TmIDH and AfIDH, respectively. Analytical ultracentrifugation revealed a tetrameric oligomeric state for TmIDH and a homodimeric state for ApIDH and PfIDH. TmIDH and ApIDH were NADP-dependent (K(m)((NADP)) of 55.2 and 44.4 microm, respectively) whereas PfIDH was NAD-dependent (K(m)((NAD)) of 68.3 microm). These data document that TmIDH represents a novel tetrameric NADP-dependent form of IDH and that PfIDH is a homodimeric NAD-dependent IDH not previously found among the archaea. The homodimeric NADP-IDH present in A. pernix is the most common form of IDH known so far. The evolutionary relationships of ApIDH, PfIDH, and TmIDH with all of the available amino acid sequences of di- and multimeric IDHs are described and discussed.

Authors+Show Affiliations

Department of Microbiology, University of Bergen, P. O. Box 7800, Jahnebakken 5, N-5020 Bergen, Norway.No affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info available

Pub Type(s)

Comparative Study
Journal Article

Language

eng

PubMed ID

11533060

Citation

Steen, I H., et al. "Comparison of Isocitrate Dehydrogenase From Three Hyperthermophiles Reveals Differences in Thermostability, Cofactor Specificity, Oligomeric State, and Phylogenetic Affiliation." The Journal of Biological Chemistry, vol. 276, no. 47, 2001, pp. 43924-31.
Steen IH, Madern D, Karlström M, et al. Comparison of isocitrate dehydrogenase from three hyperthermophiles reveals differences in thermostability, cofactor specificity, oligomeric state, and phylogenetic affiliation. J Biol Chem. 2001;276(47):43924-31.
Steen, I. H., Madern, D., Karlström, M., Lien, T., Ladenstein, R., & Birkeland, N. K. (2001). Comparison of isocitrate dehydrogenase from three hyperthermophiles reveals differences in thermostability, cofactor specificity, oligomeric state, and phylogenetic affiliation. The Journal of Biological Chemistry, 276(47), 43924-31.
Steen IH, et al. Comparison of Isocitrate Dehydrogenase From Three Hyperthermophiles Reveals Differences in Thermostability, Cofactor Specificity, Oligomeric State, and Phylogenetic Affiliation. J Biol Chem. 2001 Nov 23;276(47):43924-31. PubMed PMID: 11533060.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Comparison of isocitrate dehydrogenase from three hyperthermophiles reveals differences in thermostability, cofactor specificity, oligomeric state, and phylogenetic affiliation. AU - Steen,I H, AU - Madern,D, AU - Karlström,M, AU - Lien,T, AU - Ladenstein,R, AU - Birkeland,N K, Y1 - 2001/08/31/ PY - 2001/9/5/pubmed PY - 2002/1/5/medline PY - 2001/9/5/entrez SP - 43924 EP - 31 JF - The Journal of biological chemistry JO - J. Biol. Chem. VL - 276 IS - 47 N2 - With the aim of gaining insight into the molecular and phylogenetic relationships of isocitrate dehydrogenase (IDH) from hyperthermophiles, we carried out a comparative study of putative IDHs identified in the genomes of the eubacterium Thermotoga maritima and the archaea Aeropyrum pernix and Pyrococcus furiosus. An optimum for activity at 90 degrees C or above was found for each IDH. PfIDH and ApIDH were the most thermostable with a melting temperature of 103.7 and 109.9 degrees C, respectively, compared with 98.3 and 98.5 degrees C for TmIDH and AfIDH, respectively. Analytical ultracentrifugation revealed a tetrameric oligomeric state for TmIDH and a homodimeric state for ApIDH and PfIDH. TmIDH and ApIDH were NADP-dependent (K(m)((NADP)) of 55.2 and 44.4 microm, respectively) whereas PfIDH was NAD-dependent (K(m)((NAD)) of 68.3 microm). These data document that TmIDH represents a novel tetrameric NADP-dependent form of IDH and that PfIDH is a homodimeric NAD-dependent IDH not previously found among the archaea. The homodimeric NADP-IDH present in A. pernix is the most common form of IDH known so far. The evolutionary relationships of ApIDH, PfIDH, and TmIDH with all of the available amino acid sequences of di- and multimeric IDHs are described and discussed. SN - 0021-9258 UR - https://www.unboundmedicine.com/medline/citation/11533060/Comparison_of_isocitrate_dehydrogenase_from_three_hyperthermophiles_reveals_differences_in_thermostability_cofactor_specificity_oligomeric_state_and_phylogenetic_affiliation_ L2 - http://www.jbc.org/cgi/pmidlookup?view=long&pmid=11533060 DB - PRIME DP - Unbound Medicine ER -