Identification of enzymes homologous to isocitrate dehydrogenase that are involved in coenzyme B and leucine biosynthesis in methanoarchaea.

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  • Author(s): Howell DM;Howell DM; Graupner M; Xu H; White RH
  • Source:
    Journal of bacteriology [J Bacteriol] 2000 Sep; Vol. 182 (17), pp. 5013-6.
  • Publication Type:
    Journal Article; Research Support, U.S. Gov't, Non-P.H.S.
  • Language:
    English
  • Additional Information
    • Source:
      Publisher: American Society for Microbiology Country of Publication: United States NLM ID: 2985120R Publication Model: Print Cited Medium: Print ISSN: 0021-9193 (Print) Linking ISSN: 00219193 NLM ISO Abbreviation: J Bacteriol Subsets: MEDLINE
    • Publication Information:
      Original Publication: Washington, DC : American Society for Microbiology
    • Subject Terms:
      Alcohol Oxidoreductases/*metabolism ; Isocitrate Dehydrogenase/*metabolism ; Leucine/*biosynthesis ; Methanococcus/*enzymology ; Phosphothreonine/*analogs & derivatives; 3-Isopropylmalate Dehydrogenase ; Alcohol Oxidoreductases/genetics ; Cloning, Molecular ; Enzyme Stability ; Gene Expression ; Heating ; Heptanoic Acids/metabolism ; Isocitrate Dehydrogenase/genetics ; Methanococcus/genetics ; Phosphothreonine/metabolism ; Sulfhydryl Compounds/metabolism
    • Abstract:
      Two putative Methanococcus jannaschii isocitrate dehydrogenase genes, MJ1596 and MJ0720, were cloned and overexpressed in Escherichia coli, and their gene products were tested for the ability to catalyze the NAD- and NADP-dependent oxidative decarboxylation of DL-threo-3-isopropylmalic acid, threo-isocitrate, erythro-isocitrate, and homologs of threo-isocitrate. Neither enzyme was found to use any of the isomers of isocitrate as a substrate. The protein product of the MJ1596 gene, designated AksF, catalyzed the NAD-dependent decarboxylation of intermediates in the biosynthesis of 7-mercaptoheptanoic acid, a moiety of methanoarchaeal coenzyme B (7-mercaptoheptanylthreonine phosphate). These intermediates included (-)-threo-isohomocitrate [(-)-threo-1-hydroxy-1,2, 4-butanetricarboxylic acid], (-)-threo-iso(homo)(2)citrate [(-)-threo-1-hydroxy-1,2,5-pentanetricarboxylic acid], and (-)-threo-iso(homo)(3)citrate [(-)-threo-1-hydroxy-1,2, 6-hexanetricarboxylic acid]. The protein product of MJ0720 was found to be alpha-isopropylmalate dehydrogenase (LeuB) and was found to catalyze the NAD-dependent decarboxylation of one isomer of DL-threo-isopropylmalate to 2-ketoisocaproate; thus, it is involved in the biosynthesis of leucine. The AksF enzyme proved to be thermostable, losing only 10% of its enzymatic activity after heating at 100 degrees C for 10 min, whereas the LeuB enzyme lost 50% of its enzymatic activity after heating at 80 degrees C for 10 min.
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    • Accession Number:
      0 (Heptanoic Acids)
      0 (Sulfhydryl Compounds)
      104302-77-4 (7-mercaptoheptanoylthreonine phosphate)
      1114-81-4 (Phosphothreonine)
      52000-32-5 (7-mercaptoheptanoic acid)
      EC 1.1.- (Alcohol Oxidoreductases)
      EC 1.1.1.41 (Isocitrate Dehydrogenase)
      EC 1.1.1.85 (3-Isopropylmalate Dehydrogenase)
      GMW67QNF9C (Leucine)
    • Publication Date:
      Date Created: 20000812 Date Completed: 20000921 Latest Revision: 20210526
    • Publication Date:
      20231215
    • Accession Number:
      PMC111387
    • Accession Number:
      10.1128/JB.182.17.5013-5016.2000
    • Accession Number:
      10940051