These tools will no longer be maintained as of December 31, 2024. Archived website can be found here. PubMed4Hh GitHub repository can be found here. Contact NLM Customer Service if you have questions.


Pubmed for Handhelds

PUBMED FOR HANDHELDS

Search MEDLINE/PubMed

  • Title: The genes for anabolic 2-oxoglutarate: ferredoxin oxidoreductase from Hydrogenobacter thermophilus TK-6.
    Author: Yun NR, Arai H, Ishii M, Igarashi Y.
    Journal: Biochem Biophys Res Commun; 2001 Mar 30; 282(2):589-94. PubMed ID: 11401501.
    Abstract:
    2-Oxoglutarate: ferredoxin oxidoreductase (OGOR) of a thermophilic, chemolithoautotrophic hydrogen-oxidizing bacterium, Hydrogenobacter thermophilus TK-6, is involved in carbon dioxide fixation via a reductive TCA cycle. The enzyme is a heterodimer comprising subunits of 70 and 35 kDa. The structural genes for the subunits (korAB) were cloned with primers designed from N-terminal sequences of the purified enzyme. The korAB genes were followed by two open reading frames of unknown function (orf3 and orf4). KorA carried a binding motif for coenzyme A, and KorB carried binding motifs for Fe-S cluster and thiamine pyrophosphate. Active recombinant enzyme from korAB was produced in E. coli under the control of the lac promoter. orf3 and orf4 were not necessary for the expression of active enzyme in E. coli. The recombinant enzymes had high substrate specificity toward 2-oxoglutarate as in the case of the native enzyme purified from strain TK-6.
    [Abstract] [Full Text] [Related] [New Search]