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: Thermostable, ammonium-activated malic enzyme of Clostridium thermocellum.
    Author: Lamed R, Zeikus JG.
    Journal: Biochim Biophys Acta; 1981 Aug 13; 660(2):251-5. PubMed ID: 7284402.
    Abstract:
    "Malic" enzyme (L-malate:NADP+ oxidoreductase (oxaloacetate-decarboxylating, EC 1.1.1.40) was purified from Clostridium thermocellum by DEAE-cellulose, agarose-NADP and Sephadex G-200 column chromatography. The 117-fold purified "malic" enzyme displayed a maximum activity of 135 units/mg at 40 degrees C and represented 0.8% of the total cell protein. Sodium dodecyl sulfate (SDS)-polyacrylamide gel electrophoresis analysis of the protein suggested 90% purity and an approximate tetrameric subunit molecular weight of 40 000. The enzyme absolutely required both bivalent and monovalent cations for catalysis. Mn2+ and NH4+ were the most effective cationic activators examined. Increasing NH4+ concentration increased both enzyme activity and affinity toward L-malate. The apparent Km for L-malate was 3 X 10(-4) M at 0.4 mM NH4Cl. Enzyme activity increased linearly when temperature was raised between 22-60 degrees C and a Q10 of 2.1 was calculated from an Arrhenius plot. The enzyme was stable at heating at 60 degrees C but was denatured at higher temperatures. The enzyme half-life was 10 min at 72 degrees C. The enzyme displayed a broad pH optimum (7.2-87.2 for Tris-HCl buffer) but was inactivated by p-chloromercuribenzoate. The high thermal stability, low apparent molecular weight and NH4+ activation are properties not common to all previously described "malic" enzymes.
    [Abstract] [Full Text] [Related] [New Search]