Isolation, characterization, and physiological role of the pyruvate dehydrogenase complex and alpha-acetolactate synthase of Lactococcus lactis subsp. lactis bv. diacetylactis.

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  • 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:
      Acetolactate Synthase/*metabolism ; Lactococcus lactis/*enzymology ; Pyruvate Dehydrogenase Complex/*metabolism; Acetolactate Synthase/isolation & purification ; Cations, Divalent/metabolism ; Chromatography, High Pressure Liquid ; Kinetics ; NAD/metabolism ; Pyruvate Dehydrogenase Complex/isolation & purification ; Pyruvates/metabolism ; Pyruvic Acid ; Thiamine Pyrophosphate/metabolism
    • Abstract:
      The pyruvate dehydrogenase complex of Lactococcus lactis subsp. lactis bv. diacetylactis has a specific activity of 6.6 U/mg and a Km of 1 mM for pyruvate. The specific activities of E2 and E3 in the complex are 30 and 0.36 U/mg, respectively. The complex is very sensitive to NADH inhibition and consists of four subunits: E1 alpha (44 kDa), E1 beta (35 kDa), E2 (73 kDa), and E3 (60 kDa). The L. lactis alpha-acetolactate synthase has a specific activity of 103 U/mg and a Km of 50 mM for pyruvate. Thiamine pyrophosphate (Km = 3.2 microM) and divalent cations are essential for activity. The native enzyme measures 172 kDa and consists of 62-kDa monomers. The role of both enzymes in product formation is discussed in view of NADH inhibition and competition for pyruvate.
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    • Accession Number:
      0 (Cations, Divalent)
      0 (Pyruvate Dehydrogenase Complex)
      0 (Pyruvates)
      0U46U6E8UK (NAD)
      8558G7RUTR (Pyruvic Acid)
      EC 2.2.1.6 (Acetolactate Synthase)
      Q57971654Y (Thiamine Pyrophosphate)
    • Publication Date:
      Date Created: 19920701 Date Completed: 19920813 Latest Revision: 20190508
    • Publication Date:
      20221213
    • Accession Number:
      PMC206284
    • Accession Number:
      10.1128/jb.174.14.4838-4841.1992
    • Accession Number:
      1624471