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1993 (1)
1Author    Thomas Weber3, ThomasJ. BachbRequires cookie*
 Title    Partial Purification and Characterization of Membrane-Associated 3-Hydroxy-3-methylglutaryl-Coenzyme A Lyase from Radish Seedlings  
 Abstract    We solubilized from radish membranes and purified by 154-fold 3-hydroxy-3-methyl-glutaryl-CoA lyase (H M G L, EC catalyzing the conversion o f 3-hydroxy-3-methyl-glutaryl-(H M G -)C oA into acetyl-CoA and acetoacetate. The apparent molecular mass under non-denaturating conditions is 70 kDa. The enzyme has a broad pH optimum around 8.0 and its activation energy as determined from the linear part o f an Arrhenius plot is 137.1 kJ/mol. The K m with respect to (5)-H M G -C oA is 40 |iM . The enzyme is extremely unstable and rapidly loses activity even when kept on ice, but retains some activity over several weeks when stored at -8 0 °C. 
  Reference    Z. Naturforsch. 48c, 444 (1993); received March 12/April 13 1993 
  Published    1993 
  Keywords    Radish, Enzyme Purification, M evalonate Shunt, Leucine D egradation, H M G -C oA Synthesis, H M G -C oA M etabolism 
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 TEI-XML for    default:Reihe_C/48/ZNC-1993-48c-0444.pdf 
 Identifier    ZNC-1993-48c-0444 
 Volume    48