Partial Purification and Characterization of Glutaryl-Coenzyme A Dehydrogenase, Electron Transfer Flavoprotein, and Electron Transfer Flavoprotein-Q Oxidoreductase from Paracoccus denitrificans :

1986 ◽  
Vol 166 (2) ◽  
pp. 698.3-698
Keyword(s):  
Electron Transfer ◽  
Coenzyme A ◽  
Paracoccus Denitrificans ◽  
Partial Purification ◽  
Purification And Characterization ◽  
Electron Transfer Flavoprotein

Partial Purification and Characterization of Membrane-Associated 3-Hydroxy-3-methylglutaryl-Coenzyme A Lyase from Radish Seedlings

1993 ◽  
Vol 48 (5-6) ◽  
pp. 444-450 ◽  
Author(s):  
Thomas Weber ◽  
Thomas J. Bach
Keyword(s):  
Activation Energy ◽  
Molecular Mass ◽  
Coenzyme A ◽  
Arrhenius Plot ◽  
Linear Part ◽  
Partial Purification ◽  
Purification And Characterization ◽  
Ph Optimum ◽  
Radish Seedlings

Abstract We solubilized from radish membranes and purified by 154-fold 3-hydroxy-3-methyl-glutaryl-CoA lyase (HMGL, EC 4.1.3.4) catalyzing the conversion of 3-hydroxy-3-methyl-glutaryl-(HMG -)CoA 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 of an Arrhenius plot is 137.1 kJ/mol. The Km with respect to (5)-H MG-CoA is 40 μM . The enzyme is extremely unstable and rapidly loses activity even when kept on ice, but retains some activity over several weeks when stored at -80 °C.

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