Kinetic mechanism of glutaryl-CoA dehydrogenase |
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Authors: | Rao K Sudhindra Albro Mark Dwyer Timothy M Frerman Frank E |
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Institution: | Department of Pediatrics, University of Colorado at Denver and Health Sciences Center, 12800 East Nineteenth Avenue, P18-4404B, Mail Stop 8313, P.O. Box 6511, Aurora, Colorado 80045-0511, USA. |
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Abstract: | Glutaryl-CoA dehydrogenase (GCD) is a homotetrameric enzyme containing one noncovalently bound FAD per monomer that oxidatively decarboxylates glutaryl-CoA to crotonyl-CoA and CO2. GCD belongs to the family of acyl-CoA dehydrogenases that are evolutionarily conserved in their sequence, structure, and function. However, there are differences in the kinetic mechanisms among the different acyl-CoA dehydrogenases. One of the unanswered aspects is that of the rate-determining step in the steady-state turnover of GCD. In the present investigation, the major rate-determining step is identified to be the release of crotonyl-CoA product because the chemical steps and reoxidation of reduced FAD are much faster than the turnover of the wild-type GCD. Other steps are only partially rate-determining. This conclusion is based on the transit times of the individual reactions occurring in the active site of GCD. |
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