The reaction of mitochondrial L-3-glycerophosphate dehydrogenase with various electron acceptors.
1. The kinetics of the reaction of glycerophosphate dehydrogenase with a variety of electron acceptors have been investigated. 2. In all cases the reaction mechanism appears to involve a free modified-enzyme intermediate. 3. With some electron acceptors, the maximum velocity of the reaction and the K(m) for glycerophosphate are independent of the nature of the electron acceptor, whereas in other cases this is not so. 4. The reaction mechanism of the enzyme extracted with phospholipase A instead of with Triton X-100 is of a similar type.
D004579:Electron Transport; D005993:Glycerolphosphate Dehydrogenase; D007097:Imines; D007700:Kinetics; D008928:Mitochondria / Q000201:enzymology*; D010619:Phenazines; D011809:Quinones; D013501:Surface-Active Agents; D014451:Ubiquinone; D014812:Vitamin K
D007097:Imines; D010619:Phenazines; D011809:Quinones; D013501:Surface-Active Agents; D014812:Vitamin K; D014451:Ubiquinone; D005993:Glycerolphosphate Dehydrogenase