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Results 1 - 6 of 6
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EC Number Cofactor Commentary Reference
Display the word mapDisplay the reaction diagram Show all sequences 1.97.1.4Ferredoxin can partly substitute for flavodoxin 744943
Display the word mapDisplay the reaction diagram Show all sequences 1.97.1.4flavodoxin preferred cofactor 744943
Display the word mapDisplay the reaction diagram Show all sequences 1.97.1.4more reduced flavodoxin serves as an electron donor and SAM as a cosubstrate for PFL-AE to generate a 5'-deoxyadenosyl radical, which is responsible for PFL activation 744943
Display the word mapDisplay the reaction diagram Show all sequences 1.97.1.4S-adenosyl-L-methionine - 727665, 744943, 745316
Display the word mapDisplay the reaction diagram Show all sequences 1.97.1.4S-adenosyl-L-methionine pyruvate formate-lyase activating enzyme is a radical SAM enzyme. Conserved cysteines coordinate three irons of a [4Fe-4S] cluster, while SAM coordinates the fourth iron through its amino and carboxylate moieties 745175
Display the word mapDisplay the reaction diagram Show all sequences 1.97.1.4[4Fe-4S]-center an increase in pre-edge intensity is due to additional contributions from sulfide and thiolate of the Fe4S4 cluster into the C-S sigma* orbital. There is a backbonding interaction between the Fe4S4 cluster and C-S sigma* orbitals of S-adenosyl-L-methionine in this inner sphere complex. This backbonding is enhanced in the reduced form and this configurational interaction between the donor and acceptor orbitals facilitates the electron transfer from the cluster to S-adenosyl-L-methionine, that otherwise has a large outer sphere electron transfer barrier. The energy of the reductive cleavage of the C-S bond is sensitive to the dielectric of the protein in the immediate vicinity of the site as a high dielectric stabilizes the more charge separated reactant increasing the reaction barrier 727665
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