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Results 1 - 9 of 9
EC Number Cofactor Commentary Reference
Show all pathways known for 1.1.99.1Display the word mapDisplay the reaction diagram Show all sequences 1.1.99.1coenzyme Q primary electron acceptor in vivo 389886
Show all pathways known for 1.1.99.1Display the word mapDisplay the reaction diagram Show all sequences 1.1.99.1FAD - 654440, 699705
Show all pathways known for 1.1.99.1Display the word mapDisplay the reaction diagram Show all sequences 1.1.99.1more FAD and pyrroloquinoline quinone has no effect on activity 654268
Show all pathways known for 1.1.99.1Display the word mapDisplay the reaction diagram Show all sequences 1.1.99.1more oxygen is not the preferred electron acceptor even though the enzyme is able to utilize it. Phenazine methosulfate can act as artificial cofactor. Cytochrome c and ferricyanide give poor activity 741756
Show all pathways known for 1.1.99.1Display the word mapDisplay the reaction diagram Show all sequences 1.1.99.1more the enzyme has 3 functional domains, named FAD/NAD(P)-binding domain 1 (FB1, residues 39 to 326), FAD-linked reductase domain (RD, residues 333 to 515) and FAD/NAD(P)-binding domain 2 (FB2, residues 511 to 574) 741800
Show all pathways known for 1.1.99.1Display the word mapDisplay the reaction diagram Show all sequences 1.1.99.1more the enzyme requires no readily dissociable coenzyme for activity 389884, 389887
Show all pathways known for 1.1.99.1Display the word mapDisplay the reaction diagram Show all sequences 1.1.99.1phenazine methosulfate - 725104, 726473
Show all pathways known for 1.1.99.1Display the word mapDisplay the reaction diagram Show all sequences 1.1.99.1pyrroloquinoline quinone - 389890
Show all pathways known for 1.1.99.1Display the word mapDisplay the reaction diagram Show all sequences 1.1.99.1pyrroloquinoline quinone as prosthetic group 389883
Results 1 - 9 of 9