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Results 1 - 9 of 9
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EC Number Cofactor Commentary Reference
Show all pathways known for 4.1.1.47Display the word mapDisplay the reaction diagram Show all sequences 4.1.1.471,5-Dihydro-5-deaza-FADH2 reconstitution of the apoenzyme with 50% recovery of the ativity, Km: 0.00071 4584
Show all pathways known for 4.1.1.47Display the word mapDisplay the reaction diagram Show all sequences 4.1.1.475-deaza-FAD can reconstitute the apoenzyme to full activity, Km: 0.00074 mM 4584
Show all pathways known for 4.1.1.47Display the word mapDisplay the reaction diagram Show all sequences 4.1.1.47FAD - 705846
Show all pathways known for 4.1.1.47Display the word mapDisplay the reaction diagram Show all sequences 4.1.1.47FAD 1 mol of FAD per mol of dimer, Km: 0.00025 mM 4584
Show all pathways known for 4.1.1.47Display the word mapDisplay the reaction diagram Show all sequences 4.1.1.47FAD coenzyme 4584, 4586
Show all pathways known for 4.1.1.47Display the word mapDisplay the reaction diagram Show all sequences 4.1.1.47thiamine diphosphate - 705846
Show all pathways known for 4.1.1.47Display the word mapDisplay the reaction diagram Show all sequences 4.1.1.47thiamine diphosphate cofactor 4585
Show all pathways known for 4.1.1.47Display the word mapDisplay the reaction diagram Show all sequences 4.1.1.47thiamine diphosphate dependent on 4586, 727003
Show all pathways known for 4.1.1.47Display the word mapDisplay the reaction diagram Show all sequences 4.1.1.47thiamine diphosphate the structure of glyoxylate carboligase reveals that there is no glutamate in a position to interact with N1’ of thiamine diphosphate, the position homologous to the conserved glutamate is occupied by Val51 703643
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