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Results 1 - 10 of 16 > >>
EC Number Cofactor Commentary Reference
Show all pathways known for 1.5.8.4Display the word mapDisplay the reaction diagram Show all sequences 1.5.8.4FAD - 392527, 741817, 742499
Show all pathways known for 1.5.8.4Display the word mapDisplay the reaction diagram Show all sequences 1.5.8.4FAD A280/A450 ratios of the highly pure protein fractions are between 14-16 and 20-25 for wild-type and mutant H109R, respectively. The redox potential for the reduction of FAD is -93 mV 742499
Show all pathways known for 1.5.8.4Display the word mapDisplay the reaction diagram Show all sequences 1.5.8.4FAD absolutely required, covalently bound to the apoenzyme via a histidinyl(N3)-(8alpha)FAD linkage, cofactor-free apoenzyme shows 70% reduced activity compared to the holoenzyme 657277
Show all pathways known for 1.5.8.4Display the word mapDisplay the reaction diagram Show all sequences 1.5.8.4FAD covalent attachment of FAD to the apoenzyme proceeds in vitro spontaneously and does not require a mitochondrial protein factor 392526
Show all pathways known for 1.5.8.4Display the word mapDisplay the reaction diagram Show all sequences 1.5.8.4FAD covalently bound 392496, 392497, 392498, 392499, 392500, 392501, 392520, 392524, 392525, 392526
Show all pathways known for 1.5.8.4Display the word mapDisplay the reaction diagram Show all sequences 1.5.8.4FAD FAD is covalently bound via an autocatalytic reaction 687135
Show all pathways known for 1.5.8.4Display the word mapDisplay the reaction diagram Show all sequences 1.5.8.4FAD flavoprotein 742499
Show all pathways known for 1.5.8.4Display the word mapDisplay the reaction diagram Show all sequences 1.5.8.4FAD mitochondrial matrix can stimulate the flavinylation of the enzyme synthesized in rabbit reticulocyte lysate as well as the 6-His-tagged enzyme purified by affinity chromatography, a matrix protein factor accelerates holoenzyme formation of dimethylglycine dehydrogenase, the matrix protein factor is different from the mitochondrial chaperones Hsp60 and Hsp 70 392527
Show all pathways known for 1.5.8.4Display the word mapDisplay the reaction diagram Show all sequences 1.5.8.4FAD noncovalently bound flavin adenine dinucleotide, purified protein shows the absorption spectrum of an oxidized flavoprotein, with maxima at 222, 275, 370, and 440 nm and one shoulder at around 470 nm 763963
Show all pathways known for 1.5.8.4Display the word mapDisplay the reaction diagram Show all sequences 1.5.8.4FAD the precursor form of the enzyme is a good substrate for mitochondria-assisted flavinylation reaction, flavinylation of precursor precedes polypeptide processing by the mitochondrial processing peptidase during the biogenesis of holo-enzyme 392528
Results 1 - 10 of 16 > >>