1.5.8.4	FAD	-	392527, 741817, 742499	
1.5.8.4	FAD	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	
1.5.8.4	FAD	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	
1.5.8.4	FAD	covalent attachment of FAD to the apoenzyme proceeds in vitro spontaneously and does not require a mitochondrial protein factor	392526	
1.5.8.4	FAD	covalently bound	392496, 392497, 392498, 392499, 392500, 392501, 392520, 392524, 392525, 392526	
1.5.8.4	FAD	FAD is covalently bound via an autocatalytic reaction	687135	
1.5.8.4	FAD	flavoprotein	742499	
1.5.8.4	FAD	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	
1.5.8.4	FAD	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	
1.5.8.4	FAD	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