EC Number |
Cofactor |
Reference |
---|
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 |