EC Number |
Cofactor |
Reference |
---|
1.5.8.4 | FAD |
covalently bound |
392496, 392497, 392498, 392499, 392500, 392501, 392520, 392524, 392525, 392526 |
1.5.8.4 | Tetrahydropteroylpentaglutamate |
- |
392496, 392500, 392516, 392520, 392526 |
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 |
- |
392527, 741817, 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 |
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 |
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 | more |
1-methoxy-5-methylphenazinium methylsulfate can act as electron acceptor |
657277 |
1.5.8.4 | more |
2,6-dichlorophenolindophenol can act as electron acceptor |
657277 |
1.5.8.4 | FAD |
FAD is covalently bound via an autocatalytic reaction |
687135 |