Methylamine dehydrogenase (MADH)

Methylamine dehydrogenase (MADH) is a periplasmic quinoprotein enzyme predominantly found in methylotrophic bacteria, where it is essential for the oxidation of methylamine to formaldehyde and ammonia [1, 2]. It typically functions as a heterotetramer composed of two heavy and two light subunits, with the light subunits containing a unique, post-translationally modified tryptophan tryptophylquinone (TTQ) cofactor [10]. The enzyme serves as a prominent model for studying long-range interprotein electron transfer, specifically between the TTQ center and its physiological electron acceptor, the blue copper protein amicyanin [14]. While MADH genes have been identified in certain human pathogens such as Porphyromonas gingivalis, the enzyme is not currently established as a therapeutic target for clinical drug development [4]. As a result, there are no approved drugs that target MADH, and it is not associated with any established clinical biomarkers or safety profiles in humans [1, 15].

Other names

Methylamine dehydrogenase (amicyanin)Amine dehydrogenasePrimary-amine dehydrogenaseMethylamine:(acceptor) oxidoreductase (deaminating)