MDO Protein, Mycobacterium sp.

MDO (methanol dehydrogenase) is responsible for oxidizing methanol to produce formaldehyde. Although the in vivo electron acceptor remains unidentified, in vitro experiments indicate that N,N-dimethyl-4-nitrosaniline (NDMA) can serve as a suitable electron acceptor and is subsequently reduced to 4-(hydroxyamino) -N,N-Dimethylaniline. MDO Protein, Mycobacterium sp. is the recombinant MDO protein, expressed by E. coli , with tag free. The total length of MDO Protein, Mycobacterium sp. is 423 a.a., .

Methanol dehydrogenase (MDO) is an essential enzyme that catalyzes the oxidation of methanol to produce formaldehyde. While the specific in vivo electron acceptor remains unknown, in vitro studies have demonstrated the ability of N,N-dimethyl-4-nitrosoaniline (NDMA) to serve this function, being reduced to 4-(hydroxylamino)-N,N-dimethylaniline in the process. Remarkably, MDO exhibits versatility in substrate utilization, showcasing comparable activity with ethanol and formaldehyde as it does with methanol. Additionally, the enzyme displays weak activity with methylamine as a substrate. This broad substrate specificity suggests MDO's potential role in diverse metabolic pathways and highlights its adaptability in accommodating different alcohol and amine substrates, emphasizing its significance in cellular metabolism and the oxidation of various organic compounds (adapted from the provided passage).

Others

E. coli

Tag Free

C5MRT8 (M1-Y423)

/

Greater than 90% as determined by reducing SDS-PAGE.

<1 EU/μg, determined by LAL method.