Methylamine dehydrogenase

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Contents 1 Function 2 Structural highlights 3 3D structures of methylamine dehydrogenase 4 References

Function

Methylamine dehydrogenase (MADH) catalyzes the oxidative deamination of primary amine to aldehyde and ammonia, in particular, the conversion of methylamine to formaldehyde. MADH is tryptophan tryptophyl-quinone (TTQ) dependent. MADH is a heterotetramer containing heavy (α) and light (β) subunits. Each β subunit contains a TTQ prosthetic group. The posttranslational modification of two tryptophan residues to form the TTQ cofactor of MADH is catalyzed by methylation utilization protein (MauG). MADH forms a complex with cytochrome c-551i. In the complex, electrons are transferred from TTQ via the amicyanin copper ion center to the heme group of cytochrome^[1].

Structural highlights

3D structures of methylamine dehydrogenase

Updated on 24-April-2016

References

1. ↑ Husain M, Davidson VL. Purification and properties of methylamine dehydrogenase from Paracoccus denitrificans. J Bacteriol. 1987 Apr;169(4):1712-7. PMID:3558322