Methylamine dehydrogenase
From Proteopedia
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**[[2mta]], [[2gc7]] - PdMADH α + β + amicyanin + cytochrome c551i<br /> | **[[2mta]], [[2gc7]] - PdMADH α + β + amicyanin + cytochrome c551i<br /> | ||
**[[1mg2]], [[1mg3]], [[2gc4]] - PdMADH α (mutant) + β+ amicyanin + cytochrome c551i<br /> | **[[1mg2]], [[1mg3]], [[2gc4]] - PdMADH α (mutant) + β+ amicyanin + cytochrome c551i<br /> | ||
| - | **[[3rn1]], [[3sle]], [[3svw]], [[3sws]], [[3sxt]], [[4k3i]] - PdMADH α + β + MauG<br /> | + | **[[3rn1]], [[3sle]], [[3svw]], [[3sws]], [[3sxt]], [[4k3i]], [[4o1q]] - PdMADH α + β + MauG<br /> |
**[[3sjl]] - PdMADH α + β (mutant) + MauG<br /> | **[[3sjl]] - PdMADH α + β (mutant) + MauG<br /> | ||
Revision as of 09:16, 5 May 2015
Template:STRUCTURE 2j55 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.
3D structures of methylamine dehydrogenase
Updated on 05-May-2015
