Methylamine dehydrogenase
From Proteopedia
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| - | {{STRUCTURE_2j55 | PDB=2j55 | SIZE=400 | SCENE= | CAPTION=Methylamine dehydrogenase dimer: heavy chain (red and blue) and light chain (olive and aqua) complex with amicyanin (grey and green), tryptophylquinone and Cu+2 ion, [[2j55]] }} | + | {{STRUCTURE_2j55 | PDB=2j55 | SIZE=400 | SCENE= | CAPTION=Methylamine dehydrogenase dimer: heavy chain (red and blue) and light chain (olive and aqua) complex with amicyanin (grey and green), tryptophylquinone and Cu+2 ion (orange), [[2j55]] }} |
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Revision as of 10:51, 22 December 2013
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
1mda, 2j55, 2j56, 2j57, 3c75 – PdMADH α + β + amicyanin – Paracoccus denitrificans
1mae, 1maf, 2bbk, 2mad – PdMADH α + β
2mta, 2gc7 - PdMADH α + β + amicyanin + cytochrome c551i
1mg2, 1mg3, 2gc4 - PdMADH α (mutant) + β+ amicyanin + cytochrome c551i
pre-MADH
3l4m, 3l4o - PdMADH α + β (mutant) + MauG
3orv - PdMADH α + β (mutant) + MauG (mutant)
3pxs - PdMADH α + β + MauG
3pxt - PdMADH α + β + CO + MauG
3pxw - PdMADH α + β + NO + MauG
3rlm, 3rmz, 3rn0 - PdMADH α + β + MauG (mutant)
