Methylamine dehydrogenase
From Proteopedia
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[[3sjl]] - PdMADH α + β (mutant) + MauG<br /> | [[3sjl]] - PdMADH α + β (mutant) + MauG<br /> | ||
| - | + | ===pre-MADH=== | |
[[3l4m]], [[3l4o]] - PdMADH α + β (mutant) + MauG<br /> | [[3l4m]], [[3l4o]] - PdMADH α + β (mutant) + MauG<br /> | ||
Revision as of 06:49, 2 September 2014
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 02-September-2014
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
3rn1, 3sle, 3svw, 3sws, 3sxt, 4k3i - PdMADH α + β + MauG
3sjl - PdMADH α + β (mutant) + MauG
pre-MADH
3l4m, 3l4o - PdMADH α + β (mutant) + MauG
3orv - PdMADH α + β (mutant) + MauG (mutant)
3pxs, 4fa1, 4fa4, 4fa5, 4fa9, 4fan, 4fav, 4fb1 - PdMADH α + β + MauG
3pxt - PdMADH α + β + CO + MauG
3pxw - PdMADH α + β + NO + MauG
3rlm, 3rmz, 3rn0, 4l1q, 4l3g, 4l3h - PdMADH α + β + MauG (mutant)
