Methylamine dehydrogenase
From Proteopedia
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| - | + | *Methylamine dehydrogenase | |
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| - | + | **[[1mda]], [[2j55]], [[2j56]], [[2j57]], [[3c75]] – PdMADH α + β + amicyanin – ''Paracoccus denitrificans''<br /> | |
| + | **[[1mae]], [[1maf]], [[2bbk]], [[2mad]] – PdMADH α + β<br /> | ||
| + | **[[2mta]], [[2gc7]] - PdMADH α + 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 /> | ||
| + | **[[3sjl]] - PdMADH α + β (mutant) + MauG<br /> | ||
| - | + | *pre-MADH | |
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| + | **[[3l4m]], [[3l4o]] - PdMADH α + β (mutant) + MauG<br /> | ||
| + | **[[3orv]] - PdMADH α + β (mutant) + MauG (mutant)<br /> | ||
| + | **[[3pxs]], [[4fa1]], [[4fa4]], [[4fa5]], [[4fa9]], [[4fan]], [[4fav]], [[4fb1]] - PdMADH α + β + MauG<br /> | ||
| + | **[[3pxt]] - PdMADH α + β + CO + MauG<br /> | ||
| + | **[[3pxw]] - PdMADH α + β + NO + MauG<br /> | ||
| + | **[[3rlm]], [[3rmz]], [[3rn0]], [[4l1q]], [[4l3g]], [[4l3h]] - PdMADH α + β + MauG (mutant) | ||
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[[Category:Topic Page]] | [[Category:Topic Page]] | ||
Revision as of 09:26, 1 December 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 01-December-2014
