Methylamine dehydrogenase
From Proteopedia
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==3D structures of methylamine dehydrogenase== | ==3D structures of methylamine dehydrogenase== | ||
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[[1mda]], [[2j55]], [[2j56]], [[2j57]], [[3c75]] – PdMADH α + β + amicyanin – ''Paracoccus denitrificans''<br /> | [[1mda]], [[2j55]], [[2j56]], [[2j57]], [[3c75]] – PdMADH α + β + amicyanin – ''Paracoccus denitrificans''<br /> | ||
[[1mae]], [[1maf]], [[2bbk]], [[2mad]] – PdMADH α + β<br /> | [[1mae]], [[1maf]], [[2bbk]], [[2mad]] – PdMADH α + β<br /> | ||
[[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 | + | [[1mg2]], [[1mg3]], [[2gc4]] - PdMADH α (mutant) + β+ amicyanin + cytochrome c551i<br /> |
| + | [[3rn1]], [[3sle]], [[3svw]], [[3sws]], [[3sxt]], [[4k3i]] - PdMADH α + β + methylamine utilization protein<br /> | ||
| + | [[3sjl]] - PdMADH α + β (mutant) + methylamine utilization protein<br /> | ||
'''pre-MADH''' | '''pre-MADH''' | ||
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[[3l4m]], [[3l4o]] - PdMADH α + β (mutant) + MauG<br /> | [[3l4m]], [[3l4o]] - PdMADH α + β (mutant) + MauG<br /> | ||
[[3orv]] - PdMADH α + β (mutant) + MauG (mutant)<br /> | [[3orv]] - PdMADH α + β (mutant) + MauG (mutant)<br /> | ||
| - | [[3pxs]] - PdMADH α + β + MauG<br /> | + | [[3pxs]], [[4fa1]], [[4fa4]], [[4fa5]], [[4fa9]], [[4fan]], [[4fav]], [[4fb1]] - PdMADH α + β + MauG<br /> |
[[3pxt]] - PdMADH α + β + CO + MauG<br /> | [[3pxt]] - PdMADH α + β + CO + MauG<br /> | ||
[[3pxw]] - PdMADH α + β + NO + MauG<br /> | [[3pxw]] - PdMADH α + β + NO + MauG<br /> | ||
| - | [[3rlm]], [[3rmz]], [[3rn0]] - PdMADH α + β + MauG (mutant) | + | [[3rlm]], [[3rmz]], [[3rn0]], [[4l1q]], [[4l3g]], [[4l3h]] - PdMADH α + β + MauG (mutant) |
[[Category:Topic Page]] | [[Category:Topic Page]] | ||
Revision as of 09:47, 27 March 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 27-March-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 + methylamine utilization protein
3sjl - PdMADH α + β (mutant) + methylamine utilization protein
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)
