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 (orange), [[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]] }} | ||
| - | + | == Function == | |
| - | + | '''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<ref>PMID:3558322</ref>. | |
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| - | + | == Structural highlights == | |
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| - | '''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== | ==3D structures of methylamine dehydrogenase== | ||
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**[[3rlm]], [[3rmz]], [[3rn0]], [[4l1q]], [[4l3g]], [[4l3h]] - PdMADH α + β + MauG (mutant) | **[[3rlm]], [[3rmz]], [[3rn0]], [[4l1q]], [[4l3g]], [[4l3h]] - PdMADH α + β + MauG (mutant) | ||
}} | }} | ||
| + | == References == | ||
| + | <references/> | ||
[[Category:Topic Page]] | [[Category:Topic Page]] | ||
Revision as of 09:32, 24 April 2016
Contents |
Function
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[1].
Structural highlights
3D structures of methylamine dehydrogenase
Updated on 24-April-2016
References
- ↑ Husain M, Davidson VL. Purification and properties of methylamine dehydrogenase from Paracoccus denitrificans. J Bacteriol. 1987 Apr;169(4):1712-7. PMID:3558322
