Methylamine dehydrogenase
From Proteopedia
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| + | <StructureSection load='2bbq' size='350' side='right' 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) (PDB entry [[2pm4]])' scene=''> | ||
== Function == | == 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>. | + | '''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 2 heavy (α) and 2 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>. |
== Structural highlights == | == Structural highlights == | ||
| - | + | </StructureSection> | |
==3D structures of methylamine dehydrogenase== | ==3D structures of methylamine dehydrogenase== | ||
Revision as of 06:42, 25 April 2016
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3D structures of methylamine dehydrogenase
Updated on 25-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
