Methylamine dehydrogenase

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<StructureSection load='2bbk' 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=''>
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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=''>
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== 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 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>.
'''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>.

Revision as of 06:44, 25 April 2016

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)

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3D structures of methylamine dehydrogenase

Updated on 25-April-2016

References

  1. ↑ Husain M, Davidson VL. Purification and properties of methylamine dehydrogenase from Paracoccus denitrificans. J Bacteriol. 1987 Apr;169(4):1712-7. PMID:3558322

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Michal Harel, Alexander Berchansky, Joel L. Sussman

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