Methylamine dehydrogenase

spinqualitylabelsall models Methylamine dehydrogenase tetramer: 2 heavy chains (salmon and blue) and 2 light chains (green and yellow) complex with tryptophylquinone (TTQ) (PDB entry 2bbk) Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D 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 in preMADH 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. Structural highlights The MADH unique redox center TTQ cofactor is located in the light subunit. Whole redox center.

3D structures of methylamine dehydrogenase

Updated on 11-July-2019

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• Methylamine dehydrogenase
  • 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, 4o1q, 4y5r - PdMADH α + β + MauG
    
  • 3sjl - PdMADH α + β (mutant) + MauG
    
• 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)

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