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<center><b>Figure 2.</b>Protein molecular structures of trimethylamine dehydrogenase and it's mutation site. </center>
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<center><b>Figure 2.</b>Protein molecular structures of trimethylamine dehydrogenase and it's mutated site V344C. </center>
 
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Revision as of 03:35, 12 October 2022


Mutated TMADH

After expressing, it'll produce trimethylamine dehydrogenase (TMADH (EC 1.5.99.7)). The enzyme TMADH is an iron–sulfur flavoprotein which catalyses the oxidative demethylation of trimethylamine (TMA) to dimethylamine and formaldehyde:
(CH3)3N + H2O → (CH3)2NH + CH2O +2H+ + 2e-.

Metabolic Pathway

This enzyme is a complex iron-sulfur flavoprotein that transfers electrons to the soluble flavoprotein known as electron transferring flavoprotein. It couldn't work extracellular isolated.


Figure 1.Pathways for trimethylamine metabolism in bacteria.


Protein Molecular Structures

Trimethylamine dehydrogenase (TMADH) exist as dimers.


Figure 2.Protein molecular structures of trimethylamine dehydrogenase and it's mutated site V344C.



Sequence and Features

Sequence and Features


Assembly Compatibility:
  • 10
    INCOMPATIBLE WITH RFC[10]
    Illegal EcoRI site found at 388
    Illegal PstI site found at 183
    Illegal PstI site found at 1782
  • 12
    INCOMPATIBLE WITH RFC[12]
    Illegal EcoRI site found at 388
    Illegal PstI site found at 183
    Illegal PstI site found at 1782
  • 21
    INCOMPATIBLE WITH RFC[21]
    Illegal EcoRI site found at 388
    Illegal XhoI site found at 1717
  • 23
    INCOMPATIBLE WITH RFC[23]
    Illegal EcoRI site found at 388
    Illegal PstI site found at 183
    Illegal PstI site found at 1782
  • 25
    INCOMPATIBLE WITH RFC[25]
    Illegal EcoRI site found at 388
    Illegal PstI site found at 183
    Illegal PstI site found at 1782
    Illegal AgeI site found at 879
  • 1000
    COMPATIBLE WITH RFC[1000]