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− | <center><b>Figure 2.</b>Protein molecular structures of trimethylamine dehydrogenase and it's | + | <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.
Protein Molecular Structures
Trimethylamine dehydrogenase (TMADH) exist as dimers.
Sequence and Features
Sequence and Features
Assembly Compatibility:
- 10INCOMPATIBLE WITH RFC[10]Illegal EcoRI site found at 388
Illegal PstI site found at 183
Illegal PstI site found at 1782 - 12INCOMPATIBLE WITH RFC[12]Illegal EcoRI site found at 388
Illegal PstI site found at 183
Illegal PstI site found at 1782 - 21INCOMPATIBLE WITH RFC[21]Illegal EcoRI site found at 388
Illegal XhoI site found at 1717 - 23INCOMPATIBLE WITH RFC[23]Illegal EcoRI site found at 388
Illegal PstI site found at 183
Illegal PstI site found at 1782 - 25INCOMPATIBLE 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 - 1000COMPATIBLE WITH RFC[1000]