Difference between revisions of "Part:BBa K1813005"

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By reducing the nitro moiety, it minimizes toxic effects stemming from the presence of the imidazolidine moiety post cleavage.
 
By reducing the nitro moiety, it minimizes toxic effects stemming from the presence of the imidazolidine moiety post cleavage.
  
<h2> References <h2>
+
<h2> References </h2>
  
 
[1] Casida, J. E. (2010). Neonicotinoid metabolism: compounds, substituents, pathways, enzymes, organisms, and relevance. Journal of agricultural and food chemistry, 59(7), 2923-2931.
 
[1] Casida, J. E. (2010). Neonicotinoid metabolism: compounds, substituents, pathways, enzymes, organisms, and relevance. Journal of agricultural and food chemistry, 59(7), 2923-2931.

Revision as of 03:08, 18 September 2015

CYP2D6

HUMCYPDB1, or more accurately CYP2D6 is a cytochrome p450 enzyme known to metabolize a large range of compounds, through O-demethylation.

Sequence and Features


Assembly Compatibility:
  • 10
    COMPATIBLE WITH RFC[10]
  • 12
    COMPATIBLE WITH RFC[12]
  • 21
    INCOMPATIBLE WITH RFC[21]
    Illegal BglII site found at 323
  • 23
    COMPATIBLE WITH RFC[23]
  • 25
    INCOMPATIBLE WITH RFC[25]
    Illegal NgoMIV site found at 913
  • 1000
    COMPATIBLE WITH RFC[1000]


Background of HUMCYPDB1 / CYP2D6

As an active participant of the metabolism of more than 25% of the drugs that we take as humans, it's almost no surprise that it is capable of metabolising imidacloprid as well. It is surprising to note however, that imidacloprid is metabolized through the reduction of the nitro goup on the imidazolidine moiety [1], lowering the toxic effects of imidacloprid. In conjunction with CYP6CM1vQ and CYP6G1, it can minimize the toxicity of imidacloprid prior to spontaneous cleavage between the imidazolidine and nicotic moieties[1]. By reducing the nitro moiety, it minimizes toxic effects stemming from the presence of the imidazolidine moiety post cleavage.

References

[1] Casida, J. E. (2010). Neonicotinoid metabolism: compounds, substituents, pathways, enzymes, organisms, and relevance. Journal of agricultural and food chemistry, 59(7), 2923-2931.