Difference between revisions of "Part:BBa K5477019"

 
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CYP1A1 (Cytochrome P450 1A1) is a vital enzyme in the cytochrome P450 family that primarily metabolizes environmental toxins, including polycyclic aromatic hydrocarbons (PAHs), dioxins, and polychlorinated biphenyls (PCBs). Predominantly expressed in the lungs and liver, CYP1A1 plays a key role in phase I metabolism, where it oxidizes hydrophobic compounds, rendering them more polar and easier to excrete. CYP1A1 catalyzes the incorporation of an oxygen atom into its substrates, producing reactive intermediates that are often further processed by phase II enzymes like UGT1A1 through glucuronidation. By metabolizing these carcinogenic and mutagenic compounds, CYP1A1 helps protect the body from toxic environmental exposures (1).
 
CYP1A1 (Cytochrome P450 1A1) is a vital enzyme in the cytochrome P450 family that primarily metabolizes environmental toxins, including polycyclic aromatic hydrocarbons (PAHs), dioxins, and polychlorinated biphenyls (PCBs). Predominantly expressed in the lungs and liver, CYP1A1 plays a key role in phase I metabolism, where it oxidizes hydrophobic compounds, rendering them more polar and easier to excrete. CYP1A1 catalyzes the incorporation of an oxygen atom into its substrates, producing reactive intermediates that are often further processed by phase II enzymes like UGT1A1 through glucuronidation. By metabolizing these carcinogenic and mutagenic compounds, CYP1A1 helps protect the body from toxic environmental exposures (1).
  
In our system, CYP1A1 is integrated into a detoxification module where it initiates the oxidative breakdown of harmful pollutants, enabling them to be processed further and excreted efficiently. This part was combined with POR in our composites. The following composites and devices, where this part was used, is listed below:  
+
In our system, CYP1A1 is integrated into a detoxification module where it initiates the oxidative breakdown of harmful pollutants, enabling them to be processed further and excreted efficiently. This part was combined with POR in our composites. The following composites and devices, where this part was used, are listed below:  
  
  

Latest revision as of 17:38, 26 September 2024


CYP1A1 - Cytochrome P450 1A1

CYP1A1 (Cytochrome P450 1A1) is a vital enzyme in the cytochrome P450 family that primarily metabolizes environmental toxins, including polycyclic aromatic hydrocarbons (PAHs), dioxins, and polychlorinated biphenyls (PCBs). Predominantly expressed in the lungs and liver, CYP1A1 plays a key role in phase I metabolism, where it oxidizes hydrophobic compounds, rendering them more polar and easier to excrete. CYP1A1 catalyzes the incorporation of an oxygen atom into its substrates, producing reactive intermediates that are often further processed by phase II enzymes like UGT1A1 through glucuronidation. By metabolizing these carcinogenic and mutagenic compounds, CYP1A1 helps protect the body from toxic environmental exposures (1).

In our system, CYP1A1 is integrated into a detoxification module where it initiates the oxidative breakdown of harmful pollutants, enabling them to be processed further and excreted efficiently. This part was combined with POR in our composites. The following composites and devices, where this part was used, are listed below:


Sequence and Features


Assembly Compatibility:
  • 10
    INCOMPATIBLE WITH RFC[10]
    Illegal PstI site found at 232
    Illegal PstI site found at 1435
  • 12
    INCOMPATIBLE WITH RFC[12]
    Illegal PstI site found at 232
    Illegal PstI site found at 1435
  • 21
    COMPATIBLE WITH RFC[21]
  • 23
    INCOMPATIBLE WITH RFC[23]
    Illegal PstI site found at 232
    Illegal PstI site found at 1435
  • 25
    INCOMPATIBLE WITH RFC[25]
    Illegal PstI site found at 232
    Illegal PstI site found at 1435
    Illegal NgoMIV site found at 326
    Illegal NgoMIV site found at 413
  • 1000
    INCOMPATIBLE WITH RFC[1000]
    Illegal BsaI.rc site found at 1132
    Illegal BsaI.rc site found at 1390
    Illegal SapI.rc site found at 490


References

1. Inui H, Itoh T, Yamamoto K, Ikushiro S, Sakaki T. Mammalian cytochrome P450-dependent metabolism of polychlorinated dibenzo-p-dioxins and coplanar polychlorinated biphenyls. Int J Mol Sci. 2014 Aug 13;15(8):14044-57. doi: 10.3390/ijms150814044. PMID: 25123135; PMCID: PMC4159838.