Difference between revisions of "Part:BBa K5477022"
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<partinfo>BBa_K5477022 short</partinfo> | <partinfo>BBa_K5477022 short</partinfo> | ||
− | Cytochrome P450 oxidoreductase (POR) | + | Cytochrome P450 oxidoreductase (POR) provides the necessary electrons to support the function of cytochrome P450 enzymes in their metabolic activities(1) (2). POR is a flavoprotein, containing both FMN (flavin mononucleotide) and FAD (flavin adenine dinucleotide) cofactors, which transfers electrons from NADPH to cytochrome P450 enzymes (1) (2). This electron transfer is necessary for the P450 enzymes in phase I metabolism, specifically the oxidation of a wide variety of substrates, including drugs, toxins, and endogenous compounds (1) (2). |
+ | This part was combined with CYP3A4 or CYP1A1. The following composites and devices, where this part was used, are listed here: [https://parts.igem.org/Part:BBa_K5477037 BBa_K5477037], [https://parts.igem.org/Part:BBa_K5477038 BBa_K5477038], [https://parts.igem.org/Part:BBa_K5477039 BBa_K5477039] and [https://parts.igem.org/Part:BBa_K5477047 BBa_K5477047] | ||
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<partinfo>BBa_K5477022 parameters</partinfo> | <partinfo>BBa_K5477022 parameters</partinfo> | ||
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+ | ===References=== | ||
+ | 1. Pandey AV, Flück CE. NADPH P450 oxidoreductase: structure, function, and pathology of diseases. Pharmacol Ther. 2013;138(2):229-254. doi:10.1016/j.pharmthera.2013.01.010 | ||
+ | |||
+ | 2. Pandey AV, Sproll P. Pharmacogenomics of human P450 oxidoreductase. Front Pharmacol. 2014 May 9;5:103. doi: 10.3389/fphar.2014.00103. PMID: 24847272; PMCID: PMC4023047. |
Latest revision as of 00:35, 2 October 2024
POR - Cytochrome P450 oxidoreductase codon optimized for Saccharomyces cerevisiae
Cytochrome P450 oxidoreductase (POR) provides the necessary electrons to support the function of cytochrome P450 enzymes in their metabolic activities(1) (2). POR is a flavoprotein, containing both FMN (flavin mononucleotide) and FAD (flavin adenine dinucleotide) cofactors, which transfers electrons from NADPH to cytochrome P450 enzymes (1) (2). This electron transfer is necessary for the P450 enzymes in phase I metabolism, specifically the oxidation of a wide variety of substrates, including drugs, toxins, and endogenous compounds (1) (2).
This part was combined with CYP3A4 or CYP1A1. The following composites and devices, where this part was used, are listed here: BBa_K5477037, BBa_K5477038, BBa_K5477039 and BBa_K5477047
Sequence and Features
- 10INCOMPATIBLE WITH RFC[10]Illegal PstI site found at 296
Illegal PstI site found at 493
Illegal PstI site found at 877
Illegal PstI site found at 1317
Illegal PstI site found at 1377 - 12INCOMPATIBLE WITH RFC[12]Illegal PstI site found at 296
Illegal PstI site found at 493
Illegal PstI site found at 877
Illegal PstI site found at 1317
Illegal PstI site found at 1377 - 21COMPATIBLE WITH RFC[21]
- 23INCOMPATIBLE WITH RFC[23]Illegal PstI site found at 296
Illegal PstI site found at 493
Illegal PstI site found at 877
Illegal PstI site found at 1317
Illegal PstI site found at 1377 - 25INCOMPATIBLE WITH RFC[25]Illegal PstI site found at 296
Illegal PstI site found at 493
Illegal PstI site found at 877
Illegal PstI site found at 1317
Illegal PstI site found at 1377
Illegal NgoMIV site found at 699
Illegal NgoMIV site found at 818 - 1000COMPATIBLE WITH RFC[1000]
References
1. Pandey AV, Flück CE. NADPH P450 oxidoreductase: structure, function, and pathology of diseases. Pharmacol Ther. 2013;138(2):229-254. doi:10.1016/j.pharmthera.2013.01.010
2. Pandey AV, Sproll P. Pharmacogenomics of human P450 oxidoreductase. Front Pharmacol. 2014 May 9;5:103. doi: 10.3389/fphar.2014.00103. PMID: 24847272; PMCID: PMC4023047.