Difference between revisions of "Part:BBa K5477018"
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<partinfo>BBa_K5477018 short</partinfo> | <partinfo>BBa_K5477018 short</partinfo> | ||
− | + | UDP-glucose dehydrogenase (UDPD) biosynthesizes UDP-glucuronic acid from UDP-Glucose. UDP-glucuronic acid is a needed substrate in the phase II detoxification reactions carried out by UDP-glucuronosyltransferase (UGT). <i>Saccharomyces cerevisiae</i> has a large pool of UDP-glucose but lacks the ability to synthesize UDP-glucoronic acid (1). This sequence is from <i>Arabidopsis thaliana </i> - At1g26570/T1K7_6. | |
− | + | Due to the use of UGTs in the detoxification modules, UDPD is co-expressed to provide the necessary substrate for the glucuronidation reactions where UGT1A1 and UGT2B15 were used (1) (2). The following composites and devices, where this part was used, are listed below: [https://parts.igem.org/Part:BBa_K5477035 BBa_K5477035], [https://parts.igem.org/Part:BBa_K5477036 BBa_K5477036], [https://parts.igem.org/Part:BBa_K5477040 BBa_K5477040] and [https://parts.igem.org/Part:BBa_K5477046 BBa_K5477046] and [https://parts.igem.org/Part:BBa_K5477047 BBa_K5477047]. | |
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===References=== | ===References=== | ||
− | 1. Rowland A, Miners JO, Mackenzie PI. The UDP-glucuronosyltransferases: their role in drug metabolism and detoxification. Int J Biochem Cell Biol. 2013;45(6):1121-1132. doi:10.1016/j.biocel.2013.02.019 | + | 1. Oka T, Jigami Y. Reconstruction of de novo pathway for synthesis of UDP-glucuronic acid and UDP-xylose from intrinsic UDP-glucose in Saccharomyces cerevisiae. FEBS J. 2006 Jun;273(12):2645–57. |
+ | |||
+ | 2. Rowland A, Miners JO, Mackenzie PI. The UDP-glucuronosyltransferases: their role in drug metabolism and detoxification. Int J Biochem Cell Biol. 2013;45(6):1121-1132. doi:10.1016/j.biocel.2013.02.019 |
Latest revision as of 23:42, 1 October 2024
UDPD - UDP-glucose dehydrogenase
UDP-glucose dehydrogenase (UDPD) biosynthesizes UDP-glucuronic acid from UDP-Glucose. UDP-glucuronic acid is a needed substrate in the phase II detoxification reactions carried out by UDP-glucuronosyltransferase (UGT). Saccharomyces cerevisiae has a large pool of UDP-glucose but lacks the ability to synthesize UDP-glucoronic acid (1). This sequence is from Arabidopsis thaliana - At1g26570/T1K7_6.
Due to the use of UGTs in the detoxification modules, UDPD is co-expressed to provide the necessary substrate for the glucuronidation reactions where UGT1A1 and UGT2B15 were used (1) (2). The following composites and devices, where this part was used, are listed below: BBa_K5477035, BBa_K5477036, BBa_K5477040 and BBa_K5477046 and BBa_K5477047.
Sequence and Features
- 10INCOMPATIBLE WITH RFC[10]Illegal PstI site found at 542
- 12INCOMPATIBLE WITH RFC[12]Illegal PstI site found at 542
- 21INCOMPATIBLE WITH RFC[21]Illegal BglII site found at 1122
- 23INCOMPATIBLE WITH RFC[23]Illegal PstI site found at 542
- 25INCOMPATIBLE WITH RFC[25]Illegal PstI site found at 542
- 1000COMPATIBLE WITH RFC[1000]
References
1. Oka T, Jigami Y. Reconstruction of de novo pathway for synthesis of UDP-glucuronic acid and UDP-xylose from intrinsic UDP-glucose in Saccharomyces cerevisiae. FEBS J. 2006 Jun;273(12):2645–57.
2. Rowland A, Miners JO, Mackenzie PI. The UDP-glucuronosyltransferases: their role in drug metabolism and detoxification. Int J Biochem Cell Biol. 2013;45(6):1121-1132. doi:10.1016/j.biocel.2013.02.019