Coding

Part:BBa_K4117222:Design

Designed by: He Du,Yue Zhang   Group: iGEM22_BNU-China   (2022-09-30)
Revision as of 08:14, 12 October 2022 by Yl (Talk | contribs)

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UGT1A3


Assembly Compatibility:
  • 10
    COMPATIBLE WITH RFC[10]
  • 12
    COMPATIBLE WITH RFC[12]
  • 21
    INCOMPATIBLE WITH RFC[21]
    Illegal BglII site found at 1266
    Illegal BamHI site found at 453
  • 23
    COMPATIBLE WITH RFC[23]
  • 25
    INCOMPATIBLE WITH RFC[25]
    Illegal AgeI site found at 40
  • 1000
    COMPATIBLE WITH RFC[1000]


Design Notes

Since this subunit has been proved to be expressed successfully, we did not re-engineer this protein gene.

Source

We design the DNA sequence based on the amino acid sequence according to E. coli codon preference.The amino acid sequence is from UniProt:P35503

References

[1]Mazur A, Lichti CF, Prather PL, Zielinska AK, Bratton SM, Gallus-Zawada A, Finel M, Miller GP, Radomińska-Pandya A, Moran JH. Characterization of human hepatic and extrahepatic UDP-glucuronosyltransferase enzymes involved in the metabolism of classic cannabinoids. Drug Metab Dispos. 2009 Jul;37(7):1496-504. doi: 10.1124/dmd.109.026898. Epub 2009 Apr 1. PMID: 19339377; PMCID: PMC2698943.

[2]Doohan PT, Oldfield LD, Arnold JC, Anderson LL. Cannabinoid Interactions with Cytochrome P450 Drug Metabolism: a Full-Spectrum Characterization. AAPS J. 2021 Jun 28;23(4):91. doi: 10.1208/s12248-021-00616-7. PMID: 34181150.

[3]Sinsinbar G, Gudlur S, Metcalf KJ, Mrksich M, Nallani M, Liedberg B. Role of Lipopolysaccharide in Protecting OmpT from Autoproteolysis during In Vitro Refolding. Biomolecules. 2020;10(6):922. Published 2020 Jun 18.Ct

[4]Sugimura K, Nishihara T. Purification, characterization, and primary structure of Escherichia coli protease VII with specificity for paired basic residues: identity of protease VII and OmpT. J Bacteriol. 1988 Dec;170(12):5625-32. doi: 10.1128/jb.170.12.5625-5632.1988. PMID: 3056908; PMCID: PMC211661