Part:BBa_K2073000
fac-dex1
Fac-dex1 is a kind of enzyme under the category of fluoroacetate dehalogenase. The enzyme catalyzes the hydrolytic cleavage of carbon-fluorine bonds to form glycolate.
The reaction: fluoroacetate + H2O ⇌ glycolate + fluoride + H+
Contributions
Group: iGEM22_WVHS_SanDiego
Authors: Ananya Bharathwaj, Madison Yang
Summary: Fluoroacetate dehalogenase (FAcD) is an enzyme that has been shown to cleave C-F bonds, and is produced by various organisms. For our project, we modeled the configuration interaction between PFOA and FAcD (derived from Rhodopseudomonas palustris), and the conformation at the maximum binding energy (binding energy: -8.32, ligand efficiency: -0.33). For in-lab work, we took the sequence of FAcD, codon-optimized it for E. coli, and made it compatible with the Gibson and Golden Gate assembly methods of our u loop system (removing BsaI and Sapl restriction sites, adding 20 bases of homology to each end of the gene sequences, and adding C-D overhangs).
Below are images of our modified plasmid maps developed in SnapGene, along with our protein model developed from Autodock 4.
Sequence and Features
- 10COMPATIBLE WITH RFC[10]
- 12COMPATIBLE WITH RFC[12]
- 21COMPATIBLE WITH RFC[21]
- 23COMPATIBLE WITH RFC[23]
- 25INCOMPATIBLE WITH RFC[25]Illegal NgoMIV site found at 465
Illegal AgeI site found at 201
Illegal AgeI site found at 325
Illegal AgeI site found at 544 - 1000COMPATIBLE WITH RFC[1000]
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