Difference between revisions of "Part:BBa K4388002"

Revision as of 10:09, 5 October 2022

Arabidopsis thaliana 4-Coumarate:CoA Ligase Mutant (At4CL L57I/L460H)

The Arabidopsis thaliana 4-coumarate:CoA Ligase (At4CL) is an enzyme that catalyses the activation of 4-coumaric acid with Coenzyme A to form 4-coumaroyl-CoA.

4CL is a key enzyme of the general phenylpropanoid pathway that has been used for the production of multiple polyphenols including naringenin, resveratrol, and pterostilbene. This version of the enzyme is a mutant with amino acid changes L57I and L460H. These mutations have been shown to increase catalytic efficiency from 6.72 (wild-type) to 31.76 μmol/h/g (Yan et al., 2021).

The ORF of this compound was obtained from the iGEM registry: BBa_K1033001. This sequence was then codon optimized for E. coli K12, mutated at the desired positions, and two stop codons (TAATAA) were added to terminate translation.

Yan, Z.-B., Liang, J.-L., Niu, F.-X., Shen, Y.-P., & Liu, J.-Z. (2021). Enhanced Production of Pterostilbene in Escherichia coli Through Directed Evolution and Host Strain Engineering. Frontiers in Microbiology, 12. doi:10.1186/s12934-017-0644-6

Sequence and Features