Types | DnaRegion
|
Roles | Translational_Unit
engineered_region
|
Sequences | BBa_K2149016_sequence (Version 1)
|
Description
LuxE is an acyl-protein synthetase found in bioluminescent bacteria. LuxE catalyses the formation of an acyl-protein thiolester from a fatty acid and a protein. This is the second step in the bioluminescent fatty acid reduction system, which converts tetradecanoic acid to the aldehyde substrate of the luciferase-catalysed bioluminescence reaction [PMID: 8941351]. This enzyme takes the fatty acid substrate and catalyzes a reaction, forming a acyl-protein thioester product.
Together with the LuxC gene, represents the main reaction of the fatty aldehyde synthesis, which can then be used to produce alkanes.
Notes
The gene was synthesized with thirty nucleotides in its ends to do a Gibson Assembly overlap. Its design takes into consideration a RBS and a coding sequence.
Source
This part was synthesized by IDT, and it comes from the genomic sequence of Photorhabdus luminescens, codon optimized for Escherichia coli. The sequence was taken from the accession number JQ901710, which was used it to write the article "Synthesis of customized petroleum-replica fuel molecules by targeted modification of free fatty acid pools in Escherichia coli".