Tuning of acyl-ACP thioesterase activity directed for tailored fatty acid synthesis

Applied Microbiology and Biotechnology
Yanbin FengSong Xue

Abstract

Medium-chain fatty acids have attracted significant attention as sources of biofuels in recent years. Acyl-ACP thioesterase, which is considered as the key enzyme to determine the carbon chain length, catalyzes the termination of de novo fatty acid synthesis. Although recombinant medium-chain acyl-ACP thioesterase (TE) affects the fatty acid profile in heterologous cells, tailoring of the fatty acid composition merely by engineering a specific TE is still intractable. In this study, the activity of a C8-C10-specific thioesterase FatB2 from Cuphea hookeriana on C10-ACP was quantified twice as high as that on C8-ACP based on a synthetic C8-C16 acyl-ACP pool in vitro. Whereas in vivo, it was demonstrated that ChFatB2 preferred to accumulate C8 fatty acids with 84.9% composition in the ChFatB2-engineered E. coli strain. To achieve C10 fatty acid production, ChFatB2 was rationally tuned based on structural investigation and enzymatic analysis. An I198E mutant was identified to redistribute the C8-ACP flow, resulting in C10 fatty acid being produced as the principal component at 57.6% of total fatty acids in vivo. It was demonstrated that the activity of TE relative to β-ketoacyl-ACP synthases (KAS) directly determined the fatty acid...Continue Reading

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Citations

Mar 26, 2019·Chembiochem : a European Journal of Chemical Biology·Christina S HeilMartin Grininger
May 19, 2021·ACS Synthetic Biology·Ian Sofian YunusPatrik R Jones
Jun 23, 2021·Chemical Reviews·Pedro PaivaPedro A Fernandes
Oct 30, 2021·TAG. Theoretical and applied genetics. Theoretische und angewandte Genetik·Zhibin ZhangHaihong Shang

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Datasets Mentioned

BETA
MF974182

Methods Mentioned

BETA
transgenic
PCR

Software Mentioned

OriginPro
MODEL
ZDOCK Server
SWISS
PyMOL
ZDOCK

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