Campus Units

Biochemistry, Biophysics and Molecular Biology, Roy J. Carver Department of, Chemical and Biological Engineering, Genetics, Development and Cell Biology, Center for Biorenewable Chemicals, Center for Metabolic Biology

Document Type

Article

Publication Version

Published Version

Publication Date

2-28-2018

Journal or Book Title

Nature Communications

Volume

9

First Page

860

DOI

10.1038/s41467-018-03310-z

Abstract

The substrate specificity of acyl-ACP thioesterase (TE) plays an essential role in controlling the fatty acid profile produced by type II fatty acid synthases. Here we identify two groups of residues that synergistically determine different substrate specificities of two acyl-ACP TEs from Cuphea viscosissima (CvFatB1 and CvFatB2). One group (V194, V217, N223, R226, R227, and I268 in CvFatB2) is critical in determining the structure and depth of a hydrophobic cavity in the N-terminal hotdog domain that binds the substrate’s acyl moiety. The other group (255-RKLSKI-260 and 285-RKLPKL-289 in CvFatB2) defines positively charged surface patches that may facilitate binding of the ACP moiety. Mutagenesis of residues within these two groups results in distinct synthetic acyl-ACP TEs that efficiently hydrolyze substrates with even shorter chains (C4- to C8-ACPs). These insights into structural determinants of acyl-ACP TE substrate specificity are useful in modifying this enzyme for tailored fatty acid production in engineered organisms.

Comments

This article is published as Jing, Fuyuan, Le Zhao, Marna D. Yandeau-Nelson, and Basil J. Nikolau. "Two distinct domains contribute to the substrate acyl chain length selectivity of plant acyl-ACP thioesterase." Nature communications 9 (2018): 860. doi: 10.1038/s41467-018-03310-z. Posted with permission.

Creative Commons License

Creative Commons Attribution 4.0 License
This work is licensed under a Creative Commons Attribution 4.0 License.

Copyright Owner

The Authors

Language

en

File Format

application/pdf

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