Two distinct domains contribute to the substrate acyl chain length selectivity of plant acyl-ACP thioesterase

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 vis...

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Bibliographic Details
Published in:Nature communications 2018-02, Vol.9 (1), p.860-10, Article 860
Main Authors: Jing, Fuyuan, Zhao, Le, Yandeau-Nelson, Marna D., Nikolau, Basil J.
Format: Article
Language:English
Subjects:
38/70
631/45/173
631/45/287/1183
631/61/338/469
631/92/60
Acid production
Chains
Fatty acids
Humanities and Social Sciences
Hydrophobicity
multidisciplinary
Mutagenesis
Residues
Science
Science (multidisciplinary)
Substrate specificity
Substrates
Thioesterase
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Summary: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. The substrate specificity of acyl-ACP thioesterase (TE) plays a crucial role in determining the product profile of type II fatty acid synthase. Utilizing two FatB-type acyl-ACP TEs, the authors here define determinants of substrate specificity and create synthetic enzymes with distinct catalytic traits.
ISSN:2041-1723
2041-1723
DOI:10.1038/s41467-018-03310-z