ArticleNature communications2018
Two distinct domains contribute to the substrate acyl chain length selectivity of plant acyl-ACP thioesterase.
Article in Nature communications, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
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Who cites it
24 citing papers in PubMed.
- Plastid acyl carrier proteins play redundant roles in seed oil accumulation with functional differentiation on the fatty acid flux.Plant cell reports · 2026Article
- Structural Prioritization of FatB Thioesterase Candidates Potentially Related to Lauric Acid-Rich Seed Oil inBiomolecules · 2026Article
- Acyl-CoA thioesterases and their derived lipid mediators: linking Acyl-CoA metabolic reprogramming to the tumor microenvironment.Frontiers in immunology · 2026Review
- Genome-wide analysis of FATA associated with drought tolerance in tetraploid potato (Frontiers in plant science · 2026Article
- A synthetic metabolic pathway for the de novo biosynthesis of medium chain length γ- and δ-lactones.Journal of biological engineering · 2025Article
- Directed Evolution of a Modular Polyketide Synthase Thioesterase for Generation of a Hybrid Macrocyclic Ring System.ACS catalysis · 2025Article
- Selection of Key Genes for Apricot Kernel Oil Synthesis Based on Transcriptome Analysis.Foods (Basel, Switzerland) · 2025Article
- Transcriptomic characterization of recombinantApplied and environmental microbiology · 2024Article
- The identification and expression analysis of walnut Acyl-ACP thioesterases.Frontiers in genetics · 2024Article
- Machine learning model of the catalytic efficiency and substrate specificity of acyl-ACP thioesterase variants generated from natural andFrontiers in bioengineering and biotechnology · 2024Article
- Relative Activities of the β-ketoacyl-CoA and Acyl-CoA Reductases Influence Product Profile and Flux in a Reversed β-Oxidation Pathway.ACS catalysis · 2023Article
- Conformational Changes of Acyl Carrier Protein Switch the Chain Length Preference of Acyl-ACP Thioesterase ChFatB2.International journal of molecular sciences · 2023Article
- Determinants of substrate specificity in a catalytically diverse family of acyl-ACP thioesterases from plants.BMC plant biology · 2023Article
- Divergent evolution of extreme production of variant plant monounsaturated fatty acids.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Heterologous Expression ofInternational journal of molecular sciences · 2022Article
- Kinetically guided, ratiometric tuning of fatty acid biosynthesis.Metabolic engineering · 2022Review
- Genome-wide identification and analysis of soybean acyl-ACP thioesterase gene family reveals the role of GmFAT to improve fatty acid composition in soybean seed.TAG. Theoretical and applied genetics. Theoretische und angewandte Genetik · 2021Article
- Thermostable lipases and their dynamics of improved enzymatic properties.Applied microbiology and biotechnology · 2021Review
- Speaking the language of lipids: the cross-talk between plants and pathogens in defence and disease.Cellular and molecular life sciences : CMLS · 2021Review
- Increased Accumulation of Medium-Chain Fatty Acids by Dynamic Degradation of Long-Chain Fatty Acids inGenes · 2020Article
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Authors and funding
4 authors.
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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.
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