Structure, function, and regulation of thioesterases

Swarbrick, C.M.D.; Nanson, J.D.; Patterson, Edward I; Forwood, Jade K.

doi:10.1016/j.plipres.2020.101036

Cited by 22 publications

(16 citation statements)

References 230 publications

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“…Thioesters participate in metabolism, membrane synthesis, signal transduction and gene regulation. Thioesterases convert thioesters to the thiol and carboxylic acid components, which endorse thioesterases the important cellular roles (Swarbrick et al, 2020). This study demonstrated the native enzymes responsible for the hydrolysis of propionyl-CoA to propionate in the engineered P. putida strain.…”

Section: Enzymatic Characterization Of the Identified Thioesterase Pp_4975mentioning

confidence: 59%

Unravelling the thioesterases responsible for propionate formation in engineered Pseudomonasputida KT2440

Shi

et al. 2021

Microbial Biotechnology

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Pseudomonas putida KT2440 is becoming a new robust metabolic chassis for biotechnological applications, due to its metabolic versatility, low nutritional requirements and biosafety status. We have previously engineered P. putida KT2440 to be an efficient propionate producer from L-threonine, although the internal enzymes converting propionyl-CoA to propionate are not clear. In this study, we thoroughly investigated 13 genes annotated as potential thioesterases in the KT2440 mutant. One thioesterase encoded by locus tag PP_4975 was verified to be the major contributor to propionate production in vivo. Deletion of PP_4975 significantly decreased propionate production, whereas the performance was fully restored by gene complement. Compared with thioesterase HiYciA from Haemophilus influenza, thioesterase PP_4975 showed a faster substrate conversion rate in vitro. Thus, this study expands our knowledge on acyl-CoA thioesterases in P. putida KT2440 and may also reveal a new target for further engineering the strain to improve propionate production performance.

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Section: Enzymatic Characterization Of the Identified Thioesterase Pp_4975mentioning

confidence: 59%

Unravelling the thioesterases responsible for propionate formation in engineered Pseudomonasputida KT2440

Shi

et al. 2021

Microbial Biotechnology

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“…Most genomes displayed less than seven GX lipases, except for G. boninense and G. leucocontextum with ten and nine GX lipases respectively. They are prominent enzymes catalyzing a wide range of reactions on various cellular substrates [ 65 , 66 ].…”

Section: Resultsmentioning

confidence: 99%

Phylogenomics and Comparative Genomics Highlight Specific Genetic Features in Ganoderma Species

Sun

Lebreton

Xing

et al. 2022

JoF

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The Ganoderma species in Polyporales are ecologically and economically relevant wood decayers used in traditional medicine, but their genomic traits are still poorly documented. In the present study, we carried out a phylogenomic and comparative genomic analyses to better understand the genetic blueprint of this fungal lineage. We investigated seven Ganoderma genomes, including three new genomes, G. australe, G. leucocontextum, and G. lingzhi. The size of the newly sequenced genomes ranged from 60.34 to 84.27 Mb and they encoded 15,007 to 20,460 genes. A total of 58 species, including 40 white-rot fungi, 11 brown-rot fungi, four ectomycorrhizal fungi, one endophyte fungus, and two pathogens in Basidiomycota, were used for phylogenomic analyses based on 143 single-copy genes. It confirmed that Ganoderma species belong to the core polyporoid clade. Comparing to the other selected species, the genomes of the Ganoderma species encoded a larger set of genes involved in terpene metabolism and coding for secreted proteins (CAZymes, lipases, proteases and SSPs). Of note, G. australe has the largest genome size with no obvious genome wide duplication, but showed transposable elements (TEs) expansion and the largest set of terpene gene clusters, suggesting a high ability to produce terpenoids for medicinal treatment. G. australe also encoded the largest set of proteins containing domains for cytochrome P450s, heterokaryon incompatibility and major facilitator families. Besides, the size of G. australe secretome is the largest, including CAZymes (AA9, GH18, A01A), proteases G01, and lipases GGGX, which may enhance the catabolism of cell wall carbohydrates, proteins, and fats during hosts colonization. The current genomic resource will be used to develop further biotechnology and medicinal applications, together with ecological studies of the Ganoderma species.

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“…In a study reporting the three-dimensional cryo-electron microscopy structure of the recombinant type I FAS protein of Mycobacterium tuberculosis (which belongs to the CMN group bacteria), the narrow phylogenetic distribution of type I FAS systems in bacteria (only present in the genera Corynebacterium, Mycobacterium, and Nocardia), and the structural similarity between M. tuberculosis and fungal type I FAS, insinuates that an early horizontal gene-transfer event might have occurred from fungi to CMN bacteria. 115,124 Another hypothesis is that the CMN type I FAS represents an ancient type I FAS which further evolved in fungi and remained preserved in CMN bacteria 115 interestingly, mycolic acidproducing bacteria. 125 Comparative analysis between animal, fungal, and bacterial FAS showed that type I FAS systems are organized differently, with the main difference residing on the mechanisms of substrate shuttling during the process of fatty acid synthesis.…”

Section: Animal Fatty Acid Synthase: Architecture and Functionmentioning

confidence: 99%

Animal Fatty Acid Synthase: A Chemical Nanofactory

et al. 2021

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Fatty acids are crucial molecules for most living beings, very well spread and conserved across species. These molecules play a role in energy storage, cell membrane architecture, and cell signaling, the latter through their derivative metabolites. De novo synthesis of fatty acids is a complex chemical process that can be achieved either by a metabolic pathway built by a sequence of individual enzymes, such as in most bacteria, or by a single, large multi-enzyme, which incorporates all the chemical capabilities of the metabolic pathway, such as in animals and fungi, and in some bacteria. Here we focus on the multi-enzymes, specifically in the animal fatty acid synthase (FAS). We start by providing a historical overview of this vast field of research. We follow by describing the extraordinary architecture of animal FAS, a homodimeric multi-enzyme with seven different active sites per dimer, including a carrier protein that carries the intermediates from one active site to the next. We then delve into this multi-enzyme’s detailed chemistry and critically discuss the current knowledge on the chemical mechanism of each of the steps necessary to synthesize a single fatty acid molecule with atomic detail. In line with this, we discuss the potential and achieved FAS applications in biotechnology, as biosynthetic machines, and compare them with their homologous polyketide synthases, which are also finding wide applications in the same field. Finally, we discuss some open questions on the architecture of FAS, such as their peculiar substrate-shuttling arm, and describe possible reasons for the emergence of large megasynthases during evolution, questions that have fascinated biochemists from long ago but are still far from answered and understood.

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Structure, function, and regulation of thioesterases

Cited by 22 publications

References 230 publications

Unravelling the thioesterases responsible for propionate formation in engineered Pseudomonasputida KT2440

Unravelling the thioesterases responsible for propionate formation in engineered Pseudomonasputida KT2440

Phylogenomics and Comparative Genomics Highlight Specific Genetic Features in Ganoderma Species

Animal Fatty Acid Synthase: A Chemical Nanofactory

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