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Exploiting members of the BAHD acyltransferase family to synthesize multiple hydroxycinnamate and benzoate conjugates in yeast

Overview of attention for article published in Microbial Cell Factories, November 2016
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Title
Exploiting members of the BAHD acyltransferase family to synthesize multiple hydroxycinnamate and benzoate conjugates in yeast
Published in
Microbial Cell Factories, November 2016
DOI 10.1186/s12934-016-0593-5
Pubmed ID
Authors

Aymerick Eudes, Maxence Mouille, David S. Robinson, Veronica T. Benites, George Wang, Lucien Roux, Yi-Lin Tsai, Edward E. K. Baidoo, Tsan-Yu Chiu, Joshua L. Heazlewood, Henrik V. Scheller, Aindrila Mukhopadhyay, Jay D. Keasling, Samuel Deutsch, Dominique Loqué

Abstract

BAHD acyltransferases, named after the first four biochemically characterized enzymes of the group, are plant-specific enzymes that catalyze the transfer of coenzyme A-activated donors onto various acceptor molecules. They are responsible for the synthesis in plants of a myriad of secondary metabolites, some of which are beneficial for humans either as therapeutics or as specialty chemicals such as flavors and fragrances. The production of pharmaceutical, nutraceutical and commodity chemicals using engineered microbes is an alternative, green route to energy-intensive chemical syntheses that consume petroleum-based precursors. However, identification of appropriate enzymes and validation of their functional expression in heterologous hosts is a prerequisite for the design and implementation of metabolic pathways in microbes for the synthesis of such target chemicals. For the synthesis of valuable metabolites in the yeast Saccharomyces cerevisiae, we selected BAHD acyltransferases based on their preferred donor and acceptor substrates. In particular, BAHDs that use hydroxycinnamoyl-CoAs and/or benzoyl-CoA as donors were targeted because a large number of molecules beneficial to humans belong to this family of hydroxycinnamate and benzoate conjugates. The selected BAHD coding sequences were synthesized and cloned individually on a vector containing the Arabidopsis gene At4CL5, which encodes a promiscuous 4-coumarate:CoA ligase active on hydroxycinnamates and benzoates. The various S. cerevisiae strains obtained for co-expression of At4CL5 with the different BAHDs effectively produced a wide array of valuable hydroxycinnamate and benzoate conjugates upon addition of adequate combinations of donors and acceptor molecules. In particular, we report here for the first time the production in yeast of rosmarinic acid and its derivatives, quinate hydroxycinnamate esters such as chlorogenic acid, and glycerol hydroxycinnamate esters. Similarly, we achieved for the first time the microbial production of polyamine hydroxycinnamate amides; monolignol, malate and fatty alcohol hydroxycinnamate esters; tropane alkaloids; and benzoate/caffeate alcohol esters. In some instances, the additional expression of Flavobacterium johnsoniae tyrosine ammonia-lyase (FjTAL) allowed the synthesis of p-coumarate conjugates and eliminated the need to supplement the culture media with 4-hydroxycinnamate. We demonstrate in this study the effectiveness of expressing members of the plant BAHD acyltransferase family in yeast for the synthesis of numerous valuable hydroxycinnamate and benzoate conjugates.

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Mendeley readers

Mendeley readers

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Geographical breakdown

Country Count As %
United States 1 1%
China 1 1%
Unknown 86 98%

Demographic breakdown

Readers by professional status Count As %
Researcher 19 22%
Student > Ph. D. Student 18 20%
Student > Master 11 13%
Student > Doctoral Student 6 7%
Other 5 6%
Other 12 14%
Unknown 17 19%
Readers by discipline Count As %
Agricultural and Biological Sciences 31 35%
Biochemistry, Genetics and Molecular Biology 28 32%
Engineering 3 3%
Chemical Engineering 2 2%
Chemistry 2 2%
Other 4 5%
Unknown 18 20%
Attention Score in Context

Attention Score in Context

This research output has an Altmetric Attention Score of 2. This is our high-level measure of the quality and quantity of online attention that it has received. This Attention Score, as well as the ranking and number of research outputs shown below, was calculated when the research output was last mentioned on 31 March 2017.
All research outputs
#13,743,461
of 23,299,593 outputs
Outputs from Microbial Cell Factories
#844
of 1,641 outputs
Outputs of similar age
#209,934
of 417,399 outputs
Outputs of similar age from Microbial Cell Factories
#17
of 32 outputs
Altmetric has tracked 23,299,593 research outputs across all sources so far. This one is in the 39th percentile – i.e., 39% of other outputs scored the same or lower than it.
So far Altmetric has tracked 1,641 research outputs from this source. They receive a mean Attention Score of 4.5. This one is in the 47th percentile – i.e., 47% of its peers scored the same or lower than it.
Older research outputs will score higher simply because they've had more time to accumulate mentions. To account for age we can compare this Altmetric Attention Score to the 417,399 tracked outputs that were published within six weeks on either side of this one in any source. This one is in the 48th percentile – i.e., 48% of its contemporaries scored the same or lower than it.
We're also able to compare this research output to 32 others from the same source and published within six weeks on either side of this one. This one has gotten more attention than average, scoring higher than 50% of its contemporaries.