Merge branch 'viki_modified' into 'main'

Viki modified

See merge request ceplas-publications/FokoKuate-2023!1

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README.md

+# Kinetic data for modeling the dynamics of the enzymes involved in animal fatty acid synthesis
+
+## Original Publication
+
+Chilperic Armel Foko Kuate, Oliver Ebenhöh, Barbara M. Bakker, Adélaïde Raguin; Kinetic data for modeling the dynamics of the enzymes involved in animal fatty acid synthesis. Biosci Rep 26 July 2023; 43 (7): BSR20222496. doi: https://doi.org/10.1042/BSR20222496
+
+## Abstract
+
+The synthesis and modification of fatty acids (FAs) from carbohydrates are paramount for the production of lipids. Simultaneously, lipids are pivotal energy storage in human health. They are associated with various metabolic diseases and their production pathways are for instance candidate therapeutic targets for cancer treatments. The fatty acid *de novo* synthesis (FADNS) occurs in the cytoplasm, while the microsomal modification of fatty acids (MMFA) happens at the surface of the endoplasmic reticulum (ER). The kinetics and regulation of these complex processes involve several enzymes. In mammals, the main ones are the acetyl-CoA carboxylase (ACC), the fatty acid synthase (FAS), the very-long-chain fatty acid elongases (ELOVL 1–7), and the desaturases (delta family). Their mechanisms and expression in different organs have been studied for more than 50 years. However, modeling them in the context of complex metabolic pathways is still a challenge. Distinct modeling approaches can be implemented. Here, we focus on dynamic modeling using ordinary differential equations (ODEs) based on kinetic rate laws. This requires a combination of knowledge on the enzymatic mechanisms and their kinetics, as well as the interactions between the metabolites, and between enzymes and metabolites. In the present review, after recalling the modeling framework, we support the development of such a mathematical approach by reviewing the available kinetic information of the enzymes involved.
+
+<img src=./_publication/bsr-2022-2496i001.png width=35%>
+
+## License
+
+ 2023 The Author(s). This is an open access article published by Portland Press Limited on behalf of the Biochemical Society and distributed under the Creative Commons Attribution
+License 4.0 (CC BY).
+
+## Data availability
\ No newline at end of file