TY - JOUR
T1 - Kinetic data for modeling the dynamics of the enzymes involved in animal fatty acid synthesis
AU - Foko Kuate, Chilperic Armel
AU - Ebenhöh, Oliver
AU - Bakker, Barbara Marleen
AU - Raguin, Adélaïde
N1 - Funding Information:
This paper was supported by the European Union’s Horizon 2020 research and innovation program under the Marie Sklodowska-Curie grant agreement PoLiMeR [number 812616]. To complete this work, the position of A.R. was funded by the Federal Ministry of Education and Research of Germany in the framework of CornWall [Project Number 031B0193A], and the German federal and state program Professorinnenprogramm III for female scientists. This work was funded by the Deutsche Forschungsgemeinschaft (DFG, German Research Foundation) under Germany’s Excellence Strategy [EXC-2048/1 project ID 390686111].
Publisher Copyright:
© 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).
PY - 2023/7
Y1 - 2023/7
N2 - 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.
AB - 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.
U2 - 10.1042/BSR20222496
DO - 10.1042/BSR20222496
M3 - Review article
C2 - 37132633
SN - 0144-8463
VL - 43
JO - Bioscience reports
JF - Bioscience reports
IS - 7
M1 - BSR20222496
ER -