Freedom of assembly: metabolic enzymes come together
| Autor: | Jeffrey R. Peterson, Anika L. Burrell, Jacqueline C. Simonet, Justin M. Kollman |
|---|---|
| Jazyk: | angličtina |
| Rok vydání: | 2020 |
| Předmět: |
Cytoplasm
Dehydrogenase macromolecular substances Polymerization chemistry.chemical_compound IMP Dehydrogenase Humans Carbon-Nitrogen Ligases Enzyme kinetics Molecular Biology Cytoskeleton chemistry.chemical_classification ATP synthase biology Mechanism (biology) Cell Biology Metabolism Enzyme chemistry Biochemistry Metabolic enzymes Perspective biology.protein Protein Multimerization Cytosine HeLa Cells |
| Zdroj: | Molecular Biology of the Cell |
| ISSN: | 1939-4586 1059-1524 |
| Popis: | Many different enzymes in intermediate metabolism dynamically assemble filamentous polymers in cells, often in response to changes in physiological conditions. Most of the enzyme filaments known to date have only been observed in cells, but in a handful of cases structural and biochemical studies have revealed the mechanisms and consequences of assembly. In general, enzyme polymerization functions as a mechanism to allosterically tune enzyme kinetics, and it may play a physiological role in integrating metabolic signaling. Here, we highlight some principles of metabolic filaments by focusing on two well-studied examples in nucleotide biosynthesis pathways—inosine-5’-monophosphate (IMP) dehydrogenase and cytosine triphosphate (CTP) synthase. |
| Databáze: | OpenAIRE |
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