AI Article Synopsis
- * Researchers developed a method called MIDAS, combining mass spectrometry and equilibrium dialysis, to systematically identify these interactions and uncovered 830 protein-metabolite interactions in human carbohydrate metabolism.
- * Some interactions were validated, revealing that specific fatty acids can inhibit lactate dehydrogenase isoforms and affect the conversion of pyruvate to lactate, showcasing how these interactions may help cells adapt to different nutrient scenarios.
Article Abstract
Metabolic networks are interconnected and influence diverse cellular processes. The protein-metabolite interactions that mediate these networks are frequently low affinity and challenging to systematically discover. We developed mass spectrometry integrated with equilibrium dialysis for the discovery of allostery systematically (MIDAS) to identify such interactions. Analysis of 33 enzymes from human carbohydrate metabolism identified 830 protein-metabolite interactions, including known regulators, substrates, and products as well as previously unreported interactions. We functionally validated a subset of interactions, including the isoform-specific inhibition of lactate dehydrogenase by long-chain acyl-coenzyme A. Cell treatment with fatty acids caused a loss of pyruvate-lactate interconversion dependent on lactate dehydrogenase isoform expression. These protein-metabolite interactions may contribute to the dynamic, tissue-specific metabolic flexibility that enables growth and survival in an ever-changing nutrient environment.
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|---|---|
| http://www.ncbi.nlm.nih.gov/pmc/articles/PMC10262665 | PMC |
| http://dx.doi.org/10.1126/science.abm3452 | DOI Listing |
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