Abstract 1725 Exploring the Role of Phosphorylation in Malate Dehydrogenase: Enzymatic Analysis of Phosphomimetic Mutant S227D

Malate dehydrogenase (MDH) is a key enzyme in the citric acid cycle and thus plays a central role in whole-body metabolic regulation. Beyond its classical role as the catalytic interconverter of substrates malate and oxaloacetate (OAA), MDH has demonstrated a high-degree of adaptability to changing cellular demands and conditions. Under hypoxic conditions, MDH has been known to participate in a promiscuous reaction with α-ketoglutarate (α-KG) to form L-2-Hydroxyglutarate (L-2-HG), an oncometabolite that promotes tumorigenesis.

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Journal
Journal of Biological Chemistry
Published
2025-05-01
DOI
https://doi.org/10.1016/j.jbc.2025.109920
Primary Topic
Advanced Proteomics Techniques and Applications
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article
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article

Abstract 1725 Exploring the Role of Phosphorylation in Malate Dehydrogenase: Enzymatic Analysis of Phosphomimetic Mutant S227D

Pamela Mertz, Emily Friedman, Alice Glover
Journal of Biological Chemistry
Advanced Proteomics Techniques and Applications
article

Abstract 1725 Exploring the Role of Phosphorylation in Malate Dehydrogenase: Enzymatic Analysis of Phosphomimetic Mutant S227D

Pamela Mertz, Emily Friedman, Alice Glover
article en

Abstract

Malate dehydrogenase (MDH) is a key enzyme in the citric acid cycle and thus plays a central role in whole-body metabolic regulation. Beyond its classical role as the catalytic interconverter of substrates malate and oxaloacetate (OAA), MDH has demonstrated a high-degree of adaptability to changing cellular demands and conditions. Under hypoxic conditions, MDH has been known to participate in a promiscuous reaction with α-ketoglutarate (α-KG) to form L-2-Hydroxyglutarate (L-2-HG), an oncometabolite that promotes tumorigenesis.

Journal of Biological ChemistryVol. 301(5)
Trinity College (CA)
Zero hunger
Openalex Percentile: Top 88%
Advanced Proteomics Techniques and Applications
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