ArticleChembiochem : a European journal of chemical biology2014
Evolution of a transition state: role of Lys100 in the active site of isocitrate dehydrogenase.
Article in Chembiochem : a European journal of chemical biology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
3 citing papers in PubMed, 7 citations in OpenAlex.
- Studying lysine acetylation of citric acid cycle enzymes by genetic code expansion.Molecular microbiology · 2023Review
- Characterizing Lysine Acetylation of Isocitrate Dehydrogenase in Escherichia coli.Journal of molecular biology · 2018Article
- Crystal Structures of the Putative Isocitrate Dehydrogenase fromArchaea (Vancouver, B.C.) · 2018Article
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Authors and funding
4 authors at 4 institutions in 3 countries.
Funding
Abstract
An active site lysine essential to catalysis in isocitrate dehydrogenase (IDH) is absent from related enzymes. As all family members catalyze the same oxidative β-decarboxylation at the (2R)-malate core common to their substrates, it seems odd that an amino acid essential to one is not found in all. Ordinarily, hydride transfer to a nicotinamide C4 neutralizes the positive charge at N1 directly. In IDH, the negatively charged C4-carboxylate of isocitrate stabilizes the ground state positive charge on the adjacent nicotinamide N1, opposing hydride transfer. The critical lysine is poised to stabilize-and perhaps even protonate-an oxyanion formed on the nicotinamide 3-carboxamide, thereby enabling the hydride to be transferred while the positive charge at N1 is maintained. IDH might catalyze the same overall reaction as other family members, but dehydrogenation proceeds through a distinct, though related, transition state. Partial activation of lysine mutants by K(+) and NH4 (+) represents a throwback to the primordial state of the first promiscuous substrate family member.
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