Stroke & Vascular Disorders
Apr. 21, 2022
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In mutated L2HGDH, interacting sites within the FAD domain are lost due to the resulting frameshift and protein truncation. However, the mutant enzyme predictably showed interaction with its substrate at different positions (ie, Arg-42, Cys-38, Gly-40, and Cys-27) through conventional hydrogen bonds and at Gly-28 through a carbon-hydrogen bond. (Source: Muzammal M, Ali MZ, Brugger B, et al. A novel protein-truncating mutation in L2HGDH causes L-2-hydroxyglutaric aciduria in a consanguineous Pakistani family. Metab Brain Dis 2022;37:243-52. Creative Commons Attribution 4.0 License, https://creativecommons.org/licenses/by/4.0.)