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Studies on S445L GDH mutation associated with both Hyperinsulinism/Hyperammonemia syndrome and epilepsy

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Defense Thèse de doctorat : Univ. Genève, 2016 - Sc. 5034 - 2016/12/19
Abstract Glutamate dehydrogenase (GDH), encoded by GLUD1 gene, is a homohexameric enzyme located in the mitochondrial matrix in mammals. Structurally, it is composed of 2 trimers of subunits. The bottom domain of each trimer makes extensive contacts with the subunits from the other trimer. The top domain contains the NAD-binding domain, a long protrusion antenna region and the catalytic active site. GDH enzyme catalyzes the reversible oxidative deamination of glutamate to α-ketoglutarate and ammonia using NAD+/NADH as coenzyme. It has been demonstrated that the GDH enzymatic activity is modulated by several allosteric modulators. For instance, GTP is a potent allosteric inhibitor preventing the product release whereas ADP is a potent allosteric activator facilitating product release.
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URN: urn:nbn:ch:unige-917270
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GRIMALDI, Mariagrazia. Studies on S445L GDH mutation associated with both Hyperinsulinism/Hyperammonemia syndrome and epilepsy. Université de Genève. Thèse, 2016. https://archive-ouverte.unige.ch/unige:91727

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Deposited on : 2017-02-06

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