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Doctoral thesis
English

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

Defense date2016-12-19
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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Citation (ISO format)
GRIMALDI, Mariagrazia. Studies on S445L GDH mutation associated with both Hyperinsulinism/Hyperammonemia syndrome and epilepsy. 2016. doi: 10.13097/archive-ouverte/unige:91727
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Creation01/31/2017 5:26:00 PM
First validation01/31/2017 5:26:00 PM
Update time03/15/2023 1:21:41 AM
Status update03/15/2023 1:21:41 AM
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