BMS2021 Lecture Notes - Lecture 2: Glutamine, Adipose Tissue, Glut4
15 Aug 2018
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Describe the mechanism of deamination of amino acids. Deamination: the enzymatic removal of amino groups from biomolecules such as amino acids or nucleotides. Transamination: enzymatic transfer of an amino group from an -amino acid to an -keto acid. Amino groups from many of the amino groups are collected in the liver in the form of the amino group of l-glutamate molecules. The amino groups must be removed from glutamate to prepare them for excretion. In hepatocytes, glutamate is transported from the cytosol into mitochondria where it undergoes oxidative deamination catalysed by l- glutamate dehydrogenase. The combined action of aminotransferase and glutamate dehydrogenase is referred to as transdeamination. In humans, glutamate dehydrogenase uses either nad+ or nadp+ as a cofactor. The enzyme is allosterically regulated by gtp and adp. Releases the amino acid group from glutamate to produce ketoglutarate and ammonium. Ketoglutarate acts as a common amino group acceptor forming glutamate. Glutamate can be reconverted to a ketoglutarate by glutamate dehydrogenase.
