Glutamate dehydrogenase

spinqualitylabelsall models Glutamate dehydrogenase complex with glutamate (PDB entry 1bgv) Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Function Glutamate dehydrogenase (GLDH) catalyzes the reversible conversion of glutamate to α-ketoglutarate (AKG) and ammonium. The ammonia is removed via the urea cycle. NAD or NADP is a cofactor in GLDH activity. NAD is a cofactor in the forward reaction while NADP is a cofactor in the reverse reaction. GLDH is regulated by the cell’s energy state. ATP and GTP inhibit the enzyme while ADP, GDP and leucine positively enhance it. Glutamate dehydrogenase 1 (GLDH1) catalyzes the deamination of glutamate to 2-oxoglutarate and ammonium. GLDH1 is regulated in the same manner as GLDH. See also Citric Acid Cycle. Relevance Elevated GLDH values in blood serum indicate liver malfunction. Disease Mutations in GLDH1 are associated with familial hyperinsulinism. Structural highlights The biological assembly of GLDH from Clostridium symbiosum is homohexamer. The glutamate binding pocket of GLDH is in a cleft between the two domains of the enzyme with residue D165 serving as a general base and a protein-bound water molecule as the attacking nucleophile . Water molecules are shown as red spheres. 3D structures of glutamate dehydrogenase Glutamate dehydrogenase 3D structures

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