Glutamate dehydrogenase

From Proteopedia

Revision as of 07:47, 26 November 2014 by Michal Harel (Talk | contribs)
Jump to: navigation, search

Template:STRUCTURE 1gtm Glutamate dehydrogenase (GLDH) catalyzes the reversible conversion of glutamate to α-ketoglutarate and ammonium. The ammonia is removed via the urea cycle. Elevated GLDH values in blood serum indicate liver malfunction. 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. 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.

3D structures of glutamate dehydrogenase

Updated on 26-November-2014

Proteopedia Page Contributors and Editors (what is this?)

Michal Harel, Alexander Berchansky, Joel L. Sussman

Retrieved from "http://52.214.119.220/wiki/index.php/Glutamate_dehydrogenase"
Personal tools