Glutamate dehydrogenase
From Proteopedia
(Difference between revisions)
| Line 30: | Line 30: | ||
**[[2yfq]] - bGLDH – ''Peptoniphilus asaccharolyticus''<br /> | **[[2yfq]] - bGLDH – ''Peptoniphilus asaccharolyticus''<br /> | ||
**[[3sbo]], [[2yfg]], [[4bht]], [[4fcc]] - EcGLDH – ''Escherichia coli''<br /> | **[[3sbo]], [[2yfg]], [[4bht]], [[4fcc]] - EcGLDH – ''Escherichia coli''<br /> | ||
| - | **[[2yfh]] – EcGLDH/CsGLDH | + | **[[2yfh]] – EcGLDH/CsGLDH<br /> |
| + | **[[4xgi]] – GLDH – ''Burkholderia thailandensis''<br /> | ||
*Glutamate dehydrogenase complex | *Glutamate dehydrogenase complex | ||
Revision as of 10:49, 7 April 2015
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 07-April-2015
