GLUD1 cDNA ORF clone, Bos taurus(cattle)

Using Cryo-EM to Map Small Ligands on Dynamic Metabolic Enzymes: Studies with Glutamate Dehydrogenase.
Borgnia MJ, Banerjee S, Merk A, Matthies D, Bartesaghi A, Rao P, Pierson J, Earl LA, Falconieri V, Subramaniam S, Milne JL
Molecular pharmacology89(6)645-51(2016 06)

The role of salt bridges, charge density, and subunit flexibility in determining disassembly routes of protein complexes.
Hall Z, Hern?ndez H, Marsh JA, Teichmann SA, Robinson CV
Structure (London, England : 1993)21(8)1325-37(2013 Aug)

A novel mechanism of V-type zinc inhibition of glutamate dehydrogenase results from disruption of subunit interactions necessary for efficient catalysis.
Bailey J, Powell L, Sinanan L, Neal J, Li M, Smith T, Bell E
The FEBS journal278(17)3140-51(2011 Sep)

Electrochemical and spectral study on the effects of Al(III) and nano-Al13 species on glutamate dehydrogenase activity.
Cai L, Xie Y, Li L, Li H, Yang X, Liu S
Colloids and surfaces. B, Biointerfaces81(1)123-9(2010 Nov)

Ligand-induced changes in the conformational stability and flexibility of glutamate dehydrogenase and their role in catalysis and regulation.
Wacker SA, Bradley MJ, Marion J, Bell E
Protein science : a publication of the Protein Society19(10)1820-9(2010 Oct)

near-atomic resolution cryoelectron microscopy structures, at resolutions ranging from 3.2 A to 3.6 A for GDH complexes, is reported.
Title: Using Cryo-EM to Map Small Ligands on Dynamic Metabolic Enzymes: Studies with Glutamate Dehydrogenase.

Data show that glutamate dehydrogenase activity in an enzymatic catalyzed reaction by tracing the increasing of oxidation current of NADH.
Title: Electrochemical and spectral study on the effects of Al(III) and nano-Al13 species on glutamate dehydrogenase activity.

Data show that heat inactivation of the native GDH enzyme occurred with a rate constant of inactivation of 0.252 min-1.
Title: Ligand-induced changes in the conformational stability and flexibility of glutamate dehydrogenase and their role in catalysis and regulation.

Results showt superactivation is caused by cleavage at the N terminus of the protein and not the C-terminal allosteric site, as has previously been suggested.
Title: The structural basis of proteolytic activation of bovine glutamate dehydrogenase.

the existence of two partially unfolded states of GDH at moderate acidic pHs which may be considered as molten and pre-molten globule-like states.
Title: Partially folded conformations of bovine liver glutamate dehydrogenase induced by mild acidic conditions.