Cat No.
DIA-146
Description
Glutamate dehydrogenase (GLDH) is an enzyme, present in most microbes and the mitochondria of eukaryotes, as are some of the other enzymes required for urea synthesis, that converts glutamate to α-ketoglutarate, and vice versa. In animals, the produced ammonia is usually used as a substrate in the urea cycle. Typically, the α-ketoglutarate to glutamate reaction does not occur in mammals, as glutamate dehydrogenase equilibrium favours the production of ammonia and α-ketoglutarate.
Abbr
GLDH (Bovine)
Alias
GLDH
Source
Bovine liver
Species
Bovine
Form
Freeze dried powder
Enzyme Commission Number
EC 1.4.1.3
Bio-activity
> 500U /mg protein
CAS No.
9001-46-1
Reaction
2-Oxoglutarate + NADH + NH3 + H+ → L-Glutamate + H2O + NAD+
Appearance
White/off white powder
Molecular Mass
260 kDa (gel)
pH Stability
5.0~11.0
Michaelis Constant
9.5×10-3M (NH3); 5.0×10-3M (α-Ketoglutarate); 8.4×10-5M (NADH)
Isoelectric point
pH5.6
Unit Definition
One unit will convert one micromole of α-ketoglutarate to L-glutamate per min at pH 8.3 at 30°C.
Optimum pH
8.5(α-KG→L-Glu)
Optimum temperature
45°C
Thermal stability
< 60°C (pH8.3, 10min)
Inhibitors
Ag+, Hg2+, Cu2+, Zn2+ .
Preparation Instructions
The enzyme is reconstituted in 100mM Tris-HCl buffer, pH 8.3 for activity assay.
Gene Name
GLUD1 glutamate dehydrogenase 1 (Homo sapiens)
Synonyms
glutamate dehydrogenase [NAD(P)+]; EC 1.4.1.3; GLDH; glutamic dehydrogenase; glutamate dehydrogenase [NAD(P)]; L-glutamate: NAD(P)+ oxidoreductase (deaminating); L-GLDH; Glutamate Dehydrogenase from bovine liver; L-Glutamic Dehydrogenase; glutamate dehydrogenase
GeneID
2746
mRNA Refseq
NM_005271
Protein Refseq
NP_005262
UniProt ID
P00367
Chromosome Location
10q23.3
Pathway
Arginine and proline metabolism; D-Glutamine and D-glutamate metabolism; Glutamate metabolism; Nitrogen metabolism; Metabolism of amino acids.
Function
ATP binding; GTP binding; glutamate dehydrogenase [NAD(P)+] activity; glutamate dehydrogenase activity; nucleotide binding; oxidoreductase activity.