Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|
microsome | - |
Gallus gallus | - |
- |
mitochondrion | - |
Gallus gallus | 5739 | - |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
L-glutamate + H2O + NAD+ | Gallus gallus | - |
2-oxoglutarate + NH3 + NADH + H+ | - |
r |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Gallus gallus | - |
- |
- |
Purification (Comment) | Organism |
---|---|
native enzyme from acetone powder of chicken liver by ammonium sulfate fractionation and dialysis, to near homogeneity (about over 90% purity) | Gallus gallus |
Source Tissue | Comment | Organism | Textmining |
---|---|---|---|
liver | - |
Gallus gallus | - |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
DL-norleucine + H2O + NAD+ | 1.6% activity compared to L-glutamate, pH 9.0 | Gallus gallus | ? + NH3 + NADH + H+ | - |
r | |
L-alanine + H2O + NAD+ | 0.27% activity compared to L-glutamate, pH 9.0 | Gallus gallus | ? + NH3 + NADH + H+ | - |
r | |
L-alpha-aminobutyrate + H2O + NAD+ | 2.3% activity compared to L-glutamate, pH 9.0 | Gallus gallus | ? + NH3 + NADH + H+ | - |
r | |
L-glutamate + H2O + NAD+ | - |
Gallus gallus | 2-oxoglutarate + NH3 + NADH + H+ | - |
r | |
L-glutamate + H2O + NAD+ | best substrate, pH 8.0 | Gallus gallus | 2-oxoglutarate + NH3 + NADH + H+ | - |
r | |
L-isoleucine + H2O + NAD+ | 0.95% activity compared to L-glutamate, pH 9.0 | Gallus gallus | ? + NH3 + NADH + H+ | - |
r | |
L-leucine + H2O + NAD+ | 1.7% activity compared to L-glutamate, pH 9.0 | Gallus gallus | 2-oxoisovalerate + NH3 + NADH + H+ | - |
r | |
L-methionine + H2O + NAD+ | 0.82% activity compared to L-glutamate, pH 9.0 | Gallus gallus | ? + NH3 + NADH + H+ | - |
r | |
L-norvaline + H2O + NAD+ | 17% activity compared to L-glutamate, pH 9.0 | Gallus gallus | ? + NH3 + NADH + H+ | - |
r | |
L-valine + H2O + NAD+ | 1.6% activity compared to L-glutamate, pH 9.0 | Gallus gallus | ? + NH3 + NADH + H+ | - |
r | |
additional information | substrate specificity of partially purified enzyme, overview. The enzyme exhibits stereospecificity for the L-isomer. No activity with L-ornithine, L-lysine, L-proline, L-aspartic acid, L-alpha-aminoadipic acid, L-threonine, D-leucine, and DL-alpha-methylglutamic acid. The gamma-carboxyl group of glutamic acid facilitates the binding of this substrate to the enzyme through an electrostatic attraction between this negatively charged group and a positively charged group on the enzyme. Decrease or increase of the length of the carbon chain by a single methylene group (e.g., aspartic and alpha-aminoadipic acids) appears to abolish activity. The presence of a second positively charged group in the substrate, as in ornithine or lysine, interferes with binding to the enzyme | Gallus gallus | ? | - |
- |
Synonyms | Comment | Organism |
---|---|---|
glutamic acid dehydrogenase | - |
Gallus gallus |
L-glutamic acid dehydrogenase | - |
Gallus gallus |
More | cf. EC 1.4.1.3 | Gallus gallus |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
22 | 25 | assay at | Gallus gallus |
Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
---|---|---|---|
50 | - |
partially purified enzyme, pH 8.0, half-life is 50 min, 40% activity remaining after 60 min | Gallus gallus |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
8.5 | 10 | amino acid oxidation | Gallus gallus |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
NAD+ | - |
Gallus gallus | |
NADH | - |
Gallus gallus |