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Literature summary for 1.4.1.2 extracted from

  • Struck, J. Jr.; Sizer, I.W.
    The substrate specificity of glutamic acid dehydrogenase (1960), Arch. Biochem. Biophys., 86, 260-266 .
No PubMed abstract available

Localization

Localization Comment Organism GeneOntology No. Textmining
microsome
-
Gallus gallus
-
-
mitochondrion
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Gallus gallus 5739
-

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
L-glutamate + H2O + NAD+ Gallus gallus
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2-oxoglutarate + NH3 + NADH + H+
-
r

Organism

Organism UniProt Comment Textmining
Gallus gallus
-
-
-

Purification (Commentary)

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

Source Tissue Comment Organism Textmining
liver
-
Gallus gallus
-

Substrates and Products (Substrate)

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

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 [°C] Temperature Optimum Maximum [°C] Comment Organism
22 25 assay at Gallus gallus

Temperature Stability [°C]

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

pH Optimum Minimum pH Optimum Maximum Comment Organism
8.5 10 amino acid oxidation Gallus gallus

Cofactor

Cofactor Comment Organism Structure
NAD+
-
Gallus gallus
NADH
-
Gallus gallus