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Literature summary extracted from

  • Ferrer, J.; Cremades, R.; Pire, C.; Bonete, M.J.
    Fluorescence and quenching comparative studies of halophilic and bovine glutamate dehydrogenase (1998), J. Photochem. Photobiol. B, 47, 148-154.
    View publication on PubMed

Organic Solvent Stability

EC Number Organic Solvent Comment Organism
1.4.1.4 guanidine-HCl the denaturation process is accompanied by an exposure to the solvent of the tryptophan residues, as manifested by the red shift of the emission maximum in both cases. The unfolding of Haloferax mediterranei glutamate dehydrogenase is a gradual process, which is accompanied by a loss in enzyme activity. Fluorescence quenching by external quenchers, KI and acrylamide, has also been carried out. The tryptophan residues in the protein are more exposed to the solvent in Haloferax mediterranei than in bovine glutamate dehydrogenase. The total amount of tryptophan residues is nearly the same for both enzymes Bos taurus
1.4.1.4 guanidine-HCl the denaturation process is accompanied by an exposure to the solvent of the tryptophan residues, as manifested by the red shift of the emission maximum in both cases. The unfolding of Haloferax mediterranei glutamate dehydrogenase is a gradual process, which is accompanied by a loss in enzyme activity. Fluorescence quenching by external quenchers, KI and acrylamide, has also been carried out. The tryptophan residues in the protein are more exposed to the solvent in Haloferax mediterranei than in bovine glutamate dehydrogenase. The total amount of tryptophan residues is nearly the same for both enzymes Haloferax mediterranei

Organism

EC Number Organism UniProt Comment Textmining
1.4.1.4 Bos taurus
-
-
-
1.4.1.4 Haloferax mediterranei
-
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.4.1.4 L-glutamate + H2O + NADP+
-
 Bos taurus 2-oxoglutarate + NH3 + NADPH + H+
-
 ?
1.4.1.4 L-glutamate + H2O + NADP+
-
 Haloferax mediterranei 2-oxoglutarate + NH3 + NADPH + H+
-
 ?

Subunits

EC Number Subunits Comment Organism
1.4.1.4 homohexamer
-
 Bos taurus
1.4.1.4 homohexamer
-
 Haloferax mediterranei

Synonyms

EC Number Synonyms Comment Organism
1.4.1.4 NADP-glutamate dehydrogenase
-
 Bos taurus
1.4.1.4 NADP-glutamate dehydrogenase
-
 Haloferax mediterranei

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
1.4.1.4 25
-
 assay at Bos taurus
1.4.1.4 25
-
 assay at Haloferax mediterranei

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.4.1.4 8
-
 assay at Bos taurus
1.4.1.4 8
-
 assay at Haloferax mediterranei