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Literature summary for 1.4.1.4 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
Search for more literature for 1.4.1.4

Organic Solvent Stability

Organic Solvent Comment Organism
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
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

Organism UniProt Comment Textmining
Bos taurus
-
-
-
Haloferax mediterranei
-
-
-

Substrates and Products (Substrate)

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

Subunits

Subunits Comment Organism
homohexamer
-
 Bos taurus
homohexamer
-
 Haloferax mediterranei

Synonyms

Synonyms Comment Organism
NADP-glutamate dehydrogenase
-
 Bos taurus
NADP-glutamate dehydrogenase
-
 Haloferax mediterranei

Temperature Optimum [°C]

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

pH Optimum

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