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Literature summary for 1.4.1.2 extracted from

  • Hamza, M.A.; Martin, S.R.; Engel, P.C.
    The contribution of tryptophan residues to conformational changes in clostridial glutamate dehydrogenase - W64 and W449 as mediators of the cooperative response to glutamate (2007), FEBS J., 274, 4126-4134.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Escherichia coli [Clostridium] symbiosum

Protein Variants

Protein Variants Comment Organism
W243F decreased activity compared to the wild type enzyme, more thermostable than the wild type enzyme [Clostridium] symbiosum
W310F more thermostable than the wild type enzyme [Clostridium] symbiosum
W393F increased activity compared to the wild type enzyme, more thermostable than the wild type enzyme [Clostridium] symbiosum
W449F decreased activity compared to the wild type enzyme, more thermostable than the wild type enzyme [Clostridium] symbiosum
W64F 65% wild type enzyme activity, less thermostable than the wild type enzyme [Clostridium] symbiosum

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.125
-
NAD+ wild type enzyme, in 0.1 M potassium phosphate buffer, at pH 7.0 and 25°C [Clostridium] symbiosum
0.138
-
NAD+ mutant enzyme W393F, in 0.1 M potassium phosphate buffer, at pH 7.0 and 25°C [Clostridium] symbiosum
0.22
-
NAD+ mutant enzyme W449F, in 0.1 M potassium phosphate buffer, at pH 7.0 and 25°C [Clostridium] symbiosum
0.23
-
NAD+ mutant enzyme W64F, in 0.1 M potassium phosphate buffer, at pH 7.0 and 25°C [Clostridium] symbiosum
0.35
-
NAD+ mutant enzyme W310F, in 0.1 M potassium phosphate buffer, at pH 7.0 and 25°C [Clostridium] symbiosum
0.4
-
NAD+ mutant enzyme W243F, in 0.1 M potassium phosphate buffer, at pH 7.0 and 25°C [Clostridium] symbiosum
3.25
-
L-glutamate mutant enzyme W393F, in 0.1 M potassium phosphate buffer, at pH 7.0 and 25°C [Clostridium] symbiosum
3.25
-
L-glutamate wild type enzyme, in 0.1 M potassium phosphate buffer, at pH 7.0 and 25°C [Clostridium] symbiosum
3.3
-
L-glutamate mutant enzyme W449F, in 0.1 M potassium phosphate buffer, at pH 7.0 and 25°C [Clostridium] symbiosum
3.41
-
L-glutamate mutant enzyme W64F, in 0.1 M potassium phosphate buffer, at pH 7.0 and 25°C [Clostridium] symbiosum
3.7 5 L-glutamate mutant enzyme W310F, in 0.1 M potassium phosphate buffer, at pH 7.0 and 25°C [Clostridium] symbiosum
18.2
-
L-glutamate mutant enzyme W243F, in 0.1 M potassium phosphate buffer, at pH 7.0 and 25°C [Clostridium] symbiosum

Organism

Organism UniProt Comment Textmining
[Clostridium] symbiosum
-
-
-

Purification (Commentary)

Purification (Comment) Organism
Remazol-Red column chromatography [Clostridium] symbiosum

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-glutamate + H2O + NAD+
-
[Clostridium] symbiosum 2-oxoglutarate + NH3 + NADH + H+
-
?

Subunits

Subunits Comment Organism
hexamer x-ray crystallography [Clostridium] symbiosum

Synonyms

Synonyms Comment Organism
GDH
-
[Clostridium] symbiosum

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
50
-
the wild-type GDH retains only approximately 48% of starting activity after incubation at 50°C for 30 min in potassium phosphate (pH 7.0), mutant enzymes W243F and W449F show slightly enhanced stability, retaining approximately 5% more activity over the 30 min period, mutants W310F and W393F show greater stabilization retaining 78% and 82% of their activities, respectively, W64F retains only 37% activity after 30 min [Clostridium] symbiosum

pH Stability

pH Stability pH Stability Maximum Comment Organism
7
-
the wild type enzyme shows pH-dependent inactivation and conformational change and loses 91% of its activity over a few min on transfer from pH 7.0 to pH 8.8 [Clostridium] symbiosum

Cofactor

Cofactor Comment Organism Structure
NAD+
-
[Clostridium] symbiosum