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Literature summary for 1.4.1.3 extracted from

  • Wang, S.; Feng, Y.; Zhang, Z.; Zheng, B.; Li, N.; Cao, S.; Matsui, I.; Kosugi, Y.
    Heat effect on the structure and activity of the recombinant glutamate dehydrogenase from a hyperthermophilic archaeon (2003), Arch. Biochem. Biophys., 411, 56-62.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
overexpression in Escherichia coli BL21 Pyrococcus horikoshii

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.025
-
NADP+ pH 7.6, 90┬░C Pyrococcus horikoshii
0.037
-
NADPH pH 7.6, 90┬░C Pyrococcus horikoshii
0.083
-
NADH pH 7.6, 90┬░C Pyrococcus horikoshii
0.53
-
2-oxoglutarate pH 7.6, 90┬░C Pyrococcus horikoshii
0.6
-
L-glutamate pH 7.6, 90┬░C Pyrococcus horikoshii
2.82
-
NH4+ pH 7.6, 90┬░C Pyrococcus horikoshii

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
48000
-
6 * 48000, SDS-PAGE Pyrococcus horikoshii
290000
-
gel filtration Pyrococcus horikoshii

Organism

Organism UniProt Comment Textmining
Pyrococcus horikoshii
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Pyrococcus horikoshii

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2-oxoglutarate + NADH + NH3 no activity with NAD+ as cofactor Pyrococcus horikoshii L-glutamate + NAD+ + H2O
-
ir
L-glutamate + NADP+ + H2O
-
Pyrococcus horikoshii 2-oxoglutarate + NADPH + NH3
-
r

Subunits

Subunits Comment Organism
hexamer 6 * 48000, SDS-PAGE Pyrococcus horikoshii

Temperature Optimum [┬░C]

Temperature Optimum [┬░C] Temperature Optimum Maximum [┬░C] Comment Organism
90
-
-
Pyrococcus horikoshii

Temperature Range [┬░C]

Temperature Minimum [┬░C] Temperature Maximum [┬░C] Comment Organism
70 100 70┬░C: about 35% of maximal activity, 100┬░C: about 65% of maximal activity, reductive amination of 2-oxoglutarate Pyrococcus horikoshii
80 100 80┬░C: about 50% of maximal activity, 100┬░C: about 60% of maximal activity, oxidative amination of ketoglutarate Pyrococcus horikoshii

Temperature Stability [┬░C]

Temperature Stability Minimum [┬░C] Temperature Stability Maximum [┬░C] Comment Organism
80
-
8 h, enzyme retains more than 95% of its activity Pyrococcus horikoshii
90
-
8 h, about 35% loss of activity Pyrococcus horikoshii
100
-
8 h, about 90% loss of activity. 6 h, about 50% loss of activity Pyrococcus horikoshii

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
43.8
-
NH4+ pH 7.6, 90┬░C Pyrococcus horikoshii
121.2
-
L-glutamate pH 7.6, 90┬░C Pyrococcus horikoshii
165.3
-
2-oxoglutarate pH 7.6, 90┬░C Pyrococcus horikoshii
374.5
-
NADH pH 7.6, 90┬░C Pyrococcus horikoshii
387.5
-
NADPH pH 7.6, 90┬░C Pyrococcus horikoshii
399.6
-
NADP+ pH 7.6, 90┬░C Pyrococcus horikoshii

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.6
-
-
Pyrococcus horikoshii

Cofactor

Cofactor Comment Organism Structure
NADH
-
Pyrococcus horikoshii
NADP+ no activity with NAD+ Pyrococcus horikoshii
NADPH
-
Pyrococcus horikoshii