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Literature summary 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)

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

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.4.1.3 0.025
-
 NADP+ pH 7.6, 90°C Pyrococcus horikoshii
1.4.1.3 0.037
-
 NADPH pH 7.6, 90°C Pyrococcus horikoshii
1.4.1.3 0.083
-
 NADH pH 7.6, 90°C Pyrococcus horikoshii
1.4.1.3 0.53
-
 2-oxoglutarate pH 7.6, 90°C Pyrococcus horikoshii
1.4.1.3 0.6
-
 L-glutamate pH 7.6, 90°C Pyrococcus horikoshii
1.4.1.3 2.82
-
 NH4+ pH 7.6, 90°C Pyrococcus horikoshii

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.4.1.3 48000
-
 6 * 48000, SDS-PAGE Pyrococcus horikoshii
1.4.1.3 290000
-
 gel filtration Pyrococcus horikoshii

Organism

EC Number Organism UniProt Comment Textmining
1.4.1.3 Pyrococcus horikoshii
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.4.1.3
-
 Pyrococcus horikoshii

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.4.1.3 2-oxoglutarate + NADH + NH3 no activity with NAD+ as cofactor Pyrococcus horikoshii L-glutamate + NAD+ + H2O
-
 ir
1.4.1.3 L-glutamate + NADP+ + H2O
-
 Pyrococcus horikoshii 2-oxoglutarate + NADPH + NH3
-
 r

Subunits

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

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
1.4.1.3 90
-
-
 Pyrococcus horikoshii

Temperature Range [°C]

EC Number Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
1.4.1.3 70 100 70°C: about 35% of maximal activity, 100°C: about 65% of maximal activity, reductive amination of 2-oxoglutarate Pyrococcus horikoshii
1.4.1.3 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]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
1.4.1.3 80
-
 8 h, enzyme retains more than 95% of its activity Pyrococcus horikoshii
1.4.1.3 90
-
 8 h, about 35% loss of activity Pyrococcus horikoshii
1.4.1.3 100
-
 8 h, about 90% loss of activity. 6 h, about 50% loss of activity Pyrococcus horikoshii

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.4.1.3 43.8
-
 NH4+ pH 7.6, 90°C Pyrococcus horikoshii
1.4.1.3 121.2
-
 L-glutamate pH 7.6, 90°C Pyrococcus horikoshii
1.4.1.3 165.3
-
 2-oxoglutarate pH 7.6, 90°C Pyrococcus horikoshii
1.4.1.3 374.5
-
 NADH pH 7.6, 90°C Pyrococcus horikoshii
1.4.1.3 387.5
-
 NADPH pH 7.6, 90°C Pyrococcus horikoshii
1.4.1.3 399.6
-
 NADP+ pH 7.6, 90°C Pyrococcus horikoshii

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.4.1.3 7.6
-
-
 Pyrococcus horikoshii

Cofactor

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