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Literature summary extracted from

  • Kim, D.W.; Eum, W.S.; Jang, S.H.; Yoon, C.S.; Kim, Y.H.; Choi, S.H.; Choi, H.S.; Kim, S.Y.; Kwon, H.Y.; Kang, J.H.; Kwon, O.s.; Cho, S.w.; Park, J.; Choi, S.Y.
    Molecular gene cloning, expression, and characterization of bovine brain glutamate dehydrogenase (2003), J. Biochem. Mol. Biol., 36, 545-551.
    View publication on PubMed

Activating Compound

EC Number Activating Compound Comment Organism Structure
1.4.1.3 ADP increases the activity up to 2.3fold Bos taurus

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.4.1.3 expression in Escherichia coli BL21 by using the pET-15b expression vector containing a T7 promoter Bos taurus

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.4.1.3 ATP 0.01-0.1 mM Bos taurus

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.4.1.3 0.1
-
 NAD+ pH 8.0, 25°C, recombinant enzyme Bos taurus
1.4.1.3 0.11
-
 NAD+ pH 8.0, 25°C, native enzyme Bos taurus

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.4.1.3 57500
-
 x * 57500, recombinant enzyme, SDS-PAGE Bos taurus

Organism

EC Number Organism UniProt Comment Textmining
1.4.1.3 Bos taurus
-
-
-

Source Tissue

EC Number Source Tissue Comment Organism Textmining
1.4.1.3 brain
-
 Bos taurus
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.4.1.3 2-oxoglutarate + NADH + NH3
-
 Bos taurus L-glutamate + NAD+ + H2O
-
 ?

Subunits

EC Number Subunits Comment Organism
1.4.1.3 ? x * 57500, recombinant enzyme, SDS-PAGE Bos taurus

Cofactor

EC Number Cofactor Comment Organism Structure
1.4.1.3 NAD+
-
 Bos taurus
1.4.1.3 NADH
-
 Bos taurus