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Literature summary extracted from

  • Loulakakis, C.A.; Roubelakis-Angelakis, K.A.
    Intracellular localization and properties of NADH-glutamate dehydrogenase from Vitis vinifera L.: Purification and characterization of the major leaf isoenzyme (1990), J. Exp. Bot., 41, 1223-1230.
No PubMed abstract available

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.4.1.2 Ca2+ activation of reductive amination; no effect on oxidative deamination Vitis vinifera

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
1.4.1.2 mitochondrion
-
Vitis vinifera 5739
-

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.4.1.2 Ca2+ activation of amination, no effect on deamination Vitis vinifera

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.4.1.2 42500
-
6 * 42500, SDS-PAGE Vitis vinifera
1.4.1.2 252000
-
gel filtration Vitis vinifera

Organism

EC Number Organism UniProt Comment Textmining
1.4.1.2 Vitis vinifera
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.4.1.2 7 isoenzymes Vitis vinifera

Source Tissue

EC Number Source Tissue Comment Organism Textmining
1.4.1.2 leaf
-
Vitis vinifera
-

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
1.4.1.2 441
-
-
Vitis vinifera

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.4.1.2 L-glutamate + H2O + NAD+
-
Vitis vinifera 2-oxoglutarate + NH3 + NADH + H+
-
?

Subunits

EC Number Subunits Comment Organism
1.4.1.2 hexamer 6 * 42500, SDS-PAGE Vitis vinifera

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.4.1.2 8
-
reductive amination Vitis vinifera
1.4.1.2 9.3
-
oxidative deamination Vitis vinifera

Cofactor

EC Number Cofactor Comment Organism Structure
1.4.1.2 NAD+
-
Vitis vinifera
1.4.1.2 NADH
-
Vitis vinifera