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Literature summary for 1.4.1.2 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
Search for more literature for 1.4.1.2

Inhibitors

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

Localization

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

Metals/Ions

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

Molecular Weight [Da]

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

Organism

Organism UniProt Comment Textmining
Vitis vinifera
-
-
-

Purification (Commentary)

Purification (Comment) Organism
7 isoenzymes Vitis vinifera

Source Tissue

Source Tissue Comment Organism Textmining
leaf
-
 Vitis vinifera
-

Specific Activity [micromol/min/mg]

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

Substrates and Products (Substrate)

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

Subunits

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

pH Optimum

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

Cofactor

Cofactor Comment Organism Structure
NAD+
-
 Vitis vinifera
NADH
-
 Vitis vinifera