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Literature summary extracted from

  • Fawole, M.O.; Boulter, D.
    Purification and properties of glutamate dehydrogenase from Vigna unguiculata (L.) Walp. (1977), Planta, 134, 97-102.
    View publication on PubMed

General Stability

EC Number General Stability Organism
1.4.1.2 repeated freezing and thawing: loss of activity Vigna unguiculata

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.4.1.2 DL-valine
-
Vigna unguiculata
1.4.1.2 EDTA
-
Vigna unguiculata
1.4.1.2 isocitrate
-
Vigna unguiculata
1.4.1.2 L-aspartate
-
Vigna unguiculata
1.4.1.2 p-hydroxymercuribenzoate
-
Vigna unguiculata
1.4.1.2 Pyruvic acid
-
Vigna unguiculata

Organism

EC Number Organism UniProt Comment Textmining
1.4.1.2 Vigna unguiculata
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.4.1.2
-
Vigna unguiculata

Source Tissue

EC Number Source Tissue Comment Organism Textmining
1.4.1.2 seedling
-
Vigna unguiculata
-

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 additional information
-
-
Vigna unguiculata

Storage Stability

EC Number Storage Stability Organism
1.4.1.2 -20°C, several months Vigna unguiculata
1.4.1.2 -5°C, 20% loss of activity after 3 months Vigna unguiculata

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.4.1.2 L-glutamate + H2O + NAD+
-
Vigna unguiculata 2-oxoglutarate + NH3 + NADH + H+
-
?
1.4.1.2 L-norvaline + H2O + NAD+ at 40% the rate Vigna unguiculata 2-oxopentanoate + NH3 + NADH
-
?
1.4.1.2 L-serine + H2O + NAD+ deamination at 29% the rate of L-glutamate deamination Vigna unguiculata 3-hydroxy-2-oxopropanoate + NH3 + NADH
-
?

Cofactor

EC Number Cofactor Comment Organism Structure
1.4.1.2 NAD+
-
Vigna unguiculata
1.4.1.2 NADH
-
Vigna unguiculata
1.4.1.2 NADPH activity with NADH, NADPH and NAD+ in the ratio 126:2:1 Vigna unguiculata