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Literature summary for 1.4.1.2 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

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

Inhibitors

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

Organism

Organism UniProt Comment Textmining
Vigna unguiculata
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Vigna unguiculata

Source Tissue

Source Tissue Comment Organism Textmining
seedling
-
Vigna unguiculata
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
additional information
-
-
Vigna unguiculata

Storage Stability

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

Substrates and Products (Substrate)

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

Cofactor

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