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Literature summary for 1.4.1.2 extracted from

  • Ruano, A.R.; Riano, J.L.A.; Amil, M.R.; Santos, M.J.H.
    Some enzymatic properties of NAD+-dependent glutamate dehydrogenase of mussel hepatopancreas (Mytilus edulis L.) requirement of ADP (1985), Comp. Biochem. Physiol. B, 82, 197-202.
No PubMed abstract available
Search for more literature for 1.4.1.2

Activating Compound

Activating Compound Comment Organism Structure
ADP absolute requirement as cofactor Mytilus edulis

General Stability

General Stability Organism
2-oxoglutarate stabilizes Mytilus edulis
ADP stabilizes Mytilus edulis
NADH stabilizes Mytilus edulis

Organism

Organism UniProt Comment Textmining
Mytilus edulis
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Mytilus edulis

Source Tissue

Source Tissue Comment Organism Textmining
hepatopancreas
-
 Mytilus edulis
-

Substrates and Products (Substrate)

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

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.4 8.2 reductive amination Mytilus edulis
9.5
-
 oxidative deamination Mytilus edulis

pH Stability

pH Stability pH Stability Maximum Comment Organism
4
-
 15 min, 30°C, inactivation Mytilus edulis
6.5 7.2 15 min, 30°C, stable Mytilus edulis
8
-
 15 min, 30°C, inactivation Mytilus edulis

Cofactor

Cofactor Comment Organism Structure
NAD+
-
 Mytilus edulis
NADH
-
 Mytilus edulis
NADPH less than 1% of the activity with NADH Mytilus edulis