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Literature summary for 1.4.1.2 extracted from

  • Hamza, M.A.; Engel, P.C.
    Homotropic allosteric control in clostridial glutamate dehydrogenase: different mechanisms for glutamate and NAD+? (2008), FEBS Lett., 582, 1816-1820.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Escherichia coli [Clostridium] symbiosum

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
additional information wild-type Vmax: 23.71 (pH 7), 35.16 (pH 9) [Clostridium] symbiosum

Organism

Organism UniProt Comment Textmining
[Clostridium] symbiosum
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-glutamate + H2O + NAD+
-
[Clostridium] symbiosum 2-oxoglutarate + NH3 + NADH
-
?

Synonyms

Synonyms Comment Organism
glutamate dehydrogenase
-
[Clostridium] symbiosum

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
25
-
assay at [Clostridium] symbiosum

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7
-
assay at, the wild-type enzyme displays negative NAD+ cooperativity at pH 7 and pH 9 values [Clostridium] symbiosum
9
-
assay at, the wild-type enzyme displays negative NAD+ cooperativity at pH 7 and pH 9 values [Clostridium] symbiosum

Cofactor

Cofactor Comment Organism Structure
NADH the wild-type enzyme displays negative NAD+ cooperativity at pH 7 and pH 9 values [Clostridium] symbiosum