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Literature summary for 1.4.1.2 extracted from

  • Griffin, J.; Engel, P.C.
    The -SH protection method for determining accurate K(d) values for enzyme-coenzyme complexes of NAD-dependent glutamate dehydrogenase and engineered mutants: evidence for nonproductive NADPH complexes (2010), Enzyme Res., 2010, 951472.
    View publication on PubMedView publication on EuropePMC

Protein Variants

Protein Variants Comment Organism
D263K site-directed mutagenesis, the mutant shows altered binding kinetics for cofactors compared to the wild-type enzyme, the mutant shows increased dissociation constants for NAD+, NADH, and NADPH, but decreased for DTNB leading to inactivation by the inhibitor [Clostridium] symbiosum
F238S site-directed mutagenesis, the mutant shows altered binding kinetics for cofactors compared to the wild-type enzyme, the mutant shows increased dissociation constants [Clostridium] symbiosum
F238S/P262S site-directed mutagenesis, the mutant shows altered binding kinetics for cofactors compared to the wild-type enzyme, the mutant shows increased dissociation constants [Clostridium] symbiosum
P262S site-directed mutagenesis, the mutant shows altered binding kinetics for cofactors compared to the wild-type enzyme, the mutant shows increased dissociation constants [Clostridium] symbiosum

Inhibitors

Inhibitors Comment Organism Structure
DTNB inactivation via blocking of the only two Cys residues, Cys144 in helix alpha7a of domain I, the substrate-binding domain, and Cys320 in a loop that connects betak and alpha13 in domain II, the coenzyme-binding domain [Clostridium] symbiosum
NADPH the wrong cofactor, NADPH, without the correct binding pocket to receive its 2'-phosphate, finds an alternative and catalytically unproductive way of occupying the coenzyme site [Clostridium] symbiosum

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
additional information dissociation constants of wild-type and mutant enzymes for different coenzymes, overview [Clostridium] symbiosum

Natural Substrates/ Products (Substrates)

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

Organism

Organism UniProt Comment Textmining
[Clostridium] symbiosum P24295
-
-

Substrates and Products (Substrate)

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

Synonyms

Synonyms Comment Organism
GDH
-
[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 [Clostridium] symbiosum

Cofactor

Cofactor Comment Organism Structure
NAD+
-
[Clostridium] symbiosum

Ki Value [mM]

Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
additional information
-
additional information pseudo-first-order kinetic plots for inactivation of F238S GDH by DTNB, overview [Clostridium] symbiosum