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Literature summary for 1.4.1.4 extracted from

  • DeLuna, A.; Avendano, A.; Riego, L.; Gonzalez, A.
    NADP-glutamate dehydrogenase isoenzymes of Saccharomyces cerevisiae. Purification, kinetic properties, and physiological roles (2001), J. Biol. Chem., 276, 43775-43783.
    View publication on PubMed

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.0105
-
NADP+ oxidative deamination, Gdh3p gene Saccharomyces cerevisiae
0.0113
-
NADPH reductive amination, Gdh1p gene Saccharomyces cerevisiae
0.0141
-
NADP+ oxidative deamination, Gdh1p gene Saccharomyces cerevisiae
0.0331
-
NADPH reductive amination, Gdh3p gene Saccharomyces cerevisiae
5
-
NH3 reductive amination, Gdh3p gene Saccharomyces cerevisiae
5.96
-
NH3 reductive amination, Gdh1p gene Saccharomyces cerevisiae
6.36
-
L-glutamate oxidative deamination, Gdh3p gene Saccharomyces cerevisiae
9.79
-
L-glutamate oxidative deamination, Gdh1p gene Saccharomyces cerevisiae

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
L-glutamate + NADP+ + H2O Saccharomyces cerevisiae
-
2-oxoglutarate + NADPH + NH3
-
r

Organism

Organism UniProt Comment Textmining
Saccharomyces cerevisiae
-
contains two NADPH-dependent glutamate dehydrogenases
-

Purification (Commentary)

Purification (Comment) Organism
-
Saccharomyces cerevisiae

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-glutamate + NADP+ + H2O
-
Saccharomyces cerevisiae 2-oxoglutarate + NADPH + NH3
-
r

Cofactor

Cofactor Comment Organism Structure
NADP+
-
Saccharomyces cerevisiae
NADPH
-
Saccharomyces cerevisiae