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Literature summary for 1.4.1.3 extracted from

  • Yang, S.J.; Huh, J.W.; Lee, J.E.; Choi, S.Y.; Kim, T.U.; Cho, S.W.
    Inactivation of human glutamate dehydrogenase by aluminum (2003), Cell. Mol. Life Sci., 60, 2538-2546.
    View publication on PubMed

Protein Variants

Protein Variants Comment Organism
E279G mutant enzyme is unable to bind NAD+, no difference in sensitivity to aluminum binding between wild-type and mutant enzyme Homo sapiens
K450G mutant enzyme is unable to bind GTP, no difference in sensitivity to aluminum binding between wild-type and mutant enzyme Homo sapiens
Y187G mutant enzyme is unable to bind ADP, no difference in sensitivity to aluminum binding between wild-type and mutant enzyme Homo sapiens

Inhibitors

Inhibitors Comment Organism Structure
AlCl3 increase in sensitivity to aluminium as pH decreases, inhibitory effect is predominant below pH 7.0, no effect above pH 8.5. Completely inactivated enzyme contains 2 mol of aluminum per mol of subunit. Citrate, NaF, N-(2-hydroxyethyl) ethylenediaminetriacetic acid or EDTA efficiently protects against inactivation. Citrate and NaF release aluminum from the completely inactivated aluminum-enzyme complex and fully recover enzyme activity. Binding of aluminum induces a decrease in alpha helices and beta sheets and an increase in random coil Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2-oxoglutarate + NADH + NH3
-
Homo sapiens L-glutamate + NAD+ + H2O
-
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Cofactor

Cofactor Comment Organism Structure
NADH
-
Homo sapiens