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Literature summary extracted from

  • Xu, H.; Alguindigue, S.S.; West, A.H.; Cook, P.F.
    A proposed proton shuttle mechanism for saccharopine dehydrogenase from Saccharomyces cerevisiae (2007), Biochemistry, 46, 871-882.
    View publication on PubMedView publication on EuropePMC

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.5.1.7 2-oxoglutarate
-
 Saccharomyces cerevisiae
1.5.1.7 L-leucine L-leucine is a competitive inhibitor against L-lysine at pH 6.5-12.5 Saccharomyces cerevisiae
1.5.1.7 L-lysine
-
 Saccharomyces cerevisiae
1.5.1.7 oxalylglycine at pH 5.45 and 9.58, oxalylglycine is competitive versus 2-oxoglutarate Saccharomyces cerevisiae

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.5.1.7 additional information
-
 additional information detailed kinetic analysis including pH-dependance and deuterium kinetic effects Saccharomyces cerevisiae

Organism

EC Number Organism UniProt Comment Textmining
1.5.1.7 Saccharomyces cerevisiae
-
-
-

Reaction

EC Number Reaction Comment Organism Reaction ID
1.5.1.7 N6-(L-1,3-dicarboxypropyl)-L-lysine + NAD+ + H2O = L-lysine + 2-oxoglutarate + NADH + H+ model of proton shuttle mechanism. Concerted proton and hydride transfer, proton transfer exists in at least two sequential transition states Saccharomyces cerevisiae
a

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.5.1.7 N6-(L-1,3-dicarboxypropyl)-L-lysine + NAD+ + H2O
-
 Saccharomyces cerevisiae L-lysine + 2-oxoglutarate + NADH + H+
-
 r

Synonyms

EC Number Synonyms Comment Organism
1.5.1.7 N6-(glutaryl-2)-L-lysine:NAD oxidoreductase (L-lysine forming)
-
 Saccharomyces cerevisiae
1.5.1.7 saccharopine dehydrogenase catalyzes the final step in the alpha-aminoadipate pathway for lysine biosynthesis Saccharomyces cerevisiae
1.5.1.7 SDH
-
 Saccharomyces cerevisiae

Cofactor

EC Number Cofactor Comment Organism Structure
1.5.1.7 NAD+
-
 Saccharomyces cerevisiae