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Literature summary extracted from

  • Fujioka, M.; Nakatani, Y.
    A kinetic study of saccharopine dehydrogenase reaction (1970), Eur. J. Biochem., 16, 180-186.
    View publication on PubMed

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.5.1.7 2-oxoglutarate substrate inhibition Saccharomyces cerevisiae
1.5.1.7 lysine substrate inhibition Saccharomyces cerevisiae
1.5.1.7 NADH substrate inhibition Saccharomyces cerevisiae

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.5.1.7 0.1
-
 NAD+
-
 Saccharomyces cerevisiae
1.5.1.7 1.67
-
 saccharopine
-
 Saccharomyces cerevisiae

Organism

EC Number Organism UniProt Comment Textmining
1.5.1.7 Saccharomyces cerevisiae
-
 baker's yeast
-

Purification (Commentary)

EC Number Purification (Comment) Organism
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+ mechanism Saccharomyces cerevisiae
a

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
1.5.1.7 0.1
-
 crude extract Saccharomyces cerevisiae
1.5.1.7 24.6
-
 after purification Saccharomyces cerevisiae

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 i.e. saccharopine Saccharomyces cerevisiae L-lysine + 2-oxoglutarate + NADH
-
 r

Cofactor

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