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Literature summary for 1.5.1.7 extracted from

  • Xu, H.; West, A.H.; Cook, P.F.
    Overall kinetic mechanism of saccharopine dehydrogenase from Saccharomyces cerevisiae (2006), Biochemistry, 45, 12156-12166.
    View publication on PubMed

Inhibitors

Inhibitors Comment Organism Structure
alpha-ketoglutarate substrate inhibition, uncompetitive versus NADH Saccharomyces cerevisiae
L-lysine substrate inhibition, competitive versus NADH Saccharomyces cerevisiae
additional information detailed analysis of inhibition patterns for product and dead end inhibitors Saccharomyces cerevisiae
saccharopine product inhibition, uncompetitive versus NADH Saccharomyces cerevisiae

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.019
-
NADH 25°C, pH 7.0 Saccharomyces cerevisiae
0.9
-
NAD+ 25°C, pH 7.0 Saccharomyces cerevisiae
1.1
-
L-lysine 25°C, pH 7.0 Saccharomyces cerevisiae
6.7
-
N6-(L-1,3-dicarboxypropyl)-L-lysine 25°C, pH 7.0 Saccharomyces cerevisiae

Organism

Organism UniProt Comment Textmining
Saccharomyces cerevisiae
-
-
-

Reaction

Reaction Comment Organism Reaction ID
N6-(L-1,3-dicarboxypropyl)-L-lysine + NAD+ + H2O = L-lysine + 2-oxoglutarate + NADH + H+ ordered addition of NAD followed by saccharopine in the physiologic reaction direction. In the opposite direction, NADH adds to the enzyme first, while there is no preference for the order of binding of alpha-ketoglutarate and lysine Saccharomyces cerevisiae

Substrates and Products (Substrate)

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

Ki Value [mM]

Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
27.8
-
L-lysine 25°C, pH 7.0 Saccharomyces cerevisiae
28
-
alpha-ketoglutarate 25°C, pH 7.0 Saccharomyces cerevisiae