1.5.1.8: saccharopine dehydrogenase (NADP+, L-lysine-forming) This is an abbreviated version! For detailed information about saccharopine dehydrogenase (NADP+, L-lysine-forming), go to the full flat file .
Reaction
N6-(L-1,3-dicarboxypropyl)-L-lysine +
NADP+ +
H2O =
L-lysine +
2-oxoglutarate +
NADPH +
H+
Synonyms AasS, dehydrogenase, saccharopine (nicotinamide adenine dinucleotide phosphate, lysine-forming), L-lysine-alpha-ketoglutarate reductase, LKR, LKR/SDH, LOR, LOR-SDH, lysine 2-oxoglutarate reductase, lysine 2-oxoglutarate reductase-saccharopine dehydrogenase, lysine alpha-ketoglutarate reductase, lysine ketoglutarate reductase, lysine ketoglutarate/reductase saccharopine dehydrogenase, lysine-2-oxoglutarate reductase, lysine-alpha-ketoglutarate reductase, lysine-ketoglutarate reductase, lysine-ketoglutarate reductase/saccharopine dehydrogenase, lysine-ketoglutaric reductase, lysine:alpha-ketoglutarate:TPNH oxidoreductase (epsilon-N-[glutaryl-2]-L-lysine forming), nllkr/sdh, saccharopine (nicotinamide adenine dinucleotide phosphate, lysine-forming) dehydrogenase, saccharopine dehydrogenase, saccharopine dehydrogenase (NADP, lysine-forming), saccharopine dehydrogenase (nicotinamide adenine dinucleotide phosphate, lysine-forming)
ECTree
Metals Ions
Metals Ions on EC 1.5.1.8 - saccharopine dehydrogenase (NADP+, L-lysine-forming)
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Ca2+
-
0.5 mM Ca+ used in assay conditions
Ca2+
-
activates, lysine 2-oxoglutarate reductase activity is modulated by Ca2+, possible modulation of an inhibitory domain
Ca2+
activates the LKR domain activity
Ca2+
-
0.5 mM Ca+ used in assay conditions
Ca2+
-
activates, lysine 2-oxoglutarate reductase activity is modulated by Ca2+, possible modulation of an inhibitory domain
Ca2+
-
activates separated lysine-oxoglutarate reductase domain and this domain in bifunctional protein, Ca2+ may be the most important physiological modulator of enzyme activity, it possibly activates through the derepression of an inhibitory domain in vivo
Ca2+
A0A3L6FCN0
activates the LKR domain activity
Mg2+
activates the LKR domain activity
Mg2+
-
activates at millimolar concentrations
Mg2+
A0A3L6FCN0
activates the LKR domain activity
Salt
-
activated by high salt concentrations
Salt
-
lysine 2-oxoglutarate reductase domain is modulated by ionic strength
Salt
-
activated by high salt concentrations
Salt
-
lysine 2-oxoglutarate reductase domain is modulated by ionic strength
Salt
-
e.g. NaCl or KCl, high salt concentrations activate bifunctional enzyme, but not separated lysine-oxoglutarate reductase domain, 15fold increase of enzyme activity when salt concentration is increased from 0 to 200 mM, effect is due to decreased water activity which could induce conformational modification in LOR domain of enzyme or activation may result from stabilizing effect of the dimeric form of enzyme