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Literature summary for 1.5.1.8 extracted from

  • Kemper, E.L.; Cord-Neto, G.; Capella, A.N.; Goncalves-Butruile, M.; Azevedo, R.; Arruda, P.
    Structure and regulation of the bifunctional enzyme lysine-oxoglutarate reductase-saccharopine dehydrogenase in maize (1998), Eur. J. Biochem., 253, 720-729.
    View publication on PubMed
Search for more literature for 1.5.1.8

Activating Compound

Activating Compound Comment Organism Structure
L-lysine excess lysine is a major stimulator of enzyme activity Nicotiana tabacum
organic solvent activates Zea mays
organic solvent e.g. poly(ethylene glycol) 8000 and ethyleneglycol increase enzyme activity, but lower increase than by 200 mM Tris/HCl buffer Zea mays
Tris/HCl enzyme activity increases 6fold when the concentration of Tris/HCl is increased from 25 to 200 mM, effect is due to decreased water activity which could induce conformational modification in LOR domain of enzyme Zea mays

Protein Variants

Protein Variants Comment Organism
additional information
-
 Saccharomyces cerevisiae
additional information in endosperm of opaque-2 mutant level of enzyme activity is reduced 2-3fold compared to normal endosperm Zea mays

General Stability

General Stability Organism
stabilization of holoenzyme by high salt concentrations, e.g. KCl Zea mays

Inhibitors

Inhibitors Comment Organism Structure
Calmidazolium 0.04 mM, almost complete inhibition of Ca2+-dependent enhancement of enzyme activity, calmodulin antagonist Zea mays
EGTA 1.6 mM, 70% loss of activity in crude extract, activity can be restored by addition of 1.6 mM CaCl2 Zea mays
additional information lysine-oxoglutarate reductase shows time-dependent and protease-concentration-dependent inactivation by proteolysis followed by reactivation, saccharopine dehydrogenase-containing polypeptides obtained by prolonged digestion inhibit the activity of lysine-oxoglutarate reductase-containing polypeptides Zea mays
N-(6-Aminohexyl)-5-chloro-1-naphthalenesulfonamide 1.5 mM, almost complete inhibition of Ca2+-dependent enhancement of enzyme activity, calmodulin antagonist Zea mays

Metals/Ions

Metals/Ions Comment Organism Structure
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 Zea mays
Mg2+ activates at millimolar concentrations Zea mays
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 Zea mays

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
125000
-
 2 * 125000, bifunctional enzyme with lysine-oxoglutarate reductase EC 1.5.1.8 and saccharopine dehydrogenase EC 1.5.1.9 activities, digestion with elastase separates the functional domains into a 65 kDa polypeptide with LOR activity and a 57 kDa polypeptide with SDH activity, SDS-PAGE Zea mays
260000
-
 bifunctional enzyme with lysine-oxoglutarate reductase EC 1.5.1.8 and saccharopine dehydrogenase EC 1.5.1.9 activities, but domains are functionally independent of each other Zea mays

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
L-lysine + 2-oxoglutarate + NADPH Saccharomyces cerevisiae biosynthetic pathway of lysine in yeast and fungi N6-(L-1,3-dicarboxypropyl)-L-lysine + NADP+ + H2O
-
 ?
L-lysine + 2-oxoglutarate + NADPH Zea mays activity of native enzyme is inhibited after modulation, enzyme undergoes a conformational alteration to expose the catalytic domain for substrate binding, Ca2+ may be the most important physiological modulator of enzyme activity, it possibly activates through the derepression of an inhibitory domain in vivo N6-(L-1,3-dicarboxypropyl)-L-lysine + NADP+ + H2O
-
 ?
L-lysine + 2-oxoglutarate + NADPH Saccharomyces cerevisiae increase in free lysine concentration in cells decrease enzyme activity through repression of lys1 gene, precursor alpha-aminoadipic-delta-semialdehyde modulates a transcriptional factor that controls transcription of lys1 gene N6-(L-1,3-dicarboxypropyl)-L-lysine + NADP+ + H2O
-
 ?
L-lysine + 2-oxoglutarate + NADPH Zea mays lysine catabolism N6-(L-1,3-dicarboxypropyl)-L-lysine + NADP+ + H2O
-
 ?
L-lysine + 2-oxoglutarate + NADPH Nicotiana tabacum enzyme activity is modulated in vivo by a lysine-dependent intracellular signaling cascade, mediated by Ca2+ and protein phosphorylation/dephosphorylation N6-(L-1,3-dicarboxypropyl)-L-lysine + NADP+ + H2O
-
 ?

Organism

Organism UniProt Comment Textmining
Nicotiana tabacum
-
-
-
Saccharomyces cerevisiae
-
-
-
Zea mays
-
 hybrid F-352
-

Purification (Commentary)

Purification (Comment) Organism
partial purification of bifunctional enzyme with lysine-oxoglutarate reductase EC 1.5.1.8 and saccharopine dehydrogenase EC 1.5.1.9 activities Zea mays

Source Tissue

Source Tissue Comment Organism Textmining
endosperm during development Zea mays
-
seed developing Zea mays
-
seed developing Nicotiana tabacum
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
additional information
-
-
 Zea mays
1.273
-
-
 Zea mays

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-lysine + 2-oxoglutarate + NADPH
-
 Saccharomyces cerevisiae N6-(L-1,3-dicarboxypropyl)-L-lysine + NADP+ + H2O N6-(L-1,3-dicarboxypropyl)-L-lysine is identical with saccharopine ?
L-lysine + 2-oxoglutarate + NADPH enzyme catalyzes lysine degradation to saccharopine Zea mays N6-(L-1,3-dicarboxypropyl)-L-lysine + NADP+ + H2O N6-(L-1,3-dicarboxypropyl)-L-lysine is identical with saccharopine ?
L-lysine + 2-oxoglutarate + NADPH enzyme catalyzes lysine degradation to saccharopine Nicotiana tabacum N6-(L-1,3-dicarboxypropyl)-L-lysine + NADP+ + H2O N6-(L-1,3-dicarboxypropyl)-L-lysine is identical with saccharopine ?
L-lysine + 2-oxoglutarate + NADPH biosynthetic pathway of lysine in yeast and fungi Saccharomyces cerevisiae N6-(L-1,3-dicarboxypropyl)-L-lysine + NADP+ + H2O
-
 ?
L-lysine + 2-oxoglutarate + NADPH activity of native enzyme is inhibited after modulation, enzyme undergoes a conformational alteration to expose the catalytic domain for substrate binding, Ca2+ may be the most important physiological modulator of enzyme activity, it possibly activates through the derepression of an inhibitory domain in vivo Zea mays N6-(L-1,3-dicarboxypropyl)-L-lysine + NADP+ + H2O
-
 ?
L-lysine + 2-oxoglutarate + NADPH increase in free lysine concentration in cells decrease enzyme activity through repression of lys1 gene, precursor alpha-aminoadipic-delta-semialdehyde modulates a transcriptional factor that controls transcription of lys1 gene Saccharomyces cerevisiae N6-(L-1,3-dicarboxypropyl)-L-lysine + NADP+ + H2O
-
 ?
L-lysine + 2-oxoglutarate + NADPH lysine catabolism Zea mays N6-(L-1,3-dicarboxypropyl)-L-lysine + NADP+ + H2O
-
 ?
L-lysine + 2-oxoglutarate + NADPH enzyme activity is modulated in vivo by a lysine-dependent intracellular signaling cascade, mediated by Ca2+ and protein phosphorylation/dephosphorylation Nicotiana tabacum N6-(L-1,3-dicarboxypropyl)-L-lysine + NADP+ + H2O
-
 ?
additional information bifunctional enzyme with lysine-oxoglutarate reductase EC 1.5.1.8 and saccharopine dehydrogenase EC 1.5.1.9 activities Zea mays ?
-
 ?

Subunits

Subunits Comment Organism
homodimer 2 * 125000, bifunctional enzyme with lysine-oxoglutarate reductase EC 1.5.1.8 and saccharopine dehydrogenase EC 1.5.1.9 activities, digestion with elastase separates the functional domains into a 65 kDa polypeptide with LOR activity and a 57 kDa polypeptide with SDH activity, SDS-PAGE Zea mays

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
30
-
 assay at Zea mays

Cofactor

Cofactor Comment Organism Structure
NADPH
-
 Zea mays
NADPH
-
 Nicotiana tabacum