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Literature summary extracted from

  • Miron, D.; Ben-Yaacov, S.; Reches, D.; Schupper, A.; Galili, G.
    Purification and characterization of bifunctional lysine-ketoglutarate reductase/saccharopine dehydrogenase from developing soybean seeds (2000), Plant Physiol., 123, 655-663.
    View publication on PubMedView publication on EuropePMC

Protein Variants

EC Number Protein Variants Comment Organism
1.5.1.8 additional information high-Lys opaque-2 mutant has significantly reduced LKR activity Zea mays

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.5.1.8 Alkaline phosphatase reduces LKR activity Glycine max

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.5.1.8 3.7
-
2-oxoglutarate
-
Glycine max
1.5.1.8 13.7
-
L-lysine
-
Glycine max

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.5.1.8 123000
-
2 * 123000, bifunctional protein with lysine-ketoglutarate reductase EC 1.5.1.8 and saccharopine dehydrogenase EC 1.5.1.9 activities, additional 100 kDa band is a proteolytic cleavage product, SDS-PAGE Glycine max
1.5.1.8 256000
-
gel filtration, bifunctional protein with lysine-ketoglutarate reductase EC 1.5.1.8 and saccharopine dehydrogenase EC 1.5.1.9 activities Glycine max

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.5.1.8 L-lysine + 2-oxoglutarate + NADPH Zea mays
-
N6-(L-1,3-dicarboxypropyl)-L-lysine + NADP+ + H2O
-
?
1.5.1.8 L-lysine + 2-oxoglutarate + NADPH Oryza sativa
-
N6-(L-1,3-dicarboxypropyl)-L-lysine + NADP+ + H2O
-
?
1.5.1.8 L-lysine + 2-oxoglutarate + NADPH Glycine max first and possibly a rate-limiting step in lysine catabolism N6-(L-1,3-dicarboxypropyl)-L-lysine + NADP+ + H2O
-
?
1.5.1.8 L-lysine + 2-oxoglutarate + NADPH Glycine max 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

EC Number Organism UniProt Comment Textmining
1.5.1.8 Glycine max
-
-
-
1.5.1.8 Oryza sativa
-
-
-
1.5.1.8 Zea mays
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.5.1.8 1630.5fold purification of a bifunctional protein containing lysine-ketoglutarate reductase EC 1.5.1.8 and saccharopine dehydrogenase EC 1.5.1.9 activities Glycine max

Source Tissue

EC Number Source Tissue Comment Organism Textmining
1.5.1.8 seed developing Zea mays
-
1.5.1.8 seed developing Glycine max
-
1.5.1.8 seed developing Oryza sativa
-

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
1.5.1.8 3.261
-
-
Glycine max

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.5.1.8 L-lysine + 2-oxoglutarate + NADPH
-
Zea mays N6-(L-1,3-dicarboxypropyl)-L-lysine + NADP+ + H2O
-
?
1.5.1.8 L-lysine + 2-oxoglutarate + NADPH
-
Oryza sativa N6-(L-1,3-dicarboxypropyl)-L-lysine + NADP+ + H2O
-
?
1.5.1.8 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 ?
1.5.1.8 L-lysine + 2-oxoglutarate + NADPH enzyme catalyzes lysine degradation to saccharopine Glycine max N6-(L-1,3-dicarboxypropyl)-L-lysine + NADP+ + H2O N6-(L-1,3-dicarboxypropyl)-L-lysine is identical with saccharopine ?
1.5.1.8 L-lysine + 2-oxoglutarate + NADPH enzyme catalyzes lysine degradation to saccharopine Oryza sativa N6-(L-1,3-dicarboxypropyl)-L-lysine + NADP+ + H2O N6-(L-1,3-dicarboxypropyl)-L-lysine is identical with saccharopine ?
1.5.1.8 L-lysine + 2-oxoglutarate + NADPH first and possibly a rate-limiting step in lysine catabolism Glycine max N6-(L-1,3-dicarboxypropyl)-L-lysine + NADP+ + H2O
-
?
1.5.1.8 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 Glycine max N6-(L-1,3-dicarboxypropyl)-L-lysine + NADP+ + H2O
-
?
1.5.1.8 additional information bifunctional enzyme with lysine-oxoglutarate reductase EC 1.5.1.8 and saccharopine dehydrogenase EC 1.5.1.9 activities Zea mays ?
-
?
1.5.1.8 additional information bifunctional enzyme with lysine-oxoglutarate reductase EC 1.5.1.8 and saccharopine dehydrogenase EC 1.5.1.9 activities Glycine max ?
-
?
1.5.1.8 additional information bifunctional enzyme with lysine-oxoglutarate reductase EC 1.5.1.8 and saccharopine dehydrogenase EC 1.5.1.9 activities Oryza sativa ?
-
?

Subunits

EC Number Subunits Comment Organism
1.5.1.8 homodimer
-
Zea mays
1.5.1.8 homodimer
-
Oryza sativa
1.5.1.8 homodimer 2 * 123000, bifunctional protein with lysine-ketoglutarate reductase EC 1.5.1.8 and saccharopine dehydrogenase EC 1.5.1.9 activities, additional 100 kDa band is a proteolytic cleavage product, SDS-PAGE Glycine max

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
1.5.1.8 30
-
assay at Zea mays
1.5.1.8 30
-
assay at Glycine max
1.5.1.8 30
-
assay at Oryza sativa

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.5.1.8 7.2
-
-
Glycine max

Cofactor

EC Number Cofactor Comment Organism Structure
1.5.1.8 NADPH
-
Zea mays
1.5.1.8 NADPH
-
Glycine max
1.5.1.8 NADPH
-
Oryza sativa