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Literature summary for 1.5.1.8 extracted from

  • Markovitz, P.J.; Chuang, D.T.; Cox, R.P.
    Familial hyperlysinemias. Purification and characterization of the bifunctional aminoadipic semialdehyde synthase with lysine-ketoglutarate reductase and saccharopine dehydrogenase activities (1984), J. Biol. Chem., 259, 11643-11646.
    View publication on PubMed

Application

Application Comment Organism
medicine autosomal recessive familial hyperlysinemia type I: combined deficiency in lysine-ketoglutarate reductase and saccharopine dehydrogenase activities, EC 1.5.1.8 and EC 1.5.1.9 Homo sapiens

Localization

Localization Comment Organism GeneOntology No. Textmining
mitochondrion
-
Homo sapiens 5739
-
mitochondrion
-
Bos taurus 5739
-
mitochondrion
-
Papio sp. 5739
-

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
115000
-
4 * 115000, single protein with lysine-ketoglutarate reductase EC 1.5.1.8 and saccharopine dehydrogenase EC 1.5.1.9 activities, SDS-PAGE Bos taurus
115000
-
4 * 115000, single protein with lysine-ketoglutarate reductase EC 1.5.1.8 and saccharopine dehydrogenase EC 1.5.1.9 activities, SDS-PAGE Papio sp.
467000
-
gel filtration, single protein catalyzes both lysine-ketoglutarate reductase reaction EC 1.5.1.8 and saccharopine dehydrogenase reaction EC 1.5.1.9, bifunctional enzyme: aminoadipic semialdehyde synthase Papio sp.
468000
-
gel filtration, single protein catalyzes both lysine-ketoglutarate reductase reaction EC 1.5.1.8 and saccharopine dehydrogenase reaction EC 1.5.1.9, bifunctional enzyme: aminoadipic semialdehyde synthase Bos taurus

Organism

Organism UniProt Comment Textmining
Bos taurus
-
-
-
Homo sapiens
-
-
-
Papio sp.
-
-
-

Purification (Commentary)

Purification (Comment) Organism
500fold purification of a single protein with lysine-ketoglutarate reductase EC 1.5.1.8 and saccharopine dehydrogenase EC 1.5.1.9 activities Papio sp.
single protein with lysine-ketoglutarate reductase EC 1.5.1.8 and saccharopine dehydrogenase EC 1.5.1.9 activities: aminoadipic semialdehyde synthase Bos taurus

Source Tissue

Source Tissue Comment Organism Textmining
liver
-
Homo sapiens
-
liver
-
Bos taurus
-
liver
-
Papio sp.
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
17
-
-
Bos taurus
17.1
-
-
Papio sp.

Storage Stability

Storage Stability Organism
-70°C, 6 months, stable Papio sp.

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-lysine + 2-oxoglutarate + NADPH enzyme catalyzes lysine degradation to saccharopine Homo sapiens 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 Bos taurus 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 Papio sp. N6-(L-1,3-dicarboxypropyl)-L-lysine + NADP+ + H2O N6-(L-1,3-dicarboxypropyl)-L-lysine is identical with saccharopine ?
additional information bifunctional enzyme with lysine-oxoglutarate reductase EC 1.5.1.8 and saccharopine dehydrogenase EC 1.5.1.9 activities Homo sapiens ?
-
?
additional information bifunctional enzyme with lysine-oxoglutarate reductase EC 1.5.1.8 and saccharopine dehydrogenase EC 1.5.1.9 activities Bos taurus ?
-
?
additional information bifunctional enzyme with lysine-oxoglutarate reductase EC 1.5.1.8 and saccharopine dehydrogenase EC 1.5.1.9 activities Papio sp. ?
-
?

Subunits

Subunits Comment Organism
homotetramer 4 * 115000, single protein with lysine-ketoglutarate reductase EC 1.5.1.8 and saccharopine dehydrogenase EC 1.5.1.9 activities, SDS-PAGE Bos taurus
homotetramer 4 * 115000, single protein with lysine-ketoglutarate reductase EC 1.5.1.8 and saccharopine dehydrogenase EC 1.5.1.9 activities, SDS-PAGE Papio sp.

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
assay at Homo sapiens
37
-
assay at Bos taurus
37
-
assay at Papio sp.

Cofactor

Cofactor Comment Organism Structure
NADPH
-
Homo sapiens
NADPH
-
Bos taurus
NADPH
-
Papio sp.