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Literature summary for 1.5.1.8 extracted from

  • Markovitz, P.J.; Chuang, D.T.
    The bifunctional aminoadipic semialdehyde synthase in lysine degradation. Separation of reductase and dehydrogenase domains by limited proteolysis and column chromatography (1987), J. Biol. Chem., 262, 9353-9358.
    View publication on PubMed
Search for more literature for 1.5.1.8

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
-

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
420000
-
 sedimentation equilibrium method, single protein with lysine-ketoglutarate reductase EC 1.5.1.8 and saccharopine dehydrogenase EC 1.5.1.9 activities: aminoadipic semialdehyde synthase, but reductase and dehydrogenase domains are separately folded and functionally independent of each other Bos taurus

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
L-lysine + 2-oxoglutarate + NADPH Homo sapiens
-
 N6-(L-1,3-dicarboxypropyl)-L-lysine + NADP+ + H2O
-
 ?
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 Neurospora sp. biosynthetic pathway of lysine in yeast and fungi N6-(L-1,3-dicarboxypropyl)-L-lysine + NADP+ + H2O
-
 ?
L-lysine + 2-oxoglutarate + NADPH Bos taurus major catabolic pathway of lysine in mammalian livers N6-(L-1,3-dicarboxypropyl)-L-lysine + NADP+ + H2O
-
 ?

Organism

Organism UniProt Comment Textmining
Bos taurus
-
-
-
Homo sapiens
-
-
-
Neurospora sp.
-
-
-
Saccharomyces cerevisiae
-
-
-

Purification (Commentary)

Purification (Comment) Organism
separation of lysine-ketoglutarate reductase and saccharopine dehydrogenase activities by limited proteolysis with elastase, chymotrypsin, and papain Bos taurus
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
-

Specific Activity [micromol/min/mg]

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

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-lysine + 2-oxoglutarate + NADPH
-
 Homo sapiens N6-(L-1,3-dicarboxypropyl)-L-lysine + NADP+ + H2O
-
 ?
L-lysine + 2-oxoglutarate + NADPH enzyme catalyzes lysine synthesis from saccharopine, reverse direction is favoured 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 synthesis from saccharopine, reverse direction is favoured Neurospora sp. 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 Homo sapiens N6-(L-1,3-dicarboxypropyl)-L-lysine + NADP+ + H2O epsilon-N-(L-glutaryl-2)-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 epsilon-N-(L-glutaryl-2)-L-lysine is identical with saccharopine ?
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 biosynthetic pathway of lysine in yeast and fungi Saccharomyces cerevisiae N6-(L-1,3-dicarboxypropyl)-L-lysine + NADP+ + H2O
-
 ?
L-lysine + 2-oxoglutarate + NADPH biosynthetic pathway of lysine in yeast and fungi Neurospora sp. N6-(L-1,3-dicarboxypropyl)-L-lysine + NADP+ + H2O
-
 ?
L-lysine + 2-oxoglutarate + NADPH major catabolic pathway of lysine in mammalian livers Bos taurus 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 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 ?
-
 ?

Subunits

Subunits Comment Organism
homotetramer limited proteolysis of aminoadipic semialdehyde synthase results in two fragments: 62700 with lysine-ketoglutarate reductase activity and 49200 with saccharopine dehydrogenase activity 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 Bos taurus

Temperature Optimum [°C]

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

Cofactor

Cofactor Comment Organism Structure
NADPH
-
 Homo sapiens
NADPH
-
 Bos taurus