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Literature summary extracted from
- 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.
Application
| EC Number | Application | Comment | Organism |
|---|---|---|---|
| 1.5.1.8 | 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
| EC Number | Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|---|
| 1.5.1.8 | mitochondrion | - |
Homo sapiens | 5739 | - |
| 1.5.1.8 | mitochondrion | - |
Bos taurus | 5739 | - |
| 1.5.1.9 | mitochondrion | - |
Bos taurus | 5739 | - |
Molecular Weight [Da]
| EC Number | Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|---|
| 1.5.1.8 | 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 |
| 1.5.1.8 | 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 |
| 1.5.1.9 | 115000 | - |
4 * 115000, SDS-PAGE, lysine-ketoglutarate reductase (EC 1. 5.1.8) and saccharopine dehydrogenase activity (EC 1.5.1.9) occur on a single protein, called aminoadipic semialdehyde synthase | Bos taurus |
| 1.5.1.9 | 420000 | - |
sedimentation equilibrium method | Bos taurus |
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 | Homo sapiens | - |
N6-(L-1,3-dicarboxypropyl)-L-lysine + NADP+ + H2O | - |
? |  |
| 1.5.1.8 | L-lysine + 2-oxoglutarate + NADPH | Saccharomyces cerevisiae | biosynthetic pathway of lysine in yeast and fungi | N6-(L-1,3-dicarboxypropyl)-L-lysine + NADP+ + H2O | - |
? | |
| 1.5.1.8 | L-lysine + 2-oxoglutarate + NADPH | Neurospora sp. | biosynthetic pathway of lysine in yeast and fungi | N6-(L-1,3-dicarboxypropyl)-L-lysine + NADP+ + H2O | - |
? | |
| 1.5.1.8 | L-lysine + 2-oxoglutarate + NADPH | Bos taurus | major catabolic pathway of lysine in mammalian livers | N6-(L-1,3-dicarboxypropyl)-L-lysine + NADP+ + H2O | - |
? | |
| 1.5.1.9 | N6-(L-1,3-dicarboxypropyl)-L-lysine + NAD+ + H2O | Bos taurus | involved in lysine catabolism | L-glutamate + 2-aminoadipate 6-semialdehyde + NADH + H+ | - |
r | |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 1.5.1.8 | Bos taurus | - |
- |
- |
| 1.5.1.8 | Homo sapiens | - |
- |
- |
| 1.5.1.8 | Neurospora sp. | - |
- |
- |
| 1.5.1.8 | Saccharomyces cerevisiae | - |
- |
- |
| 1.5.1.9 | Bos taurus | - |
lysine-ketoglutarate reductase (EC 1. 5.1.8) and saccharopine dehydrogenase activity (EC 1.5.1.9) occur on a single protein, called aminoadipic semialdehyde synthase | - |
Purification (Commentary)
| EC Number | Purification (Comment) | Organism |
|---|---|---|
| 1.5.1.8 | separation of lysine-ketoglutarate reductase and saccharopine dehydrogenase activities by limited proteolysis with elastase, chymotrypsin, and papain | Bos taurus |
| 1.5.1.8 | 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 |
| 1.5.1.9 | lysine-ketoglutarate reductase (EC 1. 5.1.8) and saccharopine dehydrogenase activity (EC 1.5.1.9) occur on a single protein, called aminoadipic semialdehyde synthase | Bos taurus |
Source Tissue
| EC Number | Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|---|
| 1.5.1.8 | liver | - |
Homo sapiens | - |
| 1.5.1.8 | liver | - |
Bos taurus | - |
| 1.5.1.9 | liver | - |
Bos taurus | - |
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 | 17 | - |
- |
Bos taurus |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 1.5.1.8 | L-lysine + 2-oxoglutarate + NADPH | - |
Homo sapiens | N6-(L-1,3-dicarboxypropyl)-L-lysine + NADP+ + H2O | - |
? | |
| 1.5.1.8 | 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 | ? | |
| 1.5.1.8 | 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 | ? | |
| 1.5.1.8 | 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 | ? | |
| 1.5.1.8 | 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 | ? | |
| 1.5.1.8 | 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 | ? | |
| 1.5.1.8 | 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 | ? | |
| 1.5.1.8 | L-lysine + 2-oxoglutarate + NADPH | biosynthetic pathway of lysine in yeast and fungi | Saccharomyces cerevisiae | N6-(L-1,3-dicarboxypropyl)-L-lysine + NADP+ + H2O | - |
? | |
| 1.5.1.8 | L-lysine + 2-oxoglutarate + NADPH | biosynthetic pathway of lysine in yeast and fungi | Neurospora sp. | N6-(L-1,3-dicarboxypropyl)-L-lysine + NADP+ + H2O | - |
? | |
| 1.5.1.8 | L-lysine + 2-oxoglutarate + NADPH | major catabolic pathway of lysine in mammalian livers | Bos taurus | 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 | Homo sapiens | ? | - |
? | |
| 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 | Bos taurus | ? | - |
? | |
| 1.5.1.9 | N6-(L-1,3-dicarboxypropyl)-L-lysine + NAD+ + H2O | - |
Bos taurus | L-glutamate + 2-aminoadipate 6-semialdehyde + NADH + H+ | - |
r | |
| 1.5.1.9 | N6-(L-1,3-dicarboxypropyl)-L-lysine + NAD+ + H2O | involved in lysine catabolism | Bos taurus | L-glutamate + 2-aminoadipate 6-semialdehyde + NADH + H+ | - |
r | |
Subunits
| EC Number | Subunits | Comment | Organism |
|---|---|---|---|
| 1.5.1.8 | 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 |
| 1.5.1.8 | 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 |
| 1.5.1.9 | tetramer | 4 * 115000, SDS-PAGE, lysine-ketoglutarate reductase (EC 1. 5.1.8) and saccharopine dehydrogenase activity (EC 1.5.1.9) occur on a single protein, called aminoadipic semialdehyde synthase | Bos taurus |
Temperature Optimum [°C]
| EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 1.5.1.8 | 37 | - |
assay at | Homo sapiens |
| 1.5.1.8 | 37 | - |
assay at | Bos taurus |
Cofactor
| EC Number | Cofactor | Comment | Organism | Structure |
|---|---|---|---|---|
| 1.5.1.8 | NADPH | - |
Homo sapiens | |
| 1.5.1.8 | NADPH | - |
Bos taurus | |
| 1.5.1.9 | NAD+ | - |
Bos taurus | |
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