EC Number   |
Substrates |
Organism |
Products  |
Reversibility |
|---|
    1.5.1.9 | more |
the enzyme is bifunctional catalyzing the reaction of EC 1.5.1.8, saccharopine dehydrogenase (NADP+, L-lysine-forming) in the reverse direction, and EC 1.5.1.9, saccharopine dehydrogenase (NAD+, L-glutamate-forming) |
Nilaparvata lugens |
? |
- |
? |
| 1.5.1.9 | more |
the bifunctional enzyme lysine-ketoglutarate reductase/saccharopine dehydrogenase (LKR/SDH) comprises a LKR domain, which condenses lysine and 2-oxoglutarate into saccharopine, and the SDH domain, that hydrolyzes saccharopine to form glutamate and alpha-aminoadipate semialdehyde, the latter of which is oxidized to alpha-aminoadipate by aminoadipate semialdehyde dehydrogenase (AASADH) |
Zea mays |
? |
- |
- |
| 1.5.1.9 | more |
the bifunctional enzyme lysine-ketoglutarate reductase/saccharopine dehydrogenase (LKR/SDH) comprises a LKR domain, which condenses lysine and 2-oxoglutarate into saccharopine, and the SDH domain, that hydrolyzes saccharopine to form glutamate and alpha-aminoadipate semialdehyde, the latter of which is oxidized to alpha-aminoadipate by aminoadipate semialdehyde dehydrogenase (AASADH) |
Oryza sativa |
? |
- |
- |
| 1.5.1.9 | more |
the bifunctional enzyme lysine-ketoglutarate reductase/saccharopine dehydrogenase (LKR/SDH) comprises a LKR domain, which condenses lysine and 2-oxoglutarate into saccharopine, and the SDH domain, that hydrolyzes saccharopine to form glutamate and alpha-aminoadipate semialdehyde, the latter of which is oxidized to alpha-aminoadipate by aminoadipate semialdehyde dehydrogenase (AASADH) |
Brassica napus |
? |
- |
- |
| 1.5.1.9 | more |
the bifunctional enzyme lysine-ketoglutarate reductase/saccharopine dehydrogenase (LKR/SDH) comprises a LKR domain, which condenses lysine and 2-oxoglutarate into saccharopine, and the SDH domain, that hydrolyzes saccharopine to form glutamate and alpha-aminoadipate semialdehyde, the latter of which is oxidized to alpha-aminoadipate by aminoadipate semialdehyde dehydrogenase (AASADH) |
Homo sapiens |
? |
- |
- |
| 1.5.1.9 | more |
the bifunctional enzyme lysine-ketoglutarate reductase/saccharopine dehydrogenase (LKR/SDH) comprises a LKR domain, which condenses lysine and 2-oxoglutarate into saccharopine, and the SDH domain, that hydrolyzes saccharopine to form glutamate and alpha-aminoadipate semialdehyde, the latter of which is oxidized to alpha-aminoadipate by aminoadipate semialdehyde dehydrogenase (AASADH). Monofunctional SDH has also been found in animals and in Arabidopsis thaliana |
Arabidopsis thaliana |
? |
- |
- |
| 1.5.1.9 | N6-(L-1,3-dicarboxypropyl)-L-lysine + NAD+ + H2O |
- |
Arabidopsis sp. |
L-Glu + 2-aminoadipate 6-semialdehyde + NADH |
- |
? |
| 1.5.1.9 | N6-(L-1,3-dicarboxypropyl)-L-lysine + NAD+ + H2O |
the bifunctional reductase/saccharopine dehydrogenase contains the first two enzyme of lysine catabolism, is concertedly regulated by metabolic and stress-associated signals. The level of the bifunctional enzyme is strongly enhanced by abscisic acid, jasmonate, and sugar starvation, whereas excess sugars and nitrogen starvation reduce its level |
Arabidopsis sp. |
L-Glu + 2-aminoadipate 6-semialdehyde + NADH |
- |
? |
| 1.5.1.9 | N6-(L-1,3-dicarboxypropyl)-L-lysine + NAD+ + H2O |
- |
Hordeum vulgare |
L-glutamate + (S)-2-amino-6-oxohexanoate + NADH + H+ |
- |
? |
| 1.5.1.9 | N6-(L-1,3-dicarboxypropyl)-L-lysine + NAD+ + H2O |
- |
Triticum turgidum |
L-glutamate + (S)-2-amino-6-oxohexanoate + NADH + H+ |
- |
? |
