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 |
- |
Phaseolus vulgaris |
L-glutamate + 2-aminoadipate 6-semialdehyde + NADH + H+ |
- |
? |
1.5.1.9 | N6-(L-1,3-dicarboxypropyl)-L-lysine + NAD+ + H2O |
- |
Homo sapiens |
L-glutamate + 2-aminoadipate 6-semialdehyde + NADH + H+ |
- |
r |
1.5.1.9 | N6-(L-1,3-dicarboxypropyl)-L-lysine + NAD+ + H2O |
- |
Rattus norvegicus |
L-glutamate + 2-aminoadipate 6-semialdehyde + NADH + H+ |
- |
r |
1.5.1.9 | N6-(L-1,3-dicarboxypropyl)-L-lysine + NAD+ + H2O |
- |
Sus scrofa |
L-glutamate + 2-aminoadipate 6-semialdehyde + NADH + H+ |
- |
r |