1.5.1.9: saccharopine dehydrogenase (NAD+, L-glutamate-forming)
This is an abbreviated version!
For detailed information about saccharopine dehydrogenase (NAD+, L-glutamate-forming), go to the full flat file.
Word Map on EC 1.5.1.9
-
1.5.1.9
-
lysine-ketoglutarate
-
1.5.1.8
-
polyamine
-
alpha-ketoglutarate
-
hyperlysinemias
-
spermidine
-
pipecolate
-
maize
-
ornithine
-
analysis
- 1.5.1.9
-
lysine-ketoglutarate
-
1.5.1.8
- polyamine
- alpha-ketoglutarate
- hyperlysinemias
- spermidine
- pipecolate
- maize
- ornithine
- analysis
Reaction
Synonyms
AasS, alpha-aminoadipic-delta-semialdehehyde synthase, aminoadipic semialdehyde synthase, AtLKR/SDHp, AtSDHp, dehydrogenase, saccharopine (nicotinamide adenine dinucleotide, glutamate-forming), LKR/SDH, LOR-SDH, lysine 2-oxoglutarate reductase-saccharopine dehydrogenase, lysine ketoglutarate/reductase saccharopine dehydrogenase, lysine-ketoglutarate reductase/saccharopine dehydrogenase, NAD+ oxidoreductase (L-2-aminoadipic-delta-semialdehyde and glutamate forming), nllkr/sdh, saccharopin dehydrogenase, saccharopine dehydrogenase, SacD, SDH, spe-sdh
ECTree
Advanced search results
Subunits
Subunits on EC 1.5.1.9 - saccharopine dehydrogenase (NAD+, L-glutamate-forming)
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
dimer
-
2 * 125000, SDS-PAGE, lysine-ketoglutarate reductase (EC 1. 5.1.8) and saccharopine dehydrogenase activity (EC 1.5.1.9) occur on a single protein
tetramer
additional information
?
-
x * 120000, SDS-PAGE, lysine-ketoglutarate reductase (EC 1. 5.1.8) and saccharopine dehydrogenase activity (EC 1.5.1.9) occur on a single protein
-
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
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
the enzyme domains and activities LKR and SDH belong to a single about 120 kDa bifunctional polypeptide. In plants, the LKR and SDH domains of the bifunctional polypeptide are separated from each other by an about 130 amino acid interdomain
additional information
the enzyme domains and activities LKR and SDH belong to a single about 120 kDa bifunctional polypeptide. In plants, the LKR and SDH domains of the bifunctional polypeptide are separated from each other by an about 130 amino acid interdomain
additional information
the enzyme domains and activities LKR and SDH belong to a single about 120 kDa bifunctional polypeptide
additional information
the enzyme domains and activities LKR and SDH belong to a single about 120 kDa bifunctional polypeptide. In plants, the LKR and SDH domains of the bifunctional polypeptide are separated from each other by an about 130 amino acid interdomain