| Entry |
|
|---|
| Name |
saccharopine dehydrogenase (NAD+, L-glutamate-forming);
dehydrogenase, saccharopine (nicotinamide adenine dinucleotide, glutamate-forming);
saccharopin dehydrogenase;
NAD+ oxidoreductase (L-2-aminoadipic-delta-semialdehyde and glutamate forming);
aminoadipic semialdehyde synthase;
6-N-(L-1,3-dicarboxypropyl)-L-lysine:NAD+ oxidoreductase (L-glutamate-forming)
|
|---|
| Class |
Oxidoreductases;
Acting on the CH-NH group of donors;
With NAD+ or NADP+ as acceptor
|
|---|
| Sysname |
N6-(L-1,3-dicarboxypropyl)-L-lysine:NAD+ oxidoreductase (L-glutamate-forming)
|
|---|
| Reaction(IUBMB) |
N6-(L-1,3-dicarboxypropyl)-L-lysine + NAD+ + H2O = L-glutamate + (S)-2-amino-6-oxohexanoate + NADH + H+ [RN: R02313]
|
|---|
| Reaction(KEGG) |
|
|---|
| Substrate |
|
|---|
| Product |
|
|---|
| Comment |
The activities of this enzyme along with EC 1.5.1.8, saccharopine dehydrogenase (NADP+, L-lysine-forming), occur on a single protein.
|
|---|
| History |
EC 1.5.1.9 created 1972, modified 2011
|
|---|
| Pathway |
| ec01110 | Biosynthesis of secondary metabolites |
|
|---|
| Orthology |
| K14157 | alpha-aminoadipic semialdehyde synthase |
|
|---|
| Genes |
» show all
|
|---|
| Reference |
|
|---|
| Authors |
Hutzler J, Dancis J. |
|---|
| Title |
Conversion of lysine to saccharopine by human tissues. |
|---|
| Journal |
|
|---|
| Reference |
|
|---|
| Authors |
Markovitz PJ, Chuang DT, Cox RP. |
|---|
| Title |
Familial hyperlysinemias. Purification and characterization of the bifunctional aminoadipic semialdehyde synthase with lysine-ketoglutarate reductase and saccharopine dehydrogenase activities. |
|---|
| Journal |
J Biol Chem 259:11643-6 (1984) |
|---|
| Other DBs |
| ExplorEnz - The Enzyme Database: | 1.5.1.9 |
| ExPASy - ENZYME nomenclature database: | 1.5.1.9 |
| BRENDA, the Enzyme Database: | 1.5.1.9 |
|
|---|
| LinkDB |
|
|---|
