EC |
1.5.1.7 |
Accepted name: |
saccharopine dehydrogenase (NAD+, L-lysine-forming) |
Reaction: |
N6-(L-1,3-dicarboxypropyl)-L-lysine + NAD+ + H2O = L-lysine + 2-oxoglutarate + NADH + H+ |
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For diagram of lysine catabolism, click here and for diagram of L-lysine synthesis, click here |
Glossary: |
L-saccharopine = N6-(L-1,3-dicarboxypropyl)-L-lysine |
Other name(s): |
lysine-2-oxoglutarate reductase; dehydrogenase, saccharopine (nicotinamide adenine dinucleotide, lysine forming); ε-N-(L-glutaryl-2)-L-lysine:NAD oxidoreductase (L-lysine forming); N6-(glutar-2-yl)-L-lysine:NAD oxidoreductase (L-lysine-forming); 6-N-(L-1,3-dicarboxypropyl)-L-lysine:NAD+ oxidoreductase (L-lysine-forming) |
Systematic name: |
N6-(L-1,3-dicarboxypropyl)-L-lysine:NAD+ oxidoreductase (L-lysine-forming) |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9073-96-5 |
References: |
1. |
Fujioka, M. and Nakatani, Y. Saccharopine dehydrogenase. Interaction with substrate analogues. Eur. J. Biochem. 25 (1972) 301–307. [DOI] [PMID: 4339117] |
2. |
Saunders, P.P. and Broquist, H.P. Saccharopine, an intermediate of the aminoadipic acid pathway of lysine biosynthesis. IV. Saccharopine dehydrogenase. J. Biol. Chem. 241 (1966) 3435–3440. [PMID: 4287986] |
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[EC 1.5.1.7 created 1972] |
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EC |
1.5.1.8 |
Accepted name: |
saccharopine dehydrogenase (NADP+, L-lysine-forming) |
Reaction: |
N6-(L-1,3-dicarboxypropyl)-L-lysine + NADP+ + H2O = L-lysine + 2-oxoglutarate + NADPH + H+ |
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Glossary: |
L-saccharopine = N6-(L-1,3-dicarboxypropyl)-L-lysine |
Other name(s): |
lysine-2-oxoglutarate reductase; lysine-ketoglutarate reductase; L-lysine-α-ketoglutarate reductase; lysine:α-ketoglutarate:TPNH oxidoreductase (ε-N-[gultaryl-2]-L-lysine forming); saccharopine (nicotinamide adenine dinucleotide phosphate, lysine-forming) dehydrogenase; 6-N-(L-1,3-dicarboxypropyl)-L-lysine:NADP+ oxidoreductase (L-lysine-forming) |
Systematic name: |
N6-(L-1,3-dicarboxypropyl)-L-lysine:NADP+ oxidoreductase (L-lysine-forming) |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9031-19-0 |
References: |
1. |
Hutzler, J. and Dancis, J. Conversion of lysine to saccharopine by human tissues. Biochim. Biophys. Acta 158 (1968) 62–69. [DOI] [PMID: 4385118] |
2. |
Markovitz, P.J., Chuang, D.T. and Cox, R.P. Familial hyperlysinemias. Purification and characterization of the bifunctional aminoadipic semialdehyde synthase with lysine-ketoglutarate reductase and saccharopine dehydrogenase activities. J. Biol. Chem. 259 (1984) 11643–11646. [PMID: 6434529] |
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[EC 1.5.1.8 created 1972] |
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EC |
1.5.1.9 |
Accepted name: |
saccharopine dehydrogenase (NAD+, L-glutamate-forming) |
Reaction: |
N6-(L-1,3-dicarboxypropyl)-L-lysine + NAD+ + H2O = L-glutamate + (S)-2-amino-6-oxohexanoate + NADH + H+ |
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Glossary: |
saccharopine = N6-(L-1,3-dicarboxypropyl)-L-lysine
(S)-2-amino-6-oxohexanoate = L-2-aminoadipate 6-semialdehyde = L-allysine |
Other name(s): |
dehydrogenase, saccharopine (nicotinamide adenine dinucleotide, glutamate-forming); saccharopin dehydrogenase; NAD+ oxidoreductase (L-2-aminoadipic-δ-semialdehyde and glutamate forming); aminoadipic semialdehyde synthase; 6-N-(L-1,3-dicarboxypropyl)-L-lysine:NAD+ oxidoreductase (L-glutamate-forming) |
Systematic name: |
N6-(L-1,3-dicarboxypropyl)-L-lysine:NAD+ oxidoreductase (L-glutamate-forming) |
Comments: |
The activities of this enzyme along with EC 1.5.1.8, saccharopine dehydrogenase (NADP+, L-lysine-forming), occur on a single protein. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 37256-26-1 |
References: |
1. |
Hutzler, J. and Dancis, J. Conversion of lysine to saccharopine by human tissues. Biochim. Biophys. Acta 158 (1968) 62–69. [DOI] [PMID: 4385118] |
2. |
Markovitz, P.J., Chuang, D.T. and Cox, R.P. Familial hyperlysinemias. Purification and characterization of the bifunctional aminoadipic semialdehyde synthase with lysine-ketoglutarate reductase and saccharopine dehydrogenase activities. J. Biol. Chem. 259 (1984) 11643–11646. [PMID: 6434529] |
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[EC 1.5.1.9 created 1972, modified 2011] |
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EC |
1.5.1.10 |
Accepted name: |
saccharopine dehydrogenase (NADP+, L-glutamate-forming) |
Reaction: |
N6-(L-1,3-dicarboxypropyl)-L-lysine + NADP+ + H2O = L-glutamate + (S)-2-amino-6-oxohexanoate + NADPH + H+ |
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Glossary: |
L-saccharopine = N6-(L-1,3-dicarboxypropyl)-L-lysine
(S)-2-amino-6-oxohexanoate = L-2-aminoadipate 6-semialdehyde = L-allysine |
Other name(s): |
saccharopine (nicotinamide adenine dinucleotide phosphate, glutamate-forming) dehydrogenase; aminoadipic semialdehyde-glutamic reductase; aminoadipate semialdehyde-glutamate reductase; aminoadipic semialdehyde-glutamate reductase; ε-N-(L-glutaryl-2)-L-lysine:NAD+(P) oxidoreductase (L-2-aminoadipate-semialdehyde forming); saccharopine reductase; 6-N-(L-1,3-dicarboxypropyl)-L-lysine:NADP+ oxidoreductase (L-glutamate-forming) |
Systematic name: |
N6-(L-1,3-dicarboxypropyl)-L-lysine:NADP+ oxidoreductase (L-glutamate-forming) |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9033-55-0 |
References: |
1. |
Jones, E.E. and Broquist, H.P. Saccharopine, an intermediate of the aminoadipic acid pathway of lysine biosynthesis. 3. Aminoadipic semialdehyde-glutamate reductase. J. Biol. Chem. 241 (1966) 3430–3434. [PMID: 4380448] |
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[EC 1.5.1.10 created 1972, modified 2011] |
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EC |
1.5.3.18 |
Accepted name: |
L-saccharopine oxidase |
Reaction: |
N6-(L-1,3-dicarboxypropyl)-L-lysine + H2O + O2 = (S)-2-amino-6-oxohexanoate + L-glutamate + H2O2 |
Glossary: |
L-saccharopine = N6-(L-1,3-dicarboxypropyl)-L-lysine
(S)-2-amino-6-oxohexanoate = L-2-aminoadipate 6-semialdehyde = L-allysine |
Other name(s): |
FAP2 |
Systematic name: |
L-saccharopine:oxygen oxidoreductase (L-glutamate-forming) |
Comments: |
The enzyme is involved in pipecolic acid biosynthesis. A flavoprotein (FAD). |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
References: |
1. |
Yoshida, N., Akazawa, S., Katsuragi, T. and Tani, Y. Characterization of two fructosyl-amino acid oxidase homologs of Schizosaccharomyces pombe. J. Biosci. Bioeng. 97 (2004) 278–280. [DOI] [PMID: 16233628] |
2. |
Wickwire, B.M., Wagner, C. and Broquist, H.P. Pipecolic acid biosynthesis in Rhizoctonia leguminicola. II. Saccharopine oxidase: a unique flavin enzyme involved in pipecolic acid biosynthesis. J. Biol. Chem. 265 (1990) 14748–14753. [PMID: 2394693] |
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[EC 1.5.3.18 created 2011] |
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