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

Reaction

N6-(L-1,3-dicarboxypropyl)-L-lysine
+
NAD+
+
H2O
=
L-glutamate
+
(S)-2-amino-6-oxohexanoate
+
NADH
+
H+

Synonyms

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

     1 Oxidoreductases
         1.5 Acting on the CH-NH group of donors
             1.5.1 With NAD+ or NADP+ as acceptor
                1.5.1.9 saccharopine dehydrogenase (NAD+, L-glutamate-forming)

Reference

Reference on EC 1.5.1.9 - saccharopine dehydrogenase (NAD+, L-glutamate-forming)

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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Hutzler, J.; Dancis, J.
Lysine-ketoglutarate reductase in human tissues
Biochim. Biophys. Acta
377
42-51
1975
Homo sapiens
Manually annotated by BRENDA team
Fellows, F.C.I.; Lewis, M.H.R.
Lysine metabolism in mammals
Biochem. J.
136
329-334
1973
Bos taurus, Canis lupus familiaris, Felis catus, Homo sapiens, Ovis aries, Rattus norvegicus, Sus scrofa
Manually annotated by BRENDA team
Markovitz, P.J.; Chuang, D.T.; 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
11643-11646
1984
Bos taurus, Papio hamadryas
Manually annotated by BRENDA team
Markovitz, P.J.; Chuang, D.T.
The bifunctional aminoadipic semialdehyde synthase in lysine degradation. Separation of reductase and dehydrogenase domains by limited proteolysis and column chromatography
J. Biol. Chem.
262
9353-9358
1987
Bos taurus
Manually annotated by BRENDA team
Blemings, K.P.; Crenshaw, T.D.; Swick, R.W.; Benevenga, N.J.
Lysine-alpha-ketoglutarate reductase and saccharopine dehydrogenase are located only in the mitochondrial matrix in rat liver
J. Nutr.
124
1215-1221
1994
Rattus norvegicus
Manually annotated by BRENDA team
Gaziola, S.A.; Teixeira, C.M.; Lugli, J.; Sodek, L.; Azevedo, R.A.
The enzymology of lysine catabolism in rice seeds. Isolation, characterization, and regulatory properties of a lysine 2-oxoglutarate reductase/saccharopine dehydrogenase bifunctional polypeptide
Eur. J. Biochem.
247
364-371
1997
Oryza sativa
Manually annotated by BRENDA team
Miron, D.; Ben-Yaacov, S.; Karchi, H.; Galili, G.
In vitro dephosphorylation inhibits the activity of soybean lysine-ketoglutarate reductase in a lysine-regulated manner
Plant J.
12
1453-1458
1997
Glycine max
-
Manually annotated by BRENDA team
Fjellstedt, T.A.; Robinson, J.C.
Properties of partially purified saccharopine dehydrogenase from human placenta
Arch. Biochem. Biophys.
171
191-196
1975
Homo sapiens
Manually annotated by BRENDA team
Hutzler, J.; Dancis, J.
Saccharopine cleavage by a dehydrogenase of human liver
Biochim. Biophys. Acta
206
205-214
1970
Homo sapiens
Manually annotated by BRENDA team
Mukhopadhyay, A.; Mungre, S.M.; Desmukh, D.R.
Comparison of lysine and tryptophan catabolizing enzymes in rat and bovine tissues
Experientia
46
874-876
1990
Bos taurus, Rattus norvegicus
Manually annotated by BRENDA team
Goncalves-Butruille, M.; Szajner, P.; Torigoi, E.; Leite, A.; Arruda, P.
Purification and Characterization of the Bifunctional Enzyme Lysine-Ketoglutarate Reductase-Saccharopine Dehydrogenase from Maize
Plant Physiol.
110
765-771
1996
Zea mays
Manually annotated by BRENDA team
Zhu, X.; Tang, G.; Galili, G.
Characterization of the two saccharopine dehydrogenase isozymes of lysine catabolism encoded by the single composite AtLKR/SDH locus of Arabidopsis
Plant Physiol.
124
1363-1371
2000
Arabidopsis thaliana
Manually annotated by BRENDA team
Cunha Lima, S.T.; Azevedo, R.A.; Santoro, L.G.; Gaziola, S.A.; Lea, P.J.
Isolation of the bifunctional enzyme lysine 2-oxoglutarate reductase-saccharopine dehydrogenase from Phaseolus vulgaris
Amino Acids
24
179-186
2003
Phaseolus vulgaris
Manually annotated by BRENDA team
Fornazier, R.F.; Gaziola, S.A.; Helm, C.V.; Lea, P.J.; Azevedo, R.A.
Isolation and characterization of enzymes involved in lysine catabolism from sorghum seeds
J. Agric. Food Chem.
53
1791-1798
2005
Sorghum bicolor, Sorghum bicolor Moench
Manually annotated by BRENDA team
Stepansky, A.; Galili, G.
Synthesis of the Arabidopsis bifunctional lysine-ketoglutarate reductase/saccharopine dehydrogenase enzyme of lysine catabolism is concertedly regulated by metabolic and stress-associated signals
Plant Physiol.
133
1407-1415
2003
Arabidopsis sp.
Manually annotated by BRENDA team
Schildhauer, J.; Wiedemuth, K.; Humbeck, K.
Supply of nitrogen can reverse senescence processes and affect expression of genes coding for plastidic glutamine synthetase and lysine-ketoglutarate reductase/saccharopine dehydrogenase
Plant Biol.
10 Suppl 1
76-84
2008
Arabidopsis thaliana, Hordeum vulgare
Manually annotated by BRENDA team
Battur, B.; Boldbaatar, D.; Umemiya-Shirafuji, R.; Liao, M.; Battsetseg, B.; Taylor, D.; Baymbaa, B.; Fujisaki, K.
LKR/SDH plays important roles throughout the tick life cycle including a long starvation period
PLoS ONE
4
e7136
2009
Haemaphysalis longicornis
Manually annotated by BRENDA team
Leon-Ramirez, C.G.; Valdes-Santiago, L.; Campos-Gongora, E.; Ortiz-Castellanos, L.; Arechiga-Carvajal, E.T.; Ruiz-Herrera, J.
A molecular probe for Basidiomycota: the spermidine synthase-saccharopine dehydrogenase chimeric gene
FEMS Microbiol. Lett.
312
77-83
2010
Ustilago maydis (C0MP55)
Manually annotated by BRENDA team
Anderson, O.D.; Coleman-Derr, D.; Gu, Y.Q.; Heath, S.
Structural and transcriptional analysis of plant genes encoding the bifunctional lysine ketoglutarate reductase saccharopine dehydrogenase enzyme
BMC Plant Biol.
10
113
2010
Triticum turgidum (D8WKY4)
Manually annotated by BRENDA team
Serrano, G.C.; Rezende e Silva Figueira, T.; Kiyota, E.; Zanata, N.; Arruda, P.
Lysine degradation through the saccharopine pathway in bacteria: LKR and SDH in bacteria and its relationship to the plant and animal enzymes
FEBS Lett.
586
905-911
2012
Nostoc punctiforme, Nostoc punctiforme ATCC 29133, Ruegeria pomeroyi
Manually annotated by BRENDA team
Schmidt, D.; Rizzi, V.; Gaziola, S.A.; Medici, L.O.; Vincze, E.; Kozak, M.; Lea, P.J.; Azevedo, R.A.
Lysine metabolism in antisense C-hordein barley grains
Plant Physiol. Biochem.
87
73-83
2015
Hordeum vulgare
Manually annotated by BRENDA team
Wan, P.; Yuan, S.; Tang, Y.; Li, K.; Yang, L.; Fu, Q.; Li, G.
Pathways of amino acid degradation in Nilaparvata lugens (Stal) with special reference to lysine-ketoglutarate reductase/saccharopine dehydrogenase (LKR/SDH)
PLoS ONE
10
e0127789
2015
Nilaparvata lugens (A0A089MUZ6)
Manually annotated by BRENDA team