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Information on EC 1.5.1.9 - saccharopine dehydrogenase (NAD+, L-glutamate-forming)
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EC Tree
1.5.1.9 saccharopine dehydrogenase (NAD+, L-glutamate-forming)IUBMB Comments
The activities of this enzyme along with EC 1.5.1.8, saccharopine dehydrogenase (NADP+, L-lysine-forming), occur on a single protein.
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Word Map
- 1.5.1.9
-
1.5.1.8
-
lysine-ketoglutarate
- maize
- hyperlysinemias
- pipecolate
- alpha-ketoglutarate
- ornithine
- spermidine
- polyamine
- analysis
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
Reaction Schemes
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, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
aminoadipic semialdehyde synthase
-
-
-
-
AtLKR/SDHp
-
bifunctional enzyme, lysine-ketoglutarate reductase (EC 1. 5.1.8) and saccharopine dehydrogenase activity (EC 1.5.1.9) occur on a single protein
dehydrogenase, saccharopine (nicotinamide adenine dinucleotide, glutamate-forming)
-
-
-
-
LKR/SDH
lysine 2-oxoglutarate reductase-saccharopine dehydrogenase
-
bifunctional enzyme
lysine-ketoglutarate reductase/saccharopine dehydrogenase
NAD+ oxidoreductase (L-2-aminoadipic-delta-semialdehyde and glutamate forming)
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-
-
-
saccharopin dehydrogenase
-
-
-
-
saccharopine dehydrogenase
SDH
LKR/SDH
bifunctional enzyme with lysine ketoglutarate reductase and saccharopine dehydrogenase activities
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
N6-(L-1,3-dicarboxypropyl)-L-lysine + NAD+ + H2O = L-glutamate + (S)-2-amino-6-oxohexanoate + NADH + H+
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-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
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-
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redox reaction
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-
-
-
reduction
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
BRENDA
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SYSTEMATIC NAME
IUBMB Comments
N6-(L-1,3-dicarboxypropyl)-L-lysine:NAD+ oxidoreductase (L-glutamate-forming)
The activities of this enzyme along with EC 1.5.1.8, saccharopine dehydrogenase (NADP+, L-lysine-forming), occur on a single protein.
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CAS REGISTRY NUMBER
COMMENTARY
37256-26-1
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
N6-(L-1,3-dicarboxypropyl)-L-lysine + NAD+ + H2O
L-Glu + 2-aminoadipate 6-semialdehyde + NADH
N6-(L-1,3-dicarboxypropyl)-L-lysine + NAD+ + H2O
L-glutamate + (S)-2-amino-6-oxohexanoate + NADH + H+
N6-(L-1,3-dicarboxypropyl)-L-lysine + NAD+ + H2O
L-glutamate + 2-aminoadipate 6-semialdehyde + NADH + H+
additional information
?
-
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)
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-
?
N6-(L-1,3-dicarboxypropyl)-L-lysine + NAD+ + H2O
L-Glu + 2-aminoadipate 6-semialdehyde + NADH
-
-
-
-
?
N6-(L-1,3-dicarboxypropyl)-L-lysine + NAD+ + H2O
L-Glu + 2-aminoadipate 6-semialdehyde + NADH
-
the bifunctional reductase/saccharopine dehydrogenase contains the first two enzyme of lysine catabolism, is concertedly regulated by metabolic and stress-associated signals. The level of the bifunctional enzyme is strongly enhanced by abscisic acid, jasmonate, and sugar starvation, whereas excess sugars and nitrogen starvation reduce its level
-
-
?
N6-(L-1,3-dicarboxypropyl)-L-lysine + NAD+ + H2O
L-glutamate + (S)-2-amino-6-oxohexanoate + NADH + H+
-
-
-
-
?
N6-(L-1,3-dicarboxypropyl)-L-lysine + NAD+ + H2O
L-glutamate + (S)-2-amino-6-oxohexanoate + NADH + H+
-
-
-
?
N6-(L-1,3-dicarboxypropyl)-L-lysine + NAD+ + H2O
L-glutamate + (S)-2-amino-6-oxohexanoate + NADH + H+
-
-
-
?
N6-(L-1,3-dicarboxypropyl)-L-lysine + NAD+ + H2O
L-glutamate + 2-aminoadipate 6-semialdehyde + NADH + H+
-
-
-
-
?
N6-(L-1,3-dicarboxypropyl)-L-lysine + NAD+ + H2O
L-glutamate + 2-aminoadipate 6-semialdehyde + NADH + H+
-
-
-
-
r
N6-(L-1,3-dicarboxypropyl)-L-lysine + NAD+ + H2O
L-glutamate + 2-aminoadipate 6-semialdehyde + NADH + H+
-
involved in lysine catabolism
-
-
r
N6-(L-1,3-dicarboxypropyl)-L-lysine + NAD+ + H2O
L-glutamate + 2-aminoadipate 6-semialdehyde + NADH + H+
-
-
-
-
r
N6-(L-1,3-dicarboxypropyl)-L-lysine + NAD+ + H2O
L-glutamate + 2-aminoadipate 6-semialdehyde + NADH + H+
-
involved in lysine catabolism
-
-
?
N6-(L-1,3-dicarboxypropyl)-L-lysine + NAD+ + H2O
L-glutamate + 2-aminoadipate 6-semialdehyde + NADH + H+
-
involved in lysine catabolism
-
-
r
N6-(L-1,3-dicarboxypropyl)-L-lysine + NAD+ + H2O
L-glutamate + 2-aminoadipate 6-semialdehyde + NADH + H+
-
-
-
-
r
N6-(L-1,3-dicarboxypropyl)-L-lysine + NAD+ + H2O
L-glutamate + 2-aminoadipate 6-semialdehyde + NADH + H+
-
involved in lysine catabolism
-
-
r
N6-(L-1,3-dicarboxypropyl)-L-lysine + NAD+ + H2O
L-glutamate + 2-aminoadipate 6-semialdehyde + NADH + H+
-
-
-
-
r
N6-(L-1,3-dicarboxypropyl)-L-lysine + NAD+ + H2O
L-glutamate + 2-aminoadipate 6-semialdehyde + NADH + H+
-
involved in lysine catabolism
-
-
r
N6-(L-1,3-dicarboxypropyl)-L-lysine + NAD+ + H2O
L-glutamate + 2-aminoadipate 6-semialdehyde + NADH + H+
-
-
-
-
r
N6-(L-1,3-dicarboxypropyl)-L-lysine + NAD+ + H2O
L-glutamate + 2-aminoadipate 6-semialdehyde + NADH + H+
-
involved in lysine catabolism
-
-
r
N6-(L-1,3-dicarboxypropyl)-L-lysine + NAD+ + H2O
L-glutamate + 2-aminoadipate 6-semialdehyde + NADH + H+
-
-
-
-
?
N6-(L-1,3-dicarboxypropyl)-L-lysine + NAD+ + H2O
L-glutamate + 2-aminoadipate 6-semialdehyde + NADH + H+
-
-
-
-
r
N6-(L-1,3-dicarboxypropyl)-L-lysine + NAD+ + H2O
L-glutamate + 2-aminoadipate 6-semialdehyde + NADH + H+
-
N6-(L-1,3-dicarboxypropyl)-L-lysine is identical with saccharopine, high specificity
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-
r
N6-(L-1,3-dicarboxypropyl)-L-lysine + NAD+ + H2O
L-glutamate + 2-aminoadipate 6-semialdehyde + NADH + H+
-
involved in lysine catabolism
-
-
r
N6-(L-1,3-dicarboxypropyl)-L-lysine + NAD+ + H2O
L-glutamate + 2-aminoadipate 6-semialdehyde + NADH + H+
-
-
-
-
?
N6-(L-1,3-dicarboxypropyl)-L-lysine + NAD+ + H2O
L-glutamate + 2-aminoadipate 6-semialdehyde + NADH + H+
-
-
-
-
r
N6-(L-1,3-dicarboxypropyl)-L-lysine + NAD+ + H2O
L-glutamate + 2-aminoadipate 6-semialdehyde + NADH + H+
-
involved in lysine catabolism
-
-
r
N6-(L-1,3-dicarboxypropyl)-L-lysine + NAD+ + H2O
L-glutamate + 2-aminoadipate 6-semialdehyde + NADH + H+
-
-
-
-
r
N6-(L-1,3-dicarboxypropyl)-L-lysine + NAD+ + H2O
L-glutamate + 2-aminoadipate 6-semialdehyde + NADH + H+
-
-
-
-
r
N6-(L-1,3-dicarboxypropyl)-L-lysine + NAD+ + H2O
L-glutamate + 2-aminoadipate 6-semialdehyde + NADH + H+
-
involved in lysine catabolism
-
-
r
N6-(L-1,3-dicarboxypropyl)-L-lysine + NAD+ + H2O
L-glutamate + 2-aminoadipate 6-semialdehyde + NADH + H+
-
-
-
-
r
N6-(L-1,3-dicarboxypropyl)-L-lysine + NAD+ + H2O
L-glutamate + 2-aminoadipate 6-semialdehyde + NADH + H+
-
involved in lysine catabolism
-
-
r
N6-(L-1,3-dicarboxypropyl)-L-lysine + NAD+ + H2O
L-glutamate + 2-aminoadipate 6-semialdehyde + NADH + H+
-
-
-
-
?
N6-(L-1,3-dicarboxypropyl)-L-lysine + NAD+ + H2O
L-glutamate + 2-aminoadipate 6-semialdehyde + NADH + H+
-
-
-
-
r
N6-(L-1,3-dicarboxypropyl)-L-lysine + NAD+ + H2O
L-glutamate + 2-aminoadipate 6-semialdehyde + NADH + H+
-
involved in lysine catabolism
-
-
?
N6-(L-1,3-dicarboxypropyl)-L-lysine + NAD+ + H2O
L-glutamate + 2-aminoadipate 6-semialdehyde + NADH + H+
-
involved in lysine catabolism
-
-
r
N6-(L-1,3-dicarboxypropyl)-L-lysine + NAD+ + H2O
L-glutamate + 2-aminoadipate 6-semialdehyde + NADH + H+
-
-
-
-
r
N6-(L-1,3-dicarboxypropyl)-L-lysine + NAD+ + H2O
L-glutamate + 2-aminoadipate 6-semialdehyde + NADH + H+
-
involved in lysine catabolism
-
-
r
N6-(L-1,3-dicarboxypropyl)-L-lysine + NAD+ + H2O
L-glutamate + 2-aminoadipate 6-semialdehyde + NADH + H+
-
-
-
-
?
N6-(L-1,3-dicarboxypropyl)-L-lysine + NAD+ + H2O
L-glutamate + 2-aminoadipate 6-semialdehyde + NADH + H+
-
-
-
-
?
N6-(L-1,3-dicarboxypropyl)-L-lysine + NAD+ + H2O
L-glutamate + 2-aminoadipate 6-semialdehyde + NADH + H+
-
-
-
-
r
N6-(L-1,3-dicarboxypropyl)-L-lysine + NAD+ + H2O
L-glutamate + 2-aminoadipate 6-semialdehyde + NADH + H+
-
involved in lysine catabolism
-
-
r
N6-(L-1,3-dicarboxypropyl)-L-lysine + NAD+ + H2O
L-glutamate + 2-aminoadipate 6-semialdehyde + NADH + H+
-
-
-
-
r
N6-(L-1,3-dicarboxypropyl)-L-lysine + NAD+ + H2O
L-glutamate + 2-aminoadipate 6-semialdehyde + NADH + H+
-
involved in lysine catabolism
-
-
r
saccharopine + NAD+ + H2O
L-glutamate + alpha-aminoadipate semialdehyde + NADH + H+
-
-
-
-
r
saccharopine + NAD+ + H2O
L-glutamate + alpha-aminoadipate semialdehyde + NADH + H+
-
-
-
-
r
saccharopine + NAD+ + H2O
L-glutamate + alpha-aminoadipate semialdehyde + NADH + H+
-
-
-
-
r
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
N6-(L-1,3-dicarboxypropyl)-L-lysine + NAD+ + H2O
L-Glu + 2-aminoadipate 6-semialdehyde + NADH
-
the bifunctional reductase/saccharopine dehydrogenase contains the first two enzyme of lysine catabolism, is concertedly regulated by metabolic and stress-associated signals. The level of the bifunctional enzyme is strongly enhanced by abscisic acid, jasmonate, and sugar starvation, whereas excess sugars and nitrogen starvation reduce its level
-
-
?
N6-(L-1,3-dicarboxypropyl)-L-lysine + NAD+ + H2O
L-glutamate + (S)-2-amino-6-oxohexanoate + NADH + H+
N6-(L-1,3-dicarboxypropyl)-L-lysine + NAD+ + H2O
L-glutamate + 2-aminoadipate 6-semialdehyde + NADH + H+
N6-(L-1,3-dicarboxypropyl)-L-lysine + NAD+ + H2O
L-glutamate + (S)-2-amino-6-oxohexanoate + NADH + H+
-
-
-
-
?
N6-(L-1,3-dicarboxypropyl)-L-lysine + NAD+ + H2O
L-glutamate + (S)-2-amino-6-oxohexanoate + NADH + H+
-
-
-
?
N6-(L-1,3-dicarboxypropyl)-L-lysine + NAD+ + H2O
L-glutamate + (S)-2-amino-6-oxohexanoate + NADH + H+
-
-
-
?
N6-(L-1,3-dicarboxypropyl)-L-lysine + NAD+ + H2O
L-glutamate + 2-aminoadipate 6-semialdehyde + NADH + H+
-
involved in lysine catabolism
-
-
r
N6-(L-1,3-dicarboxypropyl)-L-lysine + NAD+ + H2O
L-glutamate + 2-aminoadipate 6-semialdehyde + NADH + H+
-
involved in lysine catabolism
-
-
?
N6-(L-1,3-dicarboxypropyl)-L-lysine + NAD+ + H2O
L-glutamate + 2-aminoadipate 6-semialdehyde + NADH + H+
-
involved in lysine catabolism
-
-
r
N6-(L-1,3-dicarboxypropyl)-L-lysine + NAD+ + H2O
L-glutamate + 2-aminoadipate 6-semialdehyde + NADH + H+
-
involved in lysine catabolism
-
-
r
N6-(L-1,3-dicarboxypropyl)-L-lysine + NAD+ + H2O
L-glutamate + 2-aminoadipate 6-semialdehyde + NADH + H+
-
involved in lysine catabolism
-
-
r
N6-(L-1,3-dicarboxypropyl)-L-lysine + NAD+ + H2O
L-glutamate + 2-aminoadipate 6-semialdehyde + NADH + H+
-
involved in lysine catabolism
-
-
r
N6-(L-1,3-dicarboxypropyl)-L-lysine + NAD+ + H2O
L-glutamate + 2-aminoadipate 6-semialdehyde + NADH + H+
-
involved in lysine catabolism
-
-
r
N6-(L-1,3-dicarboxypropyl)-L-lysine + NAD+ + H2O
L-glutamate + 2-aminoadipate 6-semialdehyde + NADH + H+
-
involved in lysine catabolism
-
-
r
N6-(L-1,3-dicarboxypropyl)-L-lysine + NAD+ + H2O
L-glutamate + 2-aminoadipate 6-semialdehyde + NADH + H+
-
involved in lysine catabolism
-
-
r
N6-(L-1,3-dicarboxypropyl)-L-lysine + NAD+ + H2O
L-glutamate + 2-aminoadipate 6-semialdehyde + NADH + H+
-
involved in lysine catabolism
-
-
r
N6-(L-1,3-dicarboxypropyl)-L-lysine + NAD+ + H2O
L-glutamate + 2-aminoadipate 6-semialdehyde + NADH + H+
-
involved in lysine catabolism
-
-
?
N6-(L-1,3-dicarboxypropyl)-L-lysine + NAD+ + H2O
L-glutamate + 2-aminoadipate 6-semialdehyde + NADH + H+
-
involved in lysine catabolism
-
-
r
N6-(L-1,3-dicarboxypropyl)-L-lysine + NAD+ + H2O
L-glutamate + 2-aminoadipate 6-semialdehyde + NADH + H+
-
involved in lysine catabolism
-
-
r
N6-(L-1,3-dicarboxypropyl)-L-lysine + NAD+ + H2O
L-glutamate + 2-aminoadipate 6-semialdehyde + NADH + H+
-
involved in lysine catabolism
-
-
r
N6-(L-1,3-dicarboxypropyl)-L-lysine + NAD+ + H2O
L-glutamate + 2-aminoadipate 6-semialdehyde + NADH + H+
-
involved in lysine catabolism
-
-
r
saccharopine + NAD+ + H2O
L-glutamate + alpha-aminoadipate semialdehyde + NADH + H+
-
-
-
-
r
saccharopine + NAD+ + H2O
L-glutamate + alpha-aminoadipate semialdehyde + NADH + H+
-
-
-
-
r
saccharopine + NAD+ + H2O
L-glutamate + alpha-aminoadipate semialdehyde + NADH + H+
-
-
-
-
r
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
C-hordein suppression alters the enzyme activity differentially in different developmental stages, the extent varies among the transgenic lines., overview
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
C-hordein suppression alters the enzyme activity differentially in different developmental stages, the extent varies among the transgenic lines., overview
-
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Hyperlysinemias
Familial hyperlysinemias. Purification and characterization of the bifunctional aminoadipic semialdehyde synthase with lysine-ketoglutarate reductase and saccharopine dehydrogenase activities.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.374
NAD+
-
pH 7, bifunctional enzyme, lysine-ketoglutarate reductase (EC 1. 5.1.8) and saccharopine dehydrogenase activity (EC 1.5.1.9) occur on a single protein
0.698
NAD+
-
pH 9, bifunctional enzyme, lysine-ketoglutarate reductase (EC 1. 5.1.8) and saccharopine dehydrogenase activity (EC 1.5.1.9) occur on a single protein
0.035
saccharopine
-
pH 9, bifunctional enzyme, lysine-ketoglutarate reductase (EC 1. 5.1.8) and saccharopine dehydrogenase activity (EC 1.5.1.9) occur on a single protein
0.063
saccharopine
-
pH 7, bifunctional enzyme, lysine-ketoglutarate reductase (EC 1. 5.1.8) and saccharopine dehydrogenase activity (EC 1.5.1.9) occur on a single protein
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
8.5
9.5
9.5
-
bifunctional enzyme, lysine-ketoglutarate reductase (EC 1. 5.1.8) and saccharopine dehydrogenase activity (EC 1.5.1.9) occur on a single protein
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
baboon, 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
-
-
brenda
bifunctional spermidine synthase, and saccharopine dehydrogenase
UniProt
brenda
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
-
-
brenda
bifunctional lysine-ketoglutarate reductase/saccharopine dehydrogenase, EC 1.5.8 and EC 1.5.9
-
-
brenda
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
-
-
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
the SDH mRNA transcripts are more abundant in unfed and starved ticks than in fed and engorged ticks
brenda
additional information
-
grain, spikes, at different developmental stages: early milk, late milk, and soft dough. The enzyme exhibits the highest activity at the late milk stage
brenda
additional information
-
expression in all developmental stages, including a long period of starvation after detachment from the host. The mRNA transcripts are more abundant in unfed and starved ticks than in fed and engorged ticks
brenda
additional information
-
no activity in: human heart, muscle, skin, brain, spleen, pancreas, adrenal, lung, gut, leukocytes and erythrocytes
brenda
additional information
Nilaparvata lugens are maintained on rice variety Taichung Native 1 (TN1) for more than 170 generations under controlled conditions. Temporal transcript profile of Nllkr/sdh in nymphs and adults, quantitative real-time PCR expression analysis. Nllkr/sdh is widely expressed in the eggs, first- through fifth-instar nymphs, and adults. The expression levels varies little among different development stages
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
metabolism
physiological function
-
gene silencing by RNAi indicates that the tick LKR/SDH plays an integral role in the osmotic regulation of water balance and development of eggs in ovary of engorged females
metabolism
the enzyme is involved in L-lysine breakdown. In Nilaparvata lugens, the degradation of L-lysine is independent from the yeast-like endosymbionts of the organism, in contrast to degradation of other amino acids, overview
Show AA Sequence and Transmembrane Helices (1683 entries)
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
115000
120000
-
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
125000
-
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
190000
-
bifunctional enzyme lysine 2-oxoglutarate reductase-saccharopine dehydrogenase, gel filtration
202000
-
native non-denaturing gel, lysine-ketoglutarate reductase (EC 1. 5.1.8) and saccharopine dehydrogenase activity (EC 1.5.1.9) occur on a single protein
203000
-
gel filtration with Sephacryl S-200, lysine-ketoglutarate reductase (EC 1. 5.1.8) and saccharopine dehydrogenase activity (EC 1.5.1.9) occur on a single protein
260000
-
gel filtration with Superdex, lysine-ketoglutarate reductase (EC 1. 5.1.8) and saccharopine dehydrogenase activity (EC 1.5.1.9) occur on a single protein
44000
44100
467000
-
gel filtration, 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
468000
-
gel filtration, 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
115000
-
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
115000
-
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
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
?
-
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
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
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
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5 - 10
-
inactive under acidic (pH 5) or alkaline (pH 10) conditions
700907
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
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OXIDATION STABILITY
ORGANISM
UNIPROT
LITERATURE
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, crude enzyme stable for several months, purified enzyme inactivated within 3 weeks
-
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
lysine-ketoglutarate reductase (EC 1. 5.1.8) and saccharopine dehydrogenase activity (EC 1.5.1.9) occur on a single protein
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
native enzyme partially through ammonium sulfate fractionation and desalting gel filtration
-
Q-Sepharose column chromatography, Ni-NTA agarose column chromatography, and Superdex 200 gel filtration
lysine-ketoglutarate reductase (EC 1. 5.1.8) and saccharopine dehydrogenase activity (EC 1.5.1.9) occur on a single protein
-
lysine-ketoglutarate reductase (EC 1. 5.1.8) and saccharopine dehydrogenase activity (EC 1.5.1.9) occur on a single protein
-
lysine-ketoglutarate reductase (EC 1. 5.1.8) and saccharopine dehydrogenase activity (EC 1.5.1.9) occur on a single protein
-
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
-
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
-
Q-Sepharose column chromatography, Ni-NTA agarose column chromatography, and Superdex 200 gel filtration
-
Q-Sepharose column chromatography, Ni-NTA agarose column chromatography, and Superdex 200 gel filtration
-
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21(DE3) cells
gene nllkr/sdh, DNA and amino acid sequence determination and analysis, phylogenic analysis, quantitative real-time PCR expression analysis
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
C-hordein suppression alters the enzyme activity differentially in different developmental stages, the extent varies among the transgenic lines, overview
-
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
analysis
the Spe-Sdh gene is specific to Basidiomycota, use of a specific fragment of the Spe-Sdh gene as a tool to unequivocally identify Basidiomycota isolates
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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
brenda
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, Ovis aries, Homo sapiens, Rattus norvegicus, Sus scrofa
brenda
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
brenda
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
brenda
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
brenda
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
brenda
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
-
brenda
Fjellstedt, T.A.; Robinson, J.C.
Properties of partially purified saccharopine dehydrogenase from human placenta
Arch. Biochem. Biophys.
171
191-196
1975
Homo sapiens
brenda
Hutzler, J.; Dancis, J.
Saccharopine cleavage by a dehydrogenase of human liver
Biochim. Biophys. Acta
206
205-214
1970
Homo sapiens
brenda
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
brenda
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
brenda
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
brenda
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
brenda
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
brenda
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.
brenda
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
brenda
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
brenda
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)
brenda
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)
brenda
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, Ruegeria pomeroyi, Nostoc punctiforme ATCC 29133
brenda
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
brenda
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)
brenda
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