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Information on EC 1.5.1.10 - saccharopine dehydrogenase (NADP+, L-glutamate-forming)
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EC Tree
1.5.1.10 saccharopine dehydrogenase (NADP+, L-glutamate-forming)Specify your search results
Word Map
- 1.5.1.10
- alpha-aminoadipate
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auxotrophs
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magnaporthe
- grisea
- homocitrate
-
pipecolic
- swainsonine
- homoisocitrate
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piperideine-6-carboxylic
- chrysogenum
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unlinked
-
rossmann
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penicillium
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ph-rate
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endophytic
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embedding
-
6-dehydrogenase
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substrate-assisted
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seven-stranded
- diaminopimelate
- oxytropis
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acid-base
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leaky
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all-helical
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anisotropic
- l-pipecolate
- dl-alpha-aminoadipate
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gene-enzyme
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Reaction Schemes
Synonyms
saccharopine reductase, 
more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
aminoadipate semialdehyde-glutamate reductase
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aminoadipic semialdehyde-glutamate reductase
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aminoadipic semialdehyde-glutamic reductase
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dehydrogenase, saccharopine (nicotinamide adenine dinucleotide phosphate, glutamate-forming)
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epsilon-N-(L-glutaryl-2)-L-lysine:NAD+(P) oxidoreductase (L-2-aminoadipate-semialdehyde forming)
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LKR/SDH
lysine-ketoglutarate reductase/saccharopine dehydrogenase
nSpe-Sdh
saccharopine dehydrogenase
saccharopine reductase
SDH
spermidine synthase-saccharopine dehydrogenase
saccharopine reductase
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-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
N6-(L-1,3-dicarboxypropyl)-L-lysine + NADP+ + H2O = L-glutamate + (S)-2-amino-6-oxohexanoate + NADPH + H+
N6-(L-1,3-dicarboxypropyl)-L-lysine + NADP+ + H2O = L-glutamate + (S)-2-amino-6-oxohexanoate + NADPH + H+
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-
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N6-(L-1,3-dicarboxypropyl)-L-lysine + NADP+ + H2O = L-glutamate + (S)-2-amino-6-oxohexanoate + NADPH + H+
ordered kinetic mechanism, the reduced dinucleotide substrate binds to enzyme first followed by L-alpha-aminoadipate-delta-semialdehyde, which adds in rapid equilibrium prior to L-glutamate, saccharopine is released prior to NADP+, primary deuterium kinetic isotope effects and solvent deuterium kinetic isotope effects, overview. A conformational change to open the site and release products (in the direction of saccharopine formation) is the rate limiting step. Two groups are involved in the acid-base chemistry of the reaction. An enzyme group with a pKa of 5.6 accepts a proton from the alpha-amine of glutamate to generate the neutral amine that can act as a nucleophile. The alpha-amine of glutamate attacks the carbonyl of the semialdehyde to generate the carbinolamine, which is protonated by a second enzyme group with a pKa of about 7.8-8.0. Ionizable residues that might play a role in the acid-base mechanism of the enzyme are D126, C154 and/or Y99
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
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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:NADP+ oxidoreductase (L-glutamate-forming)
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CAS REGISTRY NUMBER
COMMENTARY
9033-55-0
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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
2-aminoadipate 6-semialdehyde + L-glutamate + NADPH
N6-(L-1,3-dicarboxypropyl)-L-lysine + NADP+ + H2O
2-aminoadipate 6-semialdehyde + L-glutamate + NADPH + H+
N6-(L-1,3-dicarboxypropyl)-L-lysine + NADP+ + H2O
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-
-
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r
L-glutamate + 2-aminoadipate 6-semialdehyde + NADPH + H+
saccharopine + NADP+ + H2O
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piperidine-6-carboxylic acid and alpha-aminoadipate are precursors for synthesis of alpha-aminoadipate 6-semialdehyde via 3 different pathways, penultimate step in L-lysine biosynthesis
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-
?
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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r
N6-(L-1,3-dicarboxypropyl)-L-lysine + NADP+ + H2O
L-glutamate + (S)-2-amino-6-oxohexanoate + NADPH + H+
N6-(L-1,3-dicarboxypropyl)-L-lysine + NADP+ + H2O
L-glutamate + 2-aminoadipate 6-semialdehyde + NADPH + H+
saccharopine + NADP+ + H2O
L-glutamate + 2-aminoadipate 6-semialdehyde + NADPH + H+
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reverse reaction direction used for activity assay, end product is piperidine-6-carboxylic acid in assays using cell extract
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r
2-aminoadipate 6-semialdehyde + L-glutamate + NADPH
N6-(L-1,3-dicarboxypropyl)-L-lysine + NADP+ + H2O
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lysine biosynthesis
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?
2-aminoadipate 6-semialdehyde + L-glutamate + NADPH
N6-(L-1,3-dicarboxypropyl)-L-lysine + NADP+ + H2O
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lysine biosynthesis
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?
2-aminoadipate 6-semialdehyde + L-glutamate + NADPH
N6-(L-1,3-dicarboxypropyl)-L-lysine + NADP+ + H2O
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?
2-aminoadipate 6-semialdehyde + L-glutamate + NADPH
N6-(L-1,3-dicarboxypropyl)-L-lysine + NADP+ + H2O
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-
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r
2-aminoadipate 6-semialdehyde + L-glutamate + NADPH
N6-(L-1,3-dicarboxypropyl)-L-lysine + NADP+ + H2O
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r
2-aminoadipate 6-semialdehyde + L-glutamate + NADPH
N6-(L-1,3-dicarboxypropyl)-L-lysine + NADP+ + H2O
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N6-(L-1,3-dicarboxypropyl)-L-lysine is identical with saccharopine
r
2-aminoadipate 6-semialdehyde + L-glutamate + NADPH
N6-(L-1,3-dicarboxypropyl)-L-lysine + NADP+ + H2O
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N6-(L-1,3-dicarboxypropyl)-L-lysine is identical with saccharopine
r
2-aminoadipate 6-semialdehyde + L-glutamate + NADPH
N6-(L-1,3-dicarboxypropyl)-L-lysine + NADP+ + H2O
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N6-(L-1,3-dicarboxypropyl)-L-lysine is identical with saccharopine
r
2-aminoadipate 6-semialdehyde + L-glutamate + NADPH
N6-(L-1,3-dicarboxypropyl)-L-lysine + NADP+ + H2O
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lysine biosynthesis
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?
2-aminoadipate 6-semialdehyde + L-glutamate + NADPH
N6-(L-1,3-dicarboxypropyl)-L-lysine + NADP+ + H2O
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lysine biosynthesis
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?
2-aminoadipate 6-semialdehyde + L-glutamate + NADPH
N6-(L-1,3-dicarboxypropyl)-L-lysine + NADP+ + H2O
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lysine biosynthesis
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?
N6-(L-1,3-dicarboxypropyl)-L-lysine + NADP+ + H2O
L-glutamate + (S)-2-amino-6-oxohexanoate + NADPH + H+
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-
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r
N6-(L-1,3-dicarboxypropyl)-L-lysine + NADP+ + H2O
L-glutamate + (S)-2-amino-6-oxohexanoate + NADPH + H+
Agaricus bisporus Sylvan A15
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-
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r
N6-(L-1,3-dicarboxypropyl)-L-lysine + NADP+ + H2O
L-glutamate + (S)-2-amino-6-oxohexanoate + NADPH + H+
reaction of the SDH domain
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r
N6-(L-1,3-dicarboxypropyl)-L-lysine + NADP+ + H2O
L-glutamate + (S)-2-amino-6-oxohexanoate + NADPH + H+
reaction of the SDH domain
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r
N6-(L-1,3-dicarboxypropyl)-L-lysine + NADP+ + H2O
L-glutamate + (S)-2-amino-6-oxohexanoate + NADPH + H+
reaction of the SDH domain
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-
r
N6-(L-1,3-dicarboxypropyl)-L-lysine + NADP+ + H2O
L-glutamate + (S)-2-amino-6-oxohexanoate + NADPH + H+
reaction of the SDH domain
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r
N6-(L-1,3-dicarboxypropyl)-L-lysine + NADP+ + H2O
L-glutamate + (S)-2-amino-6-oxohexanoate + NADPH + H+
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?
N6-(L-1,3-dicarboxypropyl)-L-lysine + NADP+ + H2O
L-glutamate + (S)-2-amino-6-oxohexanoate + NADPH + H+
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r
N6-(L-1,3-dicarboxypropyl)-L-lysine + NADP+ + H2O
L-glutamate + (S)-2-amino-6-oxohexanoate + NADPH + H+
A0A3L6FCN0
reaction of the SDH domain
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r
N6-(L-1,3-dicarboxypropyl)-L-lysine + NADP+ + H2O
L-glutamate + 2-aminoadipate 6-semialdehyde + NADPH + H+
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?
N6-(L-1,3-dicarboxypropyl)-L-lysine + NADP+ + H2O
L-glutamate + 2-aminoadipate 6-semialdehyde + NADPH + H+
enzyme catalyzes the penultimate step in lysine biosynthesis
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-
?
N6-(L-1,3-dicarboxypropyl)-L-lysine + NADP+ + H2O
L-glutamate + 2-aminoadipate 6-semialdehyde + NADPH + H+
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?
additional information
?
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the bifunctional enzyme lysine-ketoglutarate reductase/saccharopine dehydrogenase (LKR/SDH) comprises a LKR domain, which condenses lysine and 2-oxoglutarate into saccharopine, and the SDH domain, that hydrolyzes saccharopine to form glutamate and alpha-aminoadipate semialdehyde, the latter of which is oxidized to alpha-aminoadipate by aminoadipate semialdehyde dehydrogenase (AASADH)
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additional information
?
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the bifunctional enzyme lysine-ketoglutarate reductase/saccharopine dehydrogenase (LKR/SDH) comprises a LKR domain, which condenses lysine and 2-oxoglutarate into saccharopine, and the SDH domain, that hydrolyzes saccharopine to form glutamate and alpha-aminoadipate semialdehyde, the latter of which is oxidized to alpha-aminoadipate by aminoadipate semialdehyde dehydrogenase (AASADH)
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additional information
?
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the bifunctional enzyme lysine-ketoglutarate reductase/saccharopine dehydrogenase (LKR/SDH) comprises a LKR domain, which condenses lysine and 2-oxoglutarate into saccharopine, and the SDH domain, that hydrolyzes saccharopine to form glutamate and alpha-aminoadipate semialdehyde, the latter of which is oxidized to alpha-aminoadipate by aminoadipate semialdehyde dehydrogenase (AASADH)
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additional information
?
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the bifunctional enzyme lysine-ketoglutarate reductase/saccharopine dehydrogenase (LKR/SDH) comprises a LKR domain, which condenses lysine and 2-oxoglutarate into saccharopine, and the SDH domain, that hydrolyzes saccharopine to form glutamate and alpha-aminoadipate semialdehyde, the latter of which is oxidized to alpha-aminoadipate by aminoadipate semialdehyde dehydrogenase (AASADH)
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additional information
?
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A0A3L6FCN0
the bifunctional enzyme lysine-ketoglutarate reductase/saccharopine dehydrogenase (LKR/SDH) comprises a LKR domain, which condenses lysine and 2-oxoglutarate into saccharopine, and the SDH domain, that hydrolyzes saccharopine to form glutamate and alpha-aminoadipate semialdehyde, the latter of which is oxidized to alpha-aminoadipate by aminoadipate semialdehyde dehydrogenase (AASADH)
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-
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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
2-aminoadipate 6-semialdehyde + L-glutamate + NADPH
N6-(L-1,3-dicarboxypropyl)-L-lysine + NADP+ + H2O
L-glutamate + 2-aminoadipate 6-semialdehyde + NADPH + H+
saccharopine + NADP+ + H2O
-
piperidine-6-carboxylic acid and alpha-aminoadipate are precursors for synthesis of alpha-aminoadipate 6-semialdehyde via 3 different pathways, penultimate step in L-lysine biosynthesis
-
-
?
N6-(L-1,3-dicarboxypropyl)-L-lysine + NADP+ + H2O
L-glutamate + (S)-2-amino-6-oxohexanoate + NADPH + H+
N6-(L-1,3-dicarboxypropyl)-L-lysine + NADP+ + H2O
L-glutamate + 2-aminoadipate 6-semialdehyde + NADPH + H+
enzyme catalyzes the penultimate step in lysine biosynthesis
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-
?
2-aminoadipate 6-semialdehyde + L-glutamate + NADPH
N6-(L-1,3-dicarboxypropyl)-L-lysine + NADP+ + H2O
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lysine biosynthesis
-
?
2-aminoadipate 6-semialdehyde + L-glutamate + NADPH
N6-(L-1,3-dicarboxypropyl)-L-lysine + NADP+ + H2O
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lysine biosynthesis
-
?
2-aminoadipate 6-semialdehyde + L-glutamate + NADPH
N6-(L-1,3-dicarboxypropyl)-L-lysine + NADP+ + H2O
-
lysine biosynthesis
-
?
2-aminoadipate 6-semialdehyde + L-glutamate + NADPH
N6-(L-1,3-dicarboxypropyl)-L-lysine + NADP+ + H2O
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lysine biosynthesis
-
?
2-aminoadipate 6-semialdehyde + L-glutamate + NADPH
N6-(L-1,3-dicarboxypropyl)-L-lysine + NADP+ + H2O
-
lysine biosynthesis
-
?
N6-(L-1,3-dicarboxypropyl)-L-lysine + NADP+ + H2O
L-glutamate + (S)-2-amino-6-oxohexanoate + NADPH + H+
-
-
-
r
N6-(L-1,3-dicarboxypropyl)-L-lysine + NADP+ + H2O
L-glutamate + (S)-2-amino-6-oxohexanoate + NADPH + H+
Agaricus bisporus Sylvan A15
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-
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r
N6-(L-1,3-dicarboxypropyl)-L-lysine + NADP+ + H2O
L-glutamate + (S)-2-amino-6-oxohexanoate + NADPH + H+
reaction of the SDH domain
-
-
r
N6-(L-1,3-dicarboxypropyl)-L-lysine + NADP+ + H2O
L-glutamate + (S)-2-amino-6-oxohexanoate + NADPH + H+
reaction of the SDH domain
-
-
r
N6-(L-1,3-dicarboxypropyl)-L-lysine + NADP+ + H2O
L-glutamate + (S)-2-amino-6-oxohexanoate + NADPH + H+
reaction of the SDH domain
-
-
r
N6-(L-1,3-dicarboxypropyl)-L-lysine + NADP+ + H2O
L-glutamate + (S)-2-amino-6-oxohexanoate + NADPH + H+
reaction of the SDH domain
-
-
r
N6-(L-1,3-dicarboxypropyl)-L-lysine + NADP+ + H2O
L-glutamate + (S)-2-amino-6-oxohexanoate + NADPH + H+
-
-
-
?
N6-(L-1,3-dicarboxypropyl)-L-lysine + NADP+ + H2O
L-glutamate + (S)-2-amino-6-oxohexanoate + NADPH + H+
-
-
-
r
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
NAD+
-
NAD+ and NADP+ equally effective in 2-aminoadipate 6-semialdehyde formation
NADP+
-
NAD+ and NADP+ equally effective in 2-aminoadipate 6-semialdehyde formation
additional information
A0A3L6FCN0
SDH domain hydrolyzes saccharopine into alpha-aminoadipate semialdehyde and glutamate using NAD(P)+ as cofactors, see also EC 1.5.1.9
-
additional information
SDH domain hydrolyzes saccharopine into alpha-aminoadipate semialdehyde and glutamate using NAD(P)+ as cofactors, see also EC 1.5.1.9
-
additional information
SDH domain hydrolyzes saccharopine into alpha-aminoadipate semialdehyde and glutamate using NAD(P)+ as cofactors, see also EC 1.5.1.9
-
additional information
SDH domain hydrolyzes saccharopine into alpha-aminoadipate semialdehyde and glutamate using NAD(P)+ as cofactors, see also EC 1.5.1.9
-
additional information
SDH domain hydrolyzes saccharopine into alpha-aminoadipate semialdehyde and glutamate using NAD(P)+ as cofactors, see also EC 1.5.1.9
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
Mg2+
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2-amino-6-heptenoic acid
-
competitive inhibition versus L-alpha-aminoadipate-delta-semialdehyde, uncompetitive inhibition versus NADPH, and noncompetitive inhibitition versus L-glutamate
2-oxoglutarate
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competitive inhibition versus L-glutamate and uncompetitive inhibition versus L-alpha-aminoadipate-delta-semialdehyde and NADPH; competitive inhibition versus saccharopine and uncompetitive inhibition versus NADP+
alpha-AASA
-
shows noncompetitive inhibition versus saccharopine and uncompetitive inhibition versus NADP+
glyoxylic acid
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competitive inhibition versus saccharopine and uncompetitive inhibition versus NADP+
L-glutamate
-
exhibits noncompetitive inhibition versus NADP+ and saccharopine
L-ornithine
-
competitive inhibition versus saccharopine and uncompetitive inhibition versus NADP+
L-pipecolic acid
-
competitive inhibition versus saccharopine and uncompetitive inhibition versus NADP+
N-oxalylglycine
-
competitive inhibition versus saccharopine and uncompetitive inhibition versus NADP+
NADP+
-
competitive inhibition versus NADPH, noncompetitive inhibition versus L-alpha-aminoadipate-delta-semialdehyde and L-glutamate
saccharopine
-
exhibits noncompetitive inhibition against L-alpha-aminoadipate-delta-semialdehyde, L-glutamate, and NADPH
L-leucine
-
competitive inhibition versus saccharopine and uncompetitive inhibition versus NADP+
NADPH
-
inhibition is competitive versus NADP+ and noncompetitive versus saccharopine
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
in immature rice endosperm, the enzymatic activity of the LKR domain is activated by Ca2+, Mg2+, high salt, and osmolytes
-
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5.5 - 7.8
-
pH 5.5: about 45% of activity maximum, pH 7.8: about 35% of activity maximum
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TEMPERATURE OPTIMUM
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
Agaricus bisporus Sylvan A15
strain Sylvan A15 commercially cultured in China
UniProt
brenda
serotype A, strain H99, human pathogen, chimeric spermidine synthase-saccharopine dehydrogenase gene (SPE3-LYS9)
SwissProt
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
additional information
developmental stage and tissue specific expression analysis, overview
brenda
additional information
Agaricus bisporus Sylvan A15
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developmental stage and tissue specific expression analysis, overview
-
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
additional information