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Enzyme Nomenclature
Information on EC 1.5.1.9 - saccharopine dehydrogenase (NAD+, L-glutamate-forming)
for references in articles please use BRENDA:EC1.5.1.9
Word Map on EC 1.5.1.9
- 1.5.1.9
-
1.5.1.8
-
lysine-ketoglutarate
-
tetrameric
- pipecolate
- alpha-ketoglutarate
- spermidine
- ornithine
- hyperlysinemias
-
polyamine
- maize
- analysis
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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
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EC NUMBER 
COMMENTARY 
1.5.1.9
-
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RECOMMENDED NAME
GeneOntology No.
saccharopine dehydrogenase (NAD+, L-glutamate-forming)
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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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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
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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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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
; bifunctional lysine-ketoglutarate reductase/saccharopine dehydrogenase, EC 1.5.8 and EC 1.5.9
-
-
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
-
-
bifunctional spermidine synthase, and saccharopine dehydrogenase
UniProt
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; maize hybrid F-352
-
-
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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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
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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+
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 + 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
-
-
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 SUBSTRATES
NATURAL PRODUCTS
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+
D8WKY4
-
-
-
?
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+
-
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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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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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
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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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
additional information
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
additional information
-
no activity in: human heart, muscle, skin, brain, spleen, pancreas, adrenal, lung, gut, leukocytes and erythrocytes
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
44000
44100
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
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
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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SUBUNITS
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; x * 63000, SDS-PAGE, monofunctional enzyme
?
-
x * 44000, calculated from amino acid sequence; x * 44100, SDS-PAGE
-
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
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
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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
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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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LINKS TO OTHER DATABASES (specific for EC-Number 1.5.1.9)
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