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

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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria

EC NUMBER
COMMENTARY hide
1.5.1.9
-
RECOMMENDED NAME
GeneOntology No.
saccharopine dehydrogenase (NAD+, L-glutamate-forming)
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
N6-(L-1,3-dicarboxypropyl)-L-lysine + NAD+ + H2O = L-glutamate + (S)-2-amino-6-oxohexanoate + NADH + H+
show the reaction diagram
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Biosynthesis of antibiotics
-
-
Biosynthesis of secondary metabolites
-
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L-lysine degradation XI (mammalian)
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-
Lysine degradation
-
-
Metabolic pathways
-
-
lysine metabolism
-
-
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.
CAS REGISTRY NUMBER
COMMENTARY hide
37256-26-1
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
ecotype C-24
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
soybean cv Samsun
-
-
Manually annotated by BRENDA team
; bifunctional lysine-ketoglutarate reductase/saccharopine dehydrogenase, EC 1.5.8 and EC 1.5.9
-
-
Manually annotated by BRENDA team
cultivar Steffi
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
rice var IAC-165
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
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
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
Moench
-
-
Manually annotated by BRENDA team
Moench
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
subspecies Triticum turgidum durum
UniProt
Manually annotated by BRENDA team
bifunctional spermidine synthase, and saccharopine dehydrogenase
UniProt
Manually annotated by BRENDA team
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
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
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
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
N6-(L-1,3-dicarboxypropyl)-L-lysine + NAD+ + H2O
L-Glu + 2-aminoadipate 6-semialdehyde + NADH
show the reaction diagram
N6-(L-1,3-dicarboxypropyl)-L-lysine + NAD+ + H2O
L-glutamate + (S)-2-amino-6-oxohexanoate + NADH + H+
show the reaction diagram
-
-
-
?
N6-(L-1,3-dicarboxypropyl)-L-lysine + NAD+ + H2O
L-glutamate + 2-aminoadipate 6-semialdehyde + NADH + H+
show the reaction diagram
saccharopine + NAD+ + H2O
L-glutamate + alpha-aminoadipate semialdehyde + NADH + H+
show the reaction diagram
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
N6-(L-1,3-dicarboxypropyl)-L-lysine + NAD+ + H2O
L-Glu + 2-aminoadipate 6-semialdehyde + NADH
show the reaction diagram
-
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+
show the reaction diagram
D8WKY4
-
-
-
?
N6-(L-1,3-dicarboxypropyl)-L-lysine + NAD+ + H2O
L-glutamate + 2-aminoadipate 6-semialdehyde + NADH + H+
show the reaction diagram
saccharopine + NAD+ + H2O
L-glutamate + alpha-aminoadipate semialdehyde + NADH + H+
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NADP+
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Cu2+
-
strong inhibition
Hg2+
-
strong inhibition
Zn2+
-
strong inhibition
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2-Aminoadipate
-
strong inhibition at 5 mM
2-oxoglutarate
-
-
3-acetylpyridine-NAD
-
15% inhibition
3-pyridine aldehyde-NAD
-
40% inhibition
hydroxylamine
-
slight
L-glutamate
-
-
NH4Cl
-
slight
p-hydroxymercuribenzoate
-
-
Sodium bisulfite
-
slight
additional information
-
not: L-lysine-p-nitroanilide
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0645 - 0.759
NAD+
0.035 - 1.15
saccharopine
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.0015
-
crude extract from developing seeds
0.0017
-
crude extract from immature seeds
0.0024
-
crude extract from immature endosperm
0.0045
-
-
0.0047
-
-
0.0054
-
-
0.0058
-
-
0.0069
-
-
0.03
-
crude extract
0.052
-
after purification
2.14
-
after purification
2.608
-
after purification
16.8
-
saccharopine dehydrogenase activity
17.2
-
after purification
additional information
-
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
8.8 - 9
-
-
8.9
-
2-amino-2-methyl-1,3-propanediol buffer
9
-
monofunctional enzyme
additional information
-
pH-optimum above pH 8.5
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.5 - 10
-
no activity below pH 6 and over pH 10
7.8 - 9.7
-
half maximal activities at pH 7.8 and 9.7
7.9 - 9.3
-
half maximal activities at pH 7.9 and 9.3
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
20 - 37
-
20°C: 35% of activity maximum, 37°C: 85% of activity maximum
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
the SDH mRNA transcripts are more abundant in unfed and starved ticks than in fed and engorged ticks
Manually annotated by BRENDA team
-
very low activity
Manually annotated by BRENDA team
additional information
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
48000
-
calculated from amino acid sequence
63000
-
x * 63000, SDS-PAGE, monofunctional enzyme
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
396000
-
native non-denaturing gel, low activity compared to 202000 kDa band
420000
-
sedimentation equilibrium method
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
480000
-
gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
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
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4.4
-
10 min, 60% activity
392361
4.6 - 4.9
-
10 min
392361
5 - 10
-
inactive under acidic (pH 5) or alkaline (pH 10) conditions
700907
6.6 - 9.9
-
10 min
396543
8.5
-
unstable at high pH, beta-mercaptoethanol protects
396540
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37
-
5 min
44
-
5 min, 50% activity
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
very unstable during the isolation and purification procedure
-
OXIDATION STABILITY
ORGANISM
UNIPROT
LITERATURE
5 mM beta-mercaptoethanol preserves loss of activity during enzyme assay
-
396540
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, crude enzyme stable for several months, purified enzyme inactivated within 3 weeks
-
2°C, 5-10% loss of activity per week, purified enzyme
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
heterologously expressed enzyme
-
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
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli and Sf9 insect cells
-
expressed in Escherichia coli BL21(DE3) cells
in yeast for heterologous expression
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
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
Show AA Sequence (110 entries)
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