Information on EC 1.5.1.10 - saccharopine dehydrogenase (NADP+, L-glutamate-forming)

for references in articles please use BRENDA:EC1.5.1.10
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The enzyme appears in viruses and cellular organisms

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EC NUMBER
COMMENTARY hide
1.5.1.10
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RECOMMENDED NAME
GeneOntology No.
saccharopine dehydrogenase (NADP+, L-glutamate-forming)
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
N6-(L-1,3-dicarboxypropyl)-L-lysine + NADP+ + H2O = L-glutamate + (S)-2-amino-6-oxohexanoate + NADPH + H+
show the reaction diagram
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
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-
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redox reaction
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reduction
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
L-lysine biosynthesis IV
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lysine metabolism
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Lysine biosynthesis
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Lysine degradation
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Metabolic pathways
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Biosynthesis of secondary metabolites
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Biosynthesis of antibiotics
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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 hide
9033-55-0
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
low activity
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Manually annotated by BRENDA team
serotype A, strain H99, human pathogen, chimeric spermidine synthase-saccharopine dehydrogenase gene (SPE3-LYS9)
SwissProt
Manually annotated by BRENDA team
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Manually annotated by BRENDA team
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UniProt
Manually annotated by BRENDA team
low activity
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Manually annotated by BRENDA team
fission yeast
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Manually annotated by BRENDA team
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2-aminoadipate 6-semialdehyde + L-glutamate + NADPH
N6-(L-1,3-dicarboxypropyl)-L-lysine + NADP+ + H2O
show the reaction diagram
2-aminoadipate 6-semialdehyde + L-glutamate + NADPH + H+
N6-(L-1,3-dicarboxypropyl)-L-lysine + NADP+ + H2O
show the reaction diagram
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r
L-glutamate + 2-aminoadipate 6-semialdehyde + NADPH + H+
saccharopine + NADP+ + H2O
show the reaction diagram
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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 + NADP+ + H2O
L-glutamate + (S)-2-amino-6-oxohexanoate + NADPH + H+
show the reaction diagram
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-
-
?
N6-(L-1,3-dicarboxypropyl)-L-lysine + NADP+ + H2O
L-glutamate + 2-aminoadipate 6-semialdehyde + NADPH + H+
show the reaction diagram
saccharopine + NADP+ + H2O
L-glutamate + 2-aminoadipate 6-semialdehyde + NADPH + H+
show the reaction diagram
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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
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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
2-aminoadipate 6-semialdehyde + L-glutamate + NADPH
N6-(L-1,3-dicarboxypropyl)-L-lysine + NADP+ + H2O
show the reaction diagram
L-glutamate + 2-aminoadipate 6-semialdehyde + NADPH + H+
saccharopine + NADP+ + H2O
show the reaction diagram
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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 + NADP+ + H2O
L-glutamate + (S)-2-amino-6-oxohexanoate + NADPH + H+
show the reaction diagram
Q9P4R4
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?
N6-(L-1,3-dicarboxypropyl)-L-lysine + NADP+ + H2O
L-glutamate + 2-aminoadipate 6-semialdehyde + NADPH + H+
show the reaction diagram
Q6RXX2
enzyme catalyzes the penultimate step in lysine biosynthesis
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?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NAD+
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NAD+ and NADP+ equally effective in 2-aminoadipate 6-semialdehyde formation
NADH
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NADPH far more effective than NADH in saccaropine formation
NADP+
NADPH
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1,10-phenanthroline
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2,2'-bipyridine
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2-amino-6-heptenoic acid
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competitive inhibition versus L-alpha-aminoadipate-delta-semialdehyde, uncompetitive inhibition versus NADPH, and noncompetitive inhibtition 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
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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
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exhibits noncompetitive inhibition versus NADP+ and saccharopine
L-leucine
L-ornithine
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competitive inhibition versus saccharopine and uncompetitive inhibition versus NADP+
L-Pipecolic acid
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competitive inhibition versus saccharopine and uncompetitive inhibition versus NADP+
N-oxalylglycine
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competitive inhibition versus saccharopine and uncompetitive inhibition versus NADP+
NADP+
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competitive inhibition versus NADPH, noncompetitive inhibition versus L-alpha-aminoadipate-delta-semialdehyde and L-glutamate
NADPH
p-hydroxymercuribenzoate
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saccharopine
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exhibits noncompetitive inhibition against L-alpha-aminoadipate-delta-semialdehyde, L-glutamate, and NADPH
additional information
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not: carbonyl reagents
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2.32
L-saccharopine
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0.17 - 0.22
NADP+
0.92 - 1.25
saccharopine
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.24
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crude extract
22
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wild-type strain Wis 54-1255, cell extract
269.4
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after purification
additional information
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
8.8
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saccharopine degradation
9.5
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saccharopine degradation
10
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saccharopine degradation
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.5 - 7.8
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pH 5.5: about 45% of activity maximum, pH 7.8: about 35% of activity maximum
8.3 - 10.3
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about 50% of activity maximum at pH 8.3 and 10.3
9 - 10
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about 50% of activity maximum at pH 9 and 10
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
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PDB
SCOP
CATH
ORGANISM
UNIPROT
Magnaporthe oryzae (strain 70-15 / ATCC MYA-4617 / FGSC 8958)
Magnaporthe oryzae (strain 70-15 / ATCC MYA-4617 / FGSC 8958)
Magnaporthe oryzae (strain 70-15 / ATCC MYA-4617 / FGSC 8958)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
48000
predicted from gene sequence
48900
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alpha2, 2 * 48900, predicted mass from the gene sequence
67000
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gel filtration with Sephadex G-100
73000
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density gradient centrifugation
84000
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gel filtration with Superdex 200
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
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alpha2, 2 * 48900, predicted mass from the gene sequence; alpha2, 2 * 50000, SDS-PAGE
monomer
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1 * 50000, SDS-PAGE
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
no glycoprotein
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-
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Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
with hanging-drop vapour-diffusion technique
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apo form of enzyme. Protein consists of domain I, a variant of the Rossman fold and binding to NADPH, domain II with an alpha/beta structure and binding saccharopine, and domain III with all-helical fold involved in closing the active site of the enzyme once substrates are bound
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
34
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denaturation above
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-70°C, pH 8.0, 10 mM 2-mercaptoethanol, 5 mM EDTA
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Ni-NTA column chromatography
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purification of heterologously expressed enzyme
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
cloned in Escherichia coli
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expressed in Escherichia coli
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expressed in Escherichia coli BL21/(DE-3) RIL cells
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gene lys, subcloning in Escherichia coli
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gene LYS9 is organized as a chimeric spermidine synthase-saccharopine dehydrogenase gene (SPE3-LYS9) encoding functional spermidine synthase, EC 2.5.1.16, and saccharopine dehydrogenase, DNA and amino acid sequence determination and analysis, expression of wild-type enzyme in Saccharomyces cerevisiae, the chimeric gene can complement a Saccharomyces cerevisiae lys9 mutant, but not a spe3 mutant
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
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LINKS TO OTHER DATABASES (specific for EC-Number 1.5.1.10)
ExplorEnz
ExPASy
KEGG
MetaCyc
SABIO-RK
NCBI: PubMed, Protein, Nucleotide, Structure, Genome, OMIM
IUBMB Enzyme Nomenclature
PROSITE Database of protein families and domains
InterPro (database of protein families, domains and functional sites)