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

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The expected taxonomic range for this enzyme is: Opisthokonta

EC NUMBER
COMMENTARY
1.5.1.10
-
RECOMMENDED NAME
GeneOntology No.
saccharopine dehydrogenase (NADP+, L-glutamate-forming)
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
N6-(L-1,3-dicarboxypropyl)-L-lysine + NADP+ + H2O = L-glutamate + (S)-2-amino-6-oxohexanoate + NADPH + H+
show the reaction diagram
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
PATHWAY
KEGG Link
MetaCyc Link
Biosynthesis of secondary metabolites
-
Lysine biosynthesis
-
lysine biosynthesis IV
-
Lysine degradation
-
Metabolic pathways
-
SYSTEMATIC NAME
IUBMB Comments
N6-(L-1,3-dicarboxypropyl)-L-lysine:NADP+ oxidoreductase (L-glutamate-forming)
-
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
aminoadipate semialdehyde-glutamate reductase
-
-
-
-
aminoadipic semialdehyde-glutamate reductase
-
-
-
-
aminoadipic semialdehyde-glutamic reductase
-
-
-
-
dehydrogenase, saccharopine (nicotinamide adenine dinucleotide phosphate, glutamate-forming)
-
-
-
-
epsilon-N-(L-glutaryl-2)-L-lysine:NAD+(P) oxidoreductase (L-2-aminoadipate-semialdehyde forming)
-
-
-
-
saccharopine dehydrogenase
-
-
saccharopine dehydrogenase (L-glutamate forming)
-
-
saccharopine reductase
-
-
-
-
saccharopine reductase
-
-
saccharopine reductase
-
-
CAS REGISTRY NUMBER
COMMENTARY
9033-55-0
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
low activity
-
-
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
gene lys7, strain Wis 54-1255
-
-
Manually annotated by BRENDA team
low activity
-
-
Manually annotated by BRENDA team
fission yeast
-
-
Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
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
-
-
-
-
r
2-aminoadipate 6-semialdehyde + L-glutamate + NADPH
N6-(L-1,3-dicarboxypropyl)-L-lysine + NADP+ + H2O
show the reaction diagram
-
-
-
r
2-aminoadipate 6-semialdehyde + L-glutamate + NADPH
N6-(L-1,3-dicarboxypropyl)-L-lysine + NADP+ + H2O
show the reaction diagram
-, Q96TW2
-
-
-
2-aminoadipate 6-semialdehyde + L-glutamate + NADPH
N6-(L-1,3-dicarboxypropyl)-L-lysine + NADP+ + H2O
show the reaction diagram
-
-
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
show the reaction diagram
-
-
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
show the reaction diagram
-
-
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
show the reaction diagram
-
lysine biosynthesis
-
-
2-aminoadipate 6-semialdehyde + L-glutamate + NADPH
N6-(L-1,3-dicarboxypropyl)-L-lysine + NADP+ + H2O
show the reaction diagram
-
lysine biosynthesis
-
-
2-aminoadipate 6-semialdehyde + L-glutamate + NADPH
N6-(L-1,3-dicarboxypropyl)-L-lysine + NADP+ + H2O
show the reaction diagram
-
lysine biosynthesis
-
-
2-aminoadipate 6-semialdehyde + L-glutamate + NADPH
N6-(L-1,3-dicarboxypropyl)-L-lysine + NADP+ + H2O
show the reaction diagram
Meyerozyma guilliermondii, Meyerozyma guilliermondii H17
-
lysine biosynthesis
-
-
2-aminoadipate 6-semialdehyde + L-glutamate + NADPH + H+
N6-(L-1,3-dicarboxypropyl)-L-lysine + NADP+ + H2O
show the reaction diagram
-
-
-
-
r
L-glutamate + 2-aminoadipate 6-semialdehyde + NADPH + H+
saccharopine + NADP+ + H2O
show the reaction diagram
-
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 + 2-aminoadipate 6-semialdehyde + NADPH + H+
show the reaction diagram
-
-
-
-
?
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
-
-
?
N6-(L-1,3-dicarboxypropyl)-L-lysine + NADP+ + H2O
L-glutamate + (S)-2-amino-6-oxohexanoate + NADPH + H+
show the reaction diagram
Q9P4R4
-
-
-
?
saccharopine + NADP+ + H2O
L-glutamate + 2-aminoadipate 6-semialdehyde + NADPH + H+
show the reaction diagram
-
reverse reaction direction used for activity assay, end product is piperidine-6-carboxylic acid in assays using cell extract
-
-
r
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
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
-
lysine biosynthesis
-
-
2-aminoadipate 6-semialdehyde + L-glutamate + NADPH
N6-(L-1,3-dicarboxypropyl)-L-lysine + NADP+ + H2O
show the reaction diagram
-
lysine biosynthesis
-
-
2-aminoadipate 6-semialdehyde + L-glutamate + NADPH
N6-(L-1,3-dicarboxypropyl)-L-lysine + NADP+ + H2O
show the reaction diagram
-
lysine biosynthesis
-
-
2-aminoadipate 6-semialdehyde + L-glutamate + NADPH
N6-(L-1,3-dicarboxypropyl)-L-lysine + NADP+ + H2O
show the reaction diagram
Meyerozyma guilliermondii, Meyerozyma guilliermondii H17
-
lysine biosynthesis
-
-
L-glutamate + 2-aminoadipate 6-semialdehyde + NADPH + H+
saccharopine + NADP+ + H2O
show the reaction diagram
-
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 + 2-aminoadipate 6-semialdehyde + NADPH + H+
show the reaction diagram
Q6RXX2
enzyme catalyzes the penultimate step in lysine biosynthesis
-
-
?
N6-(L-1,3-dicarboxypropyl)-L-lysine + NADP+ + H2O
L-glutamate + (S)-2-amino-6-oxohexanoate + NADPH + H+
show the reaction diagram
Q9P4R4
-
-
-
?
COFACTOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
NAD+
-
NAD+ and NADP+ equally effective in 2-aminoadipate 6-semialdehyde formation
NADH
-
NADPH far more effective than NADH in saccaropine formation
NADP+
-
NAD+ and NADP+ equally effective in 2-aminoadipate 6-semialdehyde formation
NADPH
-
far more effective than NADH in saccharopine formation
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
1,10-phenanthroline
-
-
2-amino-6-heptenoic acid
-
competitive inhibition versus L-alpha-aminoadipate-delta-semialdehyde, uncompetitive inhibition versus NADPH, and noncompetitive inhibtition versus L-glutamate
2-oxoglutarate
-
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
-
competitive inhibition versus saccharopine and uncompetitive inhibition versus NADP+
L-glutamate
-
exhibits noncompetitive inhibition versus NADP+ and saccharopine
L-leucine
-
competitive inhibition versus saccharopine and uncompetitive inhibition versus NADP+
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
NADPH
-
inhibition is competitive versus NADP+ and noncompetitive versus saccharopine
p-hydroxymercuribenzoate
-
-
saccharopine
-
exhibits noncompetitive inhibition against L-alpha-aminoadipate-delta-semialdehyde, L-glutamate, and NADPH
additional information
-
not: carbonyl reagents
-
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
2.32
-
L-saccharopine
-
-
1.25
-
saccharopine
-
-
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
0.044
-
-, Q96TW2
-
0.24
-
-
crude extract
22
-
-
wild-type strain Wis 54-1255, cell extract
269.4
-
-
after purification
additional information
-
-
-
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
7
-
-
saccharopine formation
8.8
-
-
saccharopine degradation
9.5
-
-
saccharopine degradation
10
-
-
saccharopine degradation
pH RANGE
pH RANGE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
5.5
7.8
-
pH 5.5: about 45% of activity maximum, pH 7.8: about 35% of activity maximum
8.3
10.3
-
about 50% of activity maximum at pH 8.3 and 10.3
9
10
-
about 50% of activity maximum at pH 9 and 10
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
SOURCE TISSUE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
SOURCE
PDB
SCOP
CATH
ORGANISM
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)
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
48000
-
-, Q96TW2
predicted from gene sequence
67000
-
-
gel filtration with Sephadex G-100
73000
-
-
density gradient centrifugation
84000
-
-
gel filtration with Superdex 200
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
dimer
-
alpha2, 2 * 48900, predicted mass from the gene sequence; alpha2, 2 * 50000, SDS-PAGE
monomer
-
1 * 50000, SDS-PAGE
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
no glycoprotein
-
-
Crystallization/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
with hanging-drop vapour-diffusion technique
-
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
-
TEMPERATURE STABILITY
TEMPERATURE STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
34
-
-
denaturation above
STORAGE STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
-70°C, pH 8.0, 10 mM 2-mercaptoethanol, 5 mM EDTA
-
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
purification of heterologously expressed enzyme
-
Ni-NTA column chromatography
-
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
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
Q6RXX2
cloned in Escherichia coli
-
gene lys, subcloning in Escherichia coli
-
expressed in Escherichia coli
-
expressed in Escherichia coli BL21/(DE-3) RIL cells
-
ENGINEERING
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
additional information
Q6RXX2
construction of 3 Spe3-Lys9 mutants, with defects in the spe3-part, the lys9-part, or both, which are auxotrophic for lysine and spermidine, spermidine, and lysine, respectively, transcription levels and phenotype overview, the polyamine auxotrophy due to defect spe3 cannot be overcome by spermine addition, while the mutan with lys 9 defect grows slowly at 30°C with lysine addition, but dies upon lysine starvation, the mutant with defects in both gene parts is avirulent and lethal
additional information
-
construction of an enzyme-deficient mutant strain: disruption and inactivation of gene lys7 by double-recombination method leads to lysine auxotrophy and accumulation of piperideine-6-carboxylic acid, and with L-lysine as sole N-source and supplementation of DL-alpha-aminoadipic acid, also of pipecolic acid, transformation of the mutant strain with lys7 can restore enzyme activity