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Information on EC 1.5.1.10 - saccharopine dehydrogenase (NADP+, L-glutamate-forming) for references in articles please use BRENDA:EC1.5.1.10Word Map on EC 1.5.1.10
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The enzyme appears in viruses and cellular organisms
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saccharopine dehydrogenase (NADP+, L-glutamate-forming)
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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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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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L-lysine biosynthesis IV
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Biosynthesis of secondary metabolites
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Biosynthesis of antibiotics
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N6-(L-1,3-dicarboxypropyl)-L-lysine:NADP+ oxidoreductase (L-glutamate-forming)
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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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saccharopine dehydrogenase
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saccharopine dehydrogenase (L-glutamate forming)
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saccharopine reductase
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saccharopine reductase
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saccharopine reductase
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low activity
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brenda
serotype A, strain H99, human pathogen, chimeric spermidine synthase-saccharopine dehydrogenase gene (SPE3-LYS9)
SwissProt
brenda
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brenda
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UniProt
brenda
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brenda
low activity
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brenda
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brenda
fission yeast
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brenda
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SwissProt
brenda
gene lys7, strain Wis 54-1255
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brenda
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brenda
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UniProt
brenda
baker's yeast
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brenda
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physiological function
saccharopine reductase catalyzes the reductive amination of L-alpha-aminoadipate-delta-semialdehyde with L-glutamate to give saccharopine
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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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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 + 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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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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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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?
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 + 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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?
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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
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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+
N6-(L-1,3-dicarboxypropyl)-L-lysine + NADP+ + H2O
L-glutamate + 2-aminoadipate 6-semialdehyde + NADPH + H+
Q6RXX2
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
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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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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+
Q9P4R4
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?
N6-(L-1,3-dicarboxypropyl)-L-lysine + NADP+ + H2O
L-glutamate + (S)-2-amino-6-oxohexanoate + NADPH + H+
P38999
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r
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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+
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NAD+ and NADP+ equally effective in 2-aminoadipate 6-semialdehyde formation
NADPH
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far more effective than NADH in saccharopine formation
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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-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
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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L-leucine
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L-leucine
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competitive inhibition versus saccharopine and uncompetitive inhibition versus NADP+
NADPH
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inhibition is competitive versus NADP+ and noncompetitive versus saccharopine
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0.17
NADP+
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0.92
saccharopine
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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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additional information
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8.8
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saccharopine degradation
9.5
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saccharopine degradation
10
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saccharopine degradation
7
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saccharopine formation
7
formation of L-saccharopin
9
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assay at
9
formation of L-glutamate
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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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brenda
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brenda
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brenda
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brenda
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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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48000
predicted from gene sequence
48900
-
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
50000
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1 * 50000, SDS-PAGE
50000
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alpha2, 2 * 50000, SDS-PAGE
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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
additional information
comparison of enzyme structures from Saccharomyces cerevisiae and Magnoporthe grisea
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with hanging-drop vapour-diffusion technique
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analysis of the apoenzyme crystal structure determined at 1.7 A resolution
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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-70°C, pH 8.0, 10 mM 2-mercaptoethanol, 5 mM EDTA
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Ni-NTA column chromatography
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purification of heterologously expressed enzyme
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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
recombinant expression of wild-type and mutant enzymes in Saccharomyces cerevisiae strain LYS 9
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C154S
site-directed mutagenesis
C154S/Y99F
site-directed mutagenesis
D126A
site-directed mutagenesis
D126A/C154S
site-directed mutagenesis
D126A/Y99F
site-directed mutagenesis
Y99F
site-directed mutagenesis
additional information
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
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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
additional information
kinetic parameters of the mutants in the reaction direction of glutamate formation exhibit modest decreases. The pH-rate profiles obtained with all mutant enzymes decrease at low and high pH, suggesting acid and base catalytic groups are still present in all enzymes. Solvent kinetic deuterium isotope effects are all larger than those observed for wild-type enzyme
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LYS9_MAGO7
Magnaporthe oryzae (strain 70-15 / ATCC MYA-4617 / FGSC 8958)
450
49097
Swiss-Prot
LYS9_SCHPO
Schizosaccharomyces pombe (strain 972 / ATCC 24843)
450
49938
Swiss-Prot
LYS9_YEAST
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
446
48918
Swiss-Prot
SCPDH_DICDI
480
53359
Swiss-Prot
A0A090VSN3_9FLAO
454
51397
TrEMBL
A0A099XPX6_9FLAO
457
52070
TrEMBL
A0A2H3FDC4_9HELO
442
48528
TrEMBL
G2PM06_MURRD
Muricauda ruestringensis (strain DSM 13258 / CIP 107369 / LMG 19739 / B1)
457
52295
TrEMBL
A0A084GH64_9PEZI
448
48979
TrEMBL
A0A1W6VNB5_GEOTD
386
42520
TrEMBL
A0A0L1HFB5_9PLEO
468
51218
TrEMBL
C0Q9S4_DESAH
Desulfobacterium autotrophicum (strain ATCC 43914 / DSM 3382 / HRM2)
395
43887
TrEMBL
I3R7M9_HALMT
Haloferax mediterranei (strain ATCC 33500 / DSM 1411 / JCM 8866 / NBRC 14739 / NCIMB 2177 / R-4)
412
44444
TrEMBL
B9RR16_RICCO
1050
116123
TrEMBL
S7VT91_9FLAO
454
51638
TrEMBL
A0A0P7W451_9RHOB
375
41354
TrEMBL
F4B1B9_DOKS4
Dokdonia sp. (strain 4H-3-7-5)
456
51908
TrEMBL
A0A0F8DHK5_CERFI
450
48510
TrEMBL
W8EYC3_9BACT
458
50653
TrEMBL
A0A0S1XFW3_9EURY
354
40374
TrEMBL
E3D063_9BACT
443
49180
TrEMBL
A0A1W1HJ15_9DELT
444
49423
TrEMBL
Q5V5J8_HALMA
Haloarcula marismortui (strain ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809)
429
46468
TrEMBL
A0A0P8AAH9_9RHOB
208
23075
TrEMBL
H6RES7_9BACT
449
51706
TrEMBL
A0A090QAW4_9FLAO
455
51630
TrEMBL
A0A0N1NES3_9ACTN
383
41016
TrEMBL
C5PG82_COCP7
Coccidioides posadasii (strain C735)
450
49471
TrEMBL
B0CXB5_LACBS
Laccaria bicolor (strain S238N-H82 / ATCC MYA-4686)
751
82177
TrEMBL
C5A6R0_THEGJ
Thermococcus gammatolerans (strain DSM 15229 / JCM 11827 / EJ3)
357
40117
TrEMBL
A0A090PH63_9FLAO
195
22229
TrEMBL
G0LAJ7_ZOBGA
Zobellia galactanivorans (strain DSM 12802 / CCUG 47099 / CIP 106680 / NCIMB 13871 / Dsij)
459
52506
TrEMBL
A0A090PXM0_9FLAO
454
51999
TrEMBL
E3CYK0_9BACT
445
49081
TrEMBL
A0A090PMU3_9FLAO
97
11516
TrEMBL
G8TFI1_NIAKG
Niastella koreensis (strain DSM 17620 / KACC 11465 / GR20-10)
504
56256
TrEMBL
D5HCD9_SALRM
Salinibacter ruber (strain M8)
416
45940
TrEMBL
A0A0F4YTX1_TALEM
461
50903
TrEMBL
A0A1S8A5N8_ROSNE
414
45275
TrEMBL
V9WMQ3_9RHOB
380
41733
TrEMBL
B9WEP0_CANDC
Candida dubliniensis (strain CD36 / ATCC MYA-646 / CBS 7987 / NCPF 3949 / NRRL Y-17841)
444
49245
TrEMBL
G3Y9B4_ASPNA
Aspergillus niger (strain ATCC 1015 / CBS 113.46 / FGSC A1144 / LSHB Ac4 / NCTC 3858a / NRRL 328 / USDA 3528.7)
450
49357
TrEMBL
E4TQK6_MARTH
Marivirga tractuosa (strain ATCC 23168 / DSM 4126 / NBRC 15989 / NCIMB 1408 / VKM B-1430 / H-43)
446
50565
TrEMBL
A0A090WWD9_9FLAO
454
51955
TrEMBL
A0A2S5BAT4_9BASI
750
81646
TrEMBL
A0A0A0HGR3_9RHOB
380
41991
TrEMBL
A2QIZ4_ASPNC
Aspergillus niger (strain CBS 513.88 / FGSC A1513)
448
49146
TrEMBL
A0A2V5GM47_9RHOB
380
41651
TrEMBL
A0A090W5I6_9FLAO
454
51897
TrEMBL
A0A076P6U3_FLAPS
456
51894
TrEMBL
F6GI30_LACS5
Lacinutrix sp. (strain 5H-3-7-4)
454
51513
TrEMBL
A2QB21_ASPNC
Aspergillus niger (strain CBS 513.88 / FGSC A1513)
462
49774
TrEMBL
A0A060TBC7_BLAAD
454
49618
TrEMBL
A7BNY1_9GAMM
257
28965
TrEMBL
A0A2H3EET9_9HELO
447
49127
TrEMBL
W1QIX7_OGAPD
Ogataea parapolymorpha (strain ATCC 26012 / BCRC 20466 / JCM 22074 / NRRL Y-7560 / DL-1)
445
48835
TrEMBL
E6X545_CELAD
Cellulophaga algicola (strain DSM 14237 / IC166 / ACAM 630)
457
52056
TrEMBL
A0A1S6HS69_9GAMM
386
42845
TrEMBL
A0A099KRI5_COLPS
386
42656
TrEMBL
A0A090Q8W3_9FLAO
107
11926
TrEMBL
F2ICS7_FLUTR
Fluviicola taffensis (strain DSM 16823 / NCIMB 13979 / RW262)
445
50560
TrEMBL
A0A2H1E7S8_9FLAO
465
52845
TrEMBL
G0HW78_HALHT
Haloarcula hispanica (strain ATCC 33960 / DSM 4426 / JCM 8911 / NBRC 102182 / NCIMB 2187 / VKM B-1755)
426
46388
TrEMBL
A3LQ43_PICST
Scheffersomyces stipitis (strain ATCC 58785 / CBS 6054 / NBRC 10063 / NRRL Y-11545)
444
48567
TrEMBL
G7V6N8_THELD
Thermovirga lienii (strain ATCC BAA-1197 / DSM 17291 / Cas60314)
440
48647
TrEMBL
A0A0G2RK33_9PLEO
472
51551
TrEMBL
F4L7G5_HALH1
Haliscomenobacter hydrossis (strain ATCC 27775 / DSM 1100 / LMG 10767 / O)
444
50209
TrEMBL
A0A2G9GK14_9LAMI
464
50900
TrEMBL
A0A2G9H4X7_9LAMI
411
44513
TrEMBL
T2KQ06_9FLAO
454
52127
TrEMBL
A0A0J5TF32_9RHOB
379
41730
TrEMBL
Q96TW2_PENCH
449
48752
TrEMBL
S0G1D7_9DELT
392
42740
TrEMBL
A0A081DCS1_9FLAO
455
51631
TrEMBL
A0A099KIE0_9GAMM
388
43238
TrEMBL
Q6RXX2_CRYNV
750
82620
TrEMBL
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Ye, Z.H.; Bhattacharjee, J.K.
Lysine biosynthesis pathway and biochemical blocks of lysine auxotrophs of Schizosaccharomyces pombe
J. Bacteriol.
170
5968-5970
1988
Schizosaccharomyces pombe
brenda
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Conversion of pipecolic acid into lysine in Penicillium chrysogenum requires pipecolate oxidase and saccharopine reductase: characterization of the lys7 gene encoding saccharopine reductase
J. Bacteriol.
183
7165-7172
2001
Penicillium chrysogenum, Penicillium chrysogenum (Q96TW2)
brenda
Mukhopadhyay, A.; Mungre, S.M.; Desmukh, D.R.
Comparison of lysine and tryptophan catabolizing enzymes in rat and bovine tissues
Experientia
46
874-876
1990
Bos taurus, Rattus norvegicus
brenda
Schmidt, H.; Bode, R.; Birnbaum, D.
Regulation of the lysine biosynthesis in Pichia guilliermondii
Antonie van Leeuwenhoek
56
337-347
1989
Meyerozyma guilliermondii
brenda
Broquist, H.P.
Aminoadipic semialdehyde-glutamate reductase
Methods Enzymol.
17B
121-124
1971
Saccharomyces cerevisiae
-
brenda
Jones, E.E.; Broquist, H.P.
Saccharopine, an intermediate of the aminoadipic acid pathway of lysine biosynthesis. 3. Aminoadipic semialdehyde-glutamate reductase
J. Biol. Chem.
241
3430-3434
1966
Saccharomyces cerevisiae
brenda
Storts, D.R.; Bhattacharjee, J.K.
Purification and properties of saccharopine dehydrogenase (glutamate forming) in the Saccharomyces cerevisiae lysine biosynthetic pathway
J. Bacteriol.
169
416-418
1987
Saccharomyces cerevisiae
brenda
Kinzel, J.J.; Bhattacharjee, J.K.
Role of pipecolic acid in the biosynthesis of lysine in Rhodotorula glutinis
J. Bacteriol.
138
410-417
1979
Rhodotorula glutinis
brenda
Johansson, E.; Steffens, J.J.; Emptage, M.; Lindqvist, Y.; Schneider, G.
Cloning, expression, purification and crystallization of saccharopine reductase from Magnaporthe grisea
Acta Crystallogr. Sect. D
56
662-664
2000
Magnaporthe grisea
-
brenda
Naranjo, L.; Martin de Valmaseda, E.; Casqueiro, J.; Ullan, R.V.; Lamas-Maceiras, M.; Banuelos, O.; Martin, J.F.
Inactivation of the lys7 gene, encoding saccharopine reductase in Penicillium chrysogenum, leads to accumulation of the secondary metabolite precursors piperideine-6-carboxylic acid and pipecolic acid from alpha-aminoadipic acid
Appl. Environ. Microbiol.
70
1031-1039
2004
Penicillium chrysogenum
brenda
Kingsbury, J.M.; Yang, Z.; Ganous, T.M.; Cox, G.M.; McCusker, J.H.
Novel chimeric spermidine synthase-saccharopine dehydrogenase gene (SPE3-LYS9) in the human pathogen Cryptococcus neoformans
Eukaryot. Cell
3
752-763
2004
Cryptococcus neoformans (Q6RXX2)
brenda
Andi, B.; Cook, P.F.; West, A.H.
Crystal structure of the his-tagged saccharopine reductase from Saccharomyces cerevisiae at 1.7-A resolution
Cell Biochem. Biophys.
46
17-26
2006
Saccharomyces cerevisiae
brenda
Vashishtha, A.K.; West, A.H.; Cook, P.F.
Overall kinetic mechanism of saccharopine dehydrogenase (L-glutamate forming) from Saccharomyces cerevisiae
Biochemistry
47
5417-5423
2008
Saccharomyces cerevisiae
brenda
Vashishtha, A.K.; West, A.H.; Cook, P.F.
Chemical mechanism of saccharopine reductase from Saccharomyces cerevisiae
Biochemistry
48
5899-5907
2009
Saccharomyces cerevisiae
brenda
Almasi, J.; Bushnell, E.; Gauld, J.
A QM/MM-based computational investigation on the catalytic mechanism of saccharopine reductase
Molecules
16
8569-8589
2011
Magnaporthe oryzae (Q9P4R4)
brenda
Vashishtha, A.K.; West, A.H.; Cook, P.F.
Probing the chemical mechanism of saccharopine reductase from Saccharomyces cerevisiae using site-directed mutagenesis
Arch. Biochem. Biophys.
584
98-106
2015
Saccharomyces cerevisiae (P38999), Saccharomyces cerevisiae
brenda
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