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Information on EC 1.5.1.7 - saccharopine dehydrogenase (NAD+, L-lysine-forming)
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EC Tree
1.5.1.7 saccharopine dehydrogenase (NAD+, L-lysine-forming)Specify your search results
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Reaction Schemes
Synonyms
dehydrogenase, saccharopine (nicotinamide adenine dinucleotide, lysine forming), epsilon-N-(L-glutaryl-2)-L-lysine:NAD oxidoreductase (L-lysine forming), Lysine--2-oxoglutarate reductase, lysine-2-oxoglutarate reductase, N6-(glutar-2-yl)-L-lysine:NAD oxidoreductase (L-lysine-forming), N6-(glutaryl-2)-L-lysine: NAD oxidoreductase, N6-(glutaryl-2)-L-lysine: NAD+ oxidoreductase, N6-(glutaryl-2)-l-lysine:NAD oxidoreductase, N6-(glutaryl-2)-L-lysine:NAD oxidoreductase (L-lysine forming), N6-(glutaryl-2)-L-lysine:NAD-oxidoreductase (L-lysine-forming), 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
dehydrogenase, saccharopine (nicotinamide adenine dinucleotide, lysine forming)
-
-
-
-
epsilon-N-(L-glutaryl-2)-L-lysine:NAD oxidoreductase (L-lysine forming)
-
-
-
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Lysine--2-oxoglutarate reductase
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-
-
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lysine-2-oxoglutarate reductase
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-
-
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N6-(glutar-2-yl)-L-lysine:NAD oxidoreductase (L-lysine-forming)
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-
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N6-(glutaryl-2)-L-lysine:NAD oxidoreductase (L-lysine forming)
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N6-(glutaryl-2)-L-lysine:nicotinamide adenine dinucleotide (NAD+) oxidoreductase (L-lysine-forming)
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saccharopine dehydrogenase
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catalyzes the final step in the alpha-aminoadipate pathway for lysine biosynthesis
SDH
SDH
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
N6-(L-1,3-dicarboxypropyl)-L-lysine + NAD+ + H2O = L-lysine + 2-oxoglutarate + NADH + H+
mechanism
-
N6-(L-1,3-dicarboxypropyl)-L-lysine + NAD+ + H2O = L-lysine + 2-oxoglutarate + NADH + H+
model of proton shuttle mechanism. Concerted proton and hydride transfer, proton transfer exists in at least two sequential transition states
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N6-(L-1,3-dicarboxypropyl)-L-lysine + NAD+ + H2O = L-lysine + 2-oxoglutarate + NADH + H+
ordered addition of NAD followed by saccharopine in the physiologic reaction direction. In the opposite direction, NADH adds to the enzyme first, while there is no preference for the order of binding of alpha-ketoglutarate and lysine
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N6-(L-1,3-dicarboxypropyl)-L-lysine + NAD+ + H2O = L-lysine + 2-oxoglutarate + NADH + H+
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
-
-
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redox reaction
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-
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reduction
-
-
-
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reductive condensation
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PATHWAY SOURCE
PATHWAYS
BRENDA
MetaCyc
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SYSTEMATIC NAME
IUBMB Comments
N6-(L-1,3-dicarboxypropyl)-L-lysine:NAD+ oxidoreductase (L-lysine-forming)
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CAS REGISTRY NUMBER
COMMENTARY
9073-96-5
-
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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
additional information
?
-
-
3-acetylpyridine adenine dinucleotide, 3-pyridinealdehyde adenine dinucleotide, and thionicotinamide adenine dinucleotide can serve as a substrate in the oxidative deamination reaction, as can glyoxylate, pyruvate, alpha-ketobutyrate, alpha-ketovalerate, alpha-ketomalonate, and alpha-ketoadipate in the reverse reaction
-
-
?
L-lysine + 2-oxoglutarate + NADH
N6-(L-1,3-dicarboxypropyl)-L-lysine + NAD+ + H2O
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-
-
-
?
L-lysine + 2-oxoglutarate + NADH
N6-(L-1,3-dicarboxypropyl)-L-lysine + NAD+ + H2O
-
-
-
r
L-lysine + 2-oxoglutarate + NADH + H+
N6-(L-1,3-dicarboxypropyl)-L-lysine + NAD+ + H2O
-
-
-
-
?
L-lysine + 2-oxoglutarate + NADH + H+
N6-(L-1,3-dicarboxypropyl)-L-lysine + NAD+ + H2O
-
-
-
-
r
N6-(L-1,3-dicarboxypropyl)-L-lysine + NAD+ + H2O
L-lysine + 2-oxoglutarate + NADH
-
i.e. saccharopine
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r
N6-(L-1,3-dicarboxypropyl)-L-lysine + NAD+ + H2O
L-lysine + 2-oxoglutarate + NADH
-
involved in lysine biosynthesis
-
-
?
N6-(L-1,3-dicarboxypropyl)-L-lysine + NAD+ + H2O
L-lysine + 2-oxoglutarate + NADH
-
last step of alpha-aminoadipate pathway for lysine biosynthesis
-
-
?
N6-(L-1,3-dicarboxypropyl)-L-lysine + NAD+ + H2O
L-lysine + 2-oxoglutarate + NADH
-
i.e. saccharopine
-
r
N6-(L-1,3-dicarboxypropyl)-L-lysine + NAD+ + H2O
L-lysine + 2-oxoglutarate + NADH
-
involved in lysine biosynthesis
-
-
?
N6-(L-1,3-dicarboxypropyl)-L-lysine + NAD+ + H2O
L-lysine + 2-oxoglutarate + NADH
-
last step of alpha-aminoadipate pathway for lysine biosynthesis
-
-
?
N6-(L-1,3-dicarboxypropyl)-L-lysine + NAD+ + H2O
L-lysine + 2-oxoglutarate + NADH
-
involved in lysine biosynthesis
-
-
?
N6-(L-1,3-dicarboxypropyl)-L-lysine + NAD+ + H2O
L-lysine + 2-oxoglutarate + NADH
-
last step of alpha-aminoadipate pathway for lysine biosynthesis
-
-
?
N6-(L-1,3-dicarboxypropyl)-L-lysine + NAD+ + H2O
L-lysine + 2-oxoglutarate + NADH
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-
-
-
?
N6-(L-1,3-dicarboxypropyl)-L-lysine + NAD+ + H2O
L-lysine + 2-oxoglutarate + NADH
-
-
-
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r
N6-(L-1,3-dicarboxypropyl)-L-lysine + NAD+ + H2O
L-lysine + 2-oxoglutarate + NADH
-
last step of alpha-aminoadipate pathway for lysine biosynthesis
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-
?
N6-(L-1,3-dicarboxypropyl)-L-lysine + NAD+ + H2O
L-lysine + 2-oxoglutarate + NADH
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-
-
-
?
N6-(L-1,3-dicarboxypropyl)-L-lysine + NAD+ + H2O
L-lysine + 2-oxoglutarate + NADH
-
-
-
-
r
N6-(L-1,3-dicarboxypropyl)-L-lysine + NAD+ + H2O
L-lysine + 2-oxoglutarate + NADH
-
-
-
r
N6-(L-1,3-dicarboxypropyl)-L-lysine + NAD+ + H2O
L-lysine + 2-oxoglutarate + NADH
-
high specificity with respect to coenzyme and substrate
-
-
?
N6-(L-1,3-dicarboxypropyl)-L-lysine + NAD+ + H2O
L-lysine + 2-oxoglutarate + NADH
-
high specificity with respect to coenzyme and substrate
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r
N6-(L-1,3-dicarboxypropyl)-L-lysine + NAD+ + H2O
L-lysine + 2-oxoglutarate + NADH
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A-stereospecific in hydrogen transfer in the synthesis of saccharopine from alpha-ketoglutarate and L-lysine
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-
?
N6-(L-1,3-dicarboxypropyl)-L-lysine + NAD+ + H2O
L-lysine + 2-oxoglutarate + NADH
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i.e. saccharopine
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r
N6-(L-1,3-dicarboxypropyl)-L-lysine + NAD+ + H2O
L-lysine + 2-oxoglutarate + NADH
-
i.e. saccharopine
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r
N6-(L-1,3-dicarboxypropyl)-L-lysine + NAD+ + H2O
L-lysine + 2-oxoglutarate + NADH
-
involved in lysine biosynthesis
-
-
?
N6-(L-1,3-dicarboxypropyl)-L-lysine + NAD+ + H2O
L-lysine + 2-oxoglutarate + NADH
-
last step of alpha-aminoadipate pathway for lysine biosynthesis
-
-
?
N6-(L-1,3-dicarboxypropyl)-L-lysine + NAD+ + H2O
L-lysine + 2-oxoglutarate + NADH
-
last step of alpha-aminoadipate pathway for lysine biosynthesis
-
-
?
N6-(L-1,3-dicarboxypropyl)-L-lysine + NAD+ + H2O
L-lysine + 2-oxoglutarate + NADH + H+
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-
-
-
?
N6-(L-1,3-dicarboxypropyl)-L-lysine + NAD+ + H2O
L-lysine + 2-oxoglutarate + NADH + H+
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-
-
-
r
N6-(L-1,3-dicarboxypropyl)-L-lysine + NAD+ + H2O
L-lysine + 2-oxoglutarate + NADH + H+
-
-
-
?
N6-(L-1,3-dicarboxypropyl)-L-lysine + NAD+ + H2O
L-lysine + 2-oxoglutarate + NADH + H+
-
the enzyme is specific for L-lysine
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-
r
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NATURAL SUBSTRATE
NATURAL 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
L-lysine + 2-oxoglutarate + NADH
N6-(L-1,3-dicarboxypropyl)-L-lysine + NAD+ + H2O
-
-
-
r
L-lysine + 2-oxoglutarate + NADH + H+
N6-(L-1,3-dicarboxypropyl)-L-lysine + NAD+ + H2O
-
-
-
-
r
N6-(L-1,3-dicarboxypropyl)-L-lysine + NAD+ + H2O
L-lysine + 2-oxoglutarate + NADH + H+
-
-
-
-
r
N6-(L-1,3-dicarboxypropyl)-L-lysine + NAD+ + H2O
L-lysine + 2-oxoglutarate + NADH
-
involved in lysine biosynthesis
-
-
?
N6-(L-1,3-dicarboxypropyl)-L-lysine + NAD+ + H2O
L-lysine + 2-oxoglutarate + NADH
-
last step of alpha-aminoadipate pathway for lysine biosynthesis
-
-
?
N6-(L-1,3-dicarboxypropyl)-L-lysine + NAD+ + H2O
L-lysine + 2-oxoglutarate + NADH
-
involved in lysine biosynthesis
-
-
?
N6-(L-1,3-dicarboxypropyl)-L-lysine + NAD+ + H2O
L-lysine + 2-oxoglutarate + NADH
-
last step of alpha-aminoadipate pathway for lysine biosynthesis
-
-
?
N6-(L-1,3-dicarboxypropyl)-L-lysine + NAD+ + H2O
L-lysine + 2-oxoglutarate + NADH
-
involved in lysine biosynthesis
-
-
?
N6-(L-1,3-dicarboxypropyl)-L-lysine + NAD+ + H2O
L-lysine + 2-oxoglutarate + NADH
-
last step of alpha-aminoadipate pathway for lysine biosynthesis
-
-
?
N6-(L-1,3-dicarboxypropyl)-L-lysine + NAD+ + H2O
L-lysine + 2-oxoglutarate + NADH
-
last step of alpha-aminoadipate pathway for lysine biosynthesis
-
-
?
N6-(L-1,3-dicarboxypropyl)-L-lysine + NAD+ + H2O
L-lysine + 2-oxoglutarate + NADH
-
-
-
-
?
N6-(L-1,3-dicarboxypropyl)-L-lysine + NAD+ + H2O
L-lysine + 2-oxoglutarate + NADH
-
-
-
-
r
N6-(L-1,3-dicarboxypropyl)-L-lysine + NAD+ + H2O
L-lysine + 2-oxoglutarate + NADH
-
involved in lysine biosynthesis
-
-
?
N6-(L-1,3-dicarboxypropyl)-L-lysine + NAD+ + H2O
L-lysine + 2-oxoglutarate + NADH
-
last step of alpha-aminoadipate pathway for lysine biosynthesis
-
-
?
N6-(L-1,3-dicarboxypropyl)-L-lysine + NAD+ + H2O
L-lysine + 2-oxoglutarate + NADH
-
last step of alpha-aminoadipate pathway for lysine biosynthesis
-
-
?
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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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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
NADP+
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NADP+ is competitive versus NADPH when NADPH serves as the coenzyme
alpha-ketoglutarate
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substrate inhibition, uncompetitive versus NADH
amino acids
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hydrophobic amino acids with 5 or 6 carbon atoms; hydroxylic amino acids
amino acids
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hydrophobic amino acids with 5 or 6 carbon atoms; not: dicarboxylic amino acids, aspartate, glutamate, 2-aminoadipate
L-leucine
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L-leucine is a competitive inhibitor against L-lysine at pH 6.5-12.5
L-leucine
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dead-end inhibition by L-leucine is uncompetitive versus NADPH
oxalylglycine
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at pH 5.45 and 9.58, oxalylglycine is competitive versus 2-oxoglutarate
oxalylglycine
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competitive against lysine with mutant E78A, noncompetitive with mutants E78Q, E122Q, E78Q/E122Q, E122A, E78A/E122A
p-hydroxymercuribenzoate
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inhibition counteracted by 2-mercaptoethanol or glutathione
additional information
-
no substrate inhibition by NADH, NAD+ and saccharopine
-
additional information
-
detailed analysis of inhibition patterns for product and dead end inhibitors
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
-
detailed kinetic analysis including pH-dependance and deuterium kinetic effects
-
0.11
2-oxoglutarate
wild type enzyme, in 100 mM HEPES, pH 7.0, at 25°C
9
2-oxoglutarate
mutant enzyme H96Q, in 100 mM HEPES, pH 7.0, at 25°C
10
2-oxoglutarate
mutant enzyme K77M, in 100 mM HEPES, pH 7.0, at 25°C
267
2-oxoglutarate
mutant enzyme K77M/H96Q, in 100 mM HEPES, pH 7.0, at 25°C
0.89
L-lysine
wild type enzyme, in 100 mM HEPES, pH 7.0, at 25°C
25
L-lysine
mutant enzyme K77M, in 100 mM HEPES, pH 7.0, at 25°C
96
L-lysine
mutant enzyme K77M/H96Q, in 100 mM HEPES, pH 7.0, at 25°C
267
L-lysine
mutant enzyme H96Q, in 100 mM HEPES, pH 7.0, at 25°C
0.2
N6-(L-1,3-dicarboxypropyl)-L-lysine
-
mutant enzyme C205S, at pH 7.0 and 25°C
1.4
N6-(L-1,3-dicarboxypropyl)-L-lysine
-
mutant enzyme C205V, at pH 7.0 and 25°C
6.7
N6-(L-1,3-dicarboxypropyl)-L-lysine
-
wild type enzyme, at pH 7.0 and 25°C
14
N6-(L-1,3-dicarboxypropyl)-L-lysine
-
mutant E122Q, 25°C, pH 7.2
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
-
inhibition studies with substrates analogues
-
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.09
additional information
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5.2 - 9
-
half-maximal activities at pH 5.2 and 9.0, L-lysine + 2-oxoglutarate + NADH
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
metabolism
-
saccharopine dehydrogenase is the last enzyme in the alpha-aminoadipate pathway of L-lysine biosynthesis
Show AA Sequence and Transmembrane Helices (3626 entries)
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Please use the AA Sequence and Transmembrane Helices Search for a specific query.
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
38000 - 40000
-
gel filtration, sedimentation equilibrium centrifugation, SDS-PAGE
45000
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
in complex with NAD+ and saccharopine, hanging drop vapour diffusion method in 20% (w/v) PEG 8000, 0.1 M MES (pH 6.0), and 0.2 M Ca(OAc)2
mutant enzyme C205S, hanging drop vapor diffusion method, using 100 mM Tris (pH 7.0), 30% (w/v) PEG-MME 2000 at 4°C
the apo-enzyme is obtained using the hanging drop vapour diffusion method with 100 mM Tris (pH 7.0) and 22% (w/v) PEG 8000, sulfate-, AMP-, and oxalylglycine-bound enzyme crystals are obtained by the hanging drop vapour diffusion method with 26% (w/v) PEG-MME 2000 in 100 mM Tris (pH 7.0) containing 200 mM (NH4)2SO4, or with 24% (w/v) PEG-MME 2000 in 100 mM Bis-Tris, pH 6.5, or with 24% (w/v) PEG-MME 2000 in 100 mM Tris, pH 8.0, at 4°C, respectively
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
C205S
-
the Km for N6-(L-1,3-dicarboxypropyl)-L-lysine decreases by more than 30fold for the C205S mutant
C205V
-
the Km for N6-(L-1,3-dicarboxypropyl)-L-lysine decreases by 5fold for the C205V mutant
E122A
-
mutation increases the positive charge of the active site and affects the pKa value of the catalytic group. Kinetic mechanism similar to wild-type
E122Q
-
mutation increases the positive charge of the active site and affects the pKa value of the catalytic group. Kinetic mechanism similar to wild-type
E16Q/C205S
-
the mutation decreases the turnover number by about 15fold
E78A
-
mutation increases the positive charge of the active site and affects the pKa value of the catalytic group. Kinetic mechanism differs from wild-type, 2-oxoglutarate binds to enzyme and enzyme-NADH
E78A/E122A
-
mutation increases the positive charge of the active site and affects the pKa value of the catalytic group. Kinetic mechanism similar to wild-type
E78Q
-
mutation increases the positive charge of the active site and affects the pKa value of the catalytic group. Kinetic mechanism similar to wild-type
E78Q/E122Q
-
mutation increases the positive charge of the active site and affects the pKa value of the catalytic group. Kinetic mechanism similar to wild-type
H96Q
the mutation results in 100 and more than 1000fold increases in Km values for L-lysine and 2-oxoglutarate, respectively
K13M/C205S
-
the mutation decreases the turnover number by about 15fold
K77M
the mutation results in 28 and 90fold increases in Km values for L-lysine and 2-oxoglutarate, respectively
K77M/H96Q
the mutations result in 300 and 80fold increases in Km values for L-lysine and 2-oxoglutarate, respectively
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, protein concentration above 0.1 mg/ml, pH 6.8, 1 mM EDTA, several months
-
4°C, His-tagged mutant enzymes in 100 mM HEPES, 300 mM KCl and 300 mM imidazole at pH 8.0, several months, the mutant enzymes maintain stability and remain active
-
4°C, mutant enzymes in 100 mM HEPES, 300 mM KCl, and 300 mM imidazole at pH 8.0, several months, no loss of activity
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21 (DE3)-RIL cells
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
Schmidt, H.; Bode, R.; Lindner, M.; Birnbaum, D.
Lysine biosynthesis in the yeast Candida maltosa: properties of some enzymes and regulation of the biosynthetic pathway
J. Basic Microbiol.
25
675-681
1985
Candida maltosa, Candida maltosa L4
-
brenda
Naranjo, L.; Martin de Valmaseda, E.; Banuelos, O.; Lopez, P.; Riano, J.; Casqueiro, J.; Martin, J.F.
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
brenda
Schmidt, H.; Bode, R.; Birnbaum, D.
Regulation of the lysine biosynthesis in Pichia guilliermondii
Antonie van Leeuwenhoek
56
337-347
1989
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