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Information on EC 1.5.1.7 - saccharopine dehydrogenase (NAD+, L-lysine-forming) and Organism(s) Saccharomyces cerevisiae and UniProt Accession P38998
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1.5.1.7 saccharopine dehydrogenase (NAD+, L-lysine-forming)Specify your search results
The taxonomic range for the selected organisms is: Saccharomyces cerevisiae
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Reaction Schemes
Synonyms
fvsdh, saccharopine dehydrogenase (l-lysine-forming), 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
N6-(glutaryl-2)-L-lysine:nicotinamide adenine dinucleotide (NAD+) oxidoreductase (L-lysine-forming)
-
dehydrogenase, saccharopine (nicotinamide adenine dinucleotide, lysine forming)
-
-
-
-
epsilon-N-(L-glutaryl-2)-L-lysine:NAD oxidoreductase (L-lysine forming)
-
-
-
-
Lysine--2-oxoglutarate reductase
-
-
-
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lysine-2-oxoglutarate reductase
-
-
-
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N6-(glutar-2-yl)-L-lysine:NAD oxidoreductase (L-lysine-forming)
-
-
-
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N6-(glutaryl-2)-L-lysine:NAD oxidoreductase (L-lysine forming)
-
-
saccharopine dehydrogenase
-
catalyzes the final step in the alpha-aminoadipate pathway for lysine biosynthesis
SDH
SDH
-
-
-
-
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
-
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
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
redox reaction
-
-
-
-
oxidation
-
-
-
-
reduction
-
-
-
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reductive condensation
PATHWAY SOURCE
PATHWAYS
BRENDA
-
-
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
L-lysine + 2-oxoglutarate + NADH
N6-(L-1,3-dicarboxypropyl)-L-lysine + NAD+ + H2O
-
-
-
r
N6-(L-1,3-dicarboxypropyl)-L-lysine + NAD+ + H2O
L-lysine + 2-oxoglutarate + NADH
-
-
-
r
L-lysine + 2-oxoglutarate + NADH
N6-(L-1,3-dicarboxypropyl)-L-lysine + NAD+ + H2O
-
-
-
-
?
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
-
-
?
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+
-
-
-
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
-
-
-
-
?
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
-
r
N6-(L-1,3-dicarboxypropyl)-L-lysine + NAD+ + H2O
L-lysine + 2-oxoglutarate + NADH
-
A-stereospecific in hydrogen transfer in the synthesis of saccharopine from alpha-ketoglutarate and L-lysine
-
-
?
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
-
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 + H+
-
-
-
-
?
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 + H+
-
the enzyme is specific for L-lysine
-
-
r
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
N6-(L-1,3-dicarboxypropyl)-L-lysine + NAD+ + H2O
L-lysine + 2-oxoglutarate + NADH + H+
-
-
-
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
-
-
-
-
?
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
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
NADP+
-
NADP+ is competitive versus NADPH when NADPH serves as the coenzyme
alpha-ketoglutarate
-
substrate inhibition, uncompetitive versus NADH
amino acids
-
not: dicarboxylic amino acids, aspartate, glutamate, 2-aminoadipate
L-leucine
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dead-end inhibition by L-leucine is uncompetitive versus NADPH
L-leucine
-
L-leucine is a competitive inhibitor against L-lysine at pH 6.5-12.5
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
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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
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5.2 - 9
-
half-maximal activities at pH 5.2 and 9.0, L-lysine + 2-oxoglutarate + NADH
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
peroxisomal matrix, the enzyme has a peroxisomal targeting signal type 1 (PTS1)
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
single mutants in MDH3 or GPD1 grow on lysine-deficient medium, but an mdh3/gpd1DELTA double mutant accumulates saccharopine and displays lysine bradytrophy. Lysine biosynthesis is restored when saccharopine dehydrogenase is mislocalised to the cytosol in mdh3/gpd1DELTA cells. A decrease of saccharopine dehydrogenase activity (Lys1p-activity) causes lysine bradytrophy in mdh3/gpd1DELTA cells
metabolism
in Saccharomyces cerevisiae, the ultimate step in lysine biosynthesis, the NAD+-dependent dehydrogenation of saccharopine to lysine, is a NAD+-dependent reaction performed inside peroxisomes. The availability of intraperoxisomal NAD+ required for saccharopine dehydrogenase activity can be sustained by both shuttles, the malate/oxaloacetate shuttle and a glycerol-3-phosphate dehydrogenase 1(Gpd1p)-dependent shuttle. The shuttles both are able to maintain the intraperoxisomal redox balance. The extent to which each of these shuttles contributes to the intraperoxisomal redox balance may depend on the growth medium. The presence of multiple peroxisomal redox shuttles allows eukaryotic cells to maintain the peroxisomal redox status under different metabolic conditions. During growth on glucose medium, saccharopine dehydrogenase (Lys1p) is the only lysine biosynthetic enzyme that is dependent on the availability of intraperoxisomal NAD+
physiological function
saccharopine dehydrogenase, encoded by the LYS1 gene, requires NAD+ for the production of lysine. Intraperoxisomal NAD+ is required for saccharopine dehydrogenase activity
metabolism
-
saccharopine dehydrogenase is the last enzyme in the alpha-aminoadipate pathway of L-lysine biosynthesis
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
38000 - 40000
-
gel filtration, sedimentation equilibrium centrifugation, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
H96Q
the mutation results in 100 and more than 1000fold increases in Km values for L-lysine and 2-oxoglutarate, respectively
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
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
K13M/C205S
-
the mutation decreases the turnover number by about 15fold
additional information
generation of a mdh3/gpd1DELTA double mutant that accumulates saccharopine and displays lysine bradytrophy. Lysine biosynthesis is restored when saccharopine dehydrogenase is mislocalised to the cytosol in mdh3/gpd1DELTA cells. Recombinantly expressed GFP-tagged Lys1p colocalizes with the peroxisomal marker HcRed-PTS1 in glucose-grown cells. A disruption of the peroxisomal NAD+/NADH ratio as a consequence of a block in the redox shuttles leads to an increase in the Lys1p substrate/product ratio. The saccharopine/lysine ratio increases in mdh3/gpd1DELTA cells by more than 80fold. When Lys1p is mislocalised to the cytosol in mdh3/gpd1DELTA cells, the cytosolic pool of NAD+ supports Lys1p activity and lysine biosynthesis is restored. A decrease of saccharopine dehydrogenase activity (Lys1p-activity) causes lysine bradytrophy in mdh3/gpd1DELTA cells
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
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
-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
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene LYS1, recombinant expression of GFP-tagged Lys1p in glucose-grown cells, it colocalizes with the peroxisomal marker HcRed-PTS1, recombinant expression of the enzyme in mdh3/gpd1DELTA cells and mislocation to the cytosol
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Saunders, P.P.; Broquist, H.P.
Saccharopine, an intermediate of the aminoadipic acid pathway of lysine biosynthesis. IV. Saccharopine dehydrogenase
J. Biol. Chem.
241
3435-3440
1966
Saccharomyces cerevisiae
Fujioka, M.
Chemical mechanism of saccharopine dehydrogenase (NAD+, L-lysine-forming) as deduced from initial rate pH studies
Arch. Biochem. Biophys.
230
553-559
1984
Saccharomyces cerevisiae
Fujioka, M.
Active-site residues of saccharopine dehydrogenase (NAD+, lysine-forming) from bakers yeast
Biochem. Soc. Trans.
9
281-282
1981
Saccharomyces cerevisiae
Fujioka, M.; Takata, Y.
Role of arginine residue in saccharopine dehydrogenase (L-lysine forming) from bakers yeast
Biochemistry
20
468-472
1981
Saccharomyces cerevisiae
Ogawa, H.; Fujioka, M.
The reaction of pyridoxal 5-phosphate with an essential lysine residue of saccharopine dehydrogenase (L-lysine-forming)
J. Biol. Chem.
255
7420-7425
1980
Saccharomyces cerevisiae
Fujioka, M.; Takata, Y.; Ogawa, H.; Okamoto, M.
The inactivation of saccharopine dehydrogenase (L-lysine-forming) by diethyl pyrocarbonate
J. Biol. Chem.
255
937-942
1980
Saccharomyces cerevisiae
Fujioka, M.; Takata, Y.
Stereospecificity of hydrogen transfer in the saccharopine dehydrogenase reaction
Biochim. Biophys. Acta
570
210-212
1979
Saccharomyces cerevisiae
Ogawa, H.; Okamoto, M.; Fujioka, M.
Chemical modification of the active site sulfhydryl group of saccharopine dehydrogenase (L-lysine-forming)
J. Biol. Chem.
254
7030-7035
1979
Saccharomyces cerevisiae
Sugimoto, K.; Fujioka, M.
The reaction of pyruvate with saccharopine dehydrogenase
Eur. J. Biochem.
90
301-307
1978
Saccharomyces cerevisiae
Ogawa, H.; Fujioka, M.
Purification and characterization of saccharopine dehydrogenase from bakers yeast
J. Biol. Chem.
253
3666-3670
1978
Saccharomyces cerevisiae
Fujioka, M.
Saccharopine dehydrogenase. Substrate inhibition studies
J. Biol. Chem.
250
8986-8989
1975
Saccharomyces cerevisiae
Fujioka, M.; Nakatani, Y.
Saccharopine dehydrogenase. A kinetic study of coenzyme binding
J. Biol. Chem.
249
6886-6891
1974
Saccharomyces cerevisiae
Fujioka, M.; Nakatani, Y.
Saccharopine dehydrogenase. Interaction with substrate analogues
Eur. J. Biochem.
25
301-307
1972
Saccharomyces cerevisiae
Fujioka, M.; Nakatani, Y.
A kinetic study of saccharopine dehydrogenase reaction
Eur. J. Biochem.
16
180-186
1970
Saccharomyces cerevisiae
Broquist, H.P.
Saccharopine dehydrogenase
Methods Enzymol.
17B
124-129
1971
Saccharomyces cerevisiae
-
Xu, H.; West, A.H.; Cook, P.F.
Overall kinetic mechanism of saccharopine dehydrogenase from Saccharomyces cerevisiae
Biochemistry
45
12156-12166
2006
Saccharomyces cerevisiae
Xu, H.; Alguindigue, S.S.; West, A.H.; Cook, P.F.
A proposed proton shuttle mechanism for saccharopine dehydrogenase from Saccharomyces cerevisiae
Biochemistry
46
871-882
2007
Saccharomyces cerevisiae
Andi, B.; Xu, H.; Cook, P.F.; West, A.H.
Crystal structures of ligand-bound saccharopine dehydrogenase from Saccharomyces cerevisiae
Biochemistry
46
12512-12521
2007
Saccharomyces cerevisiae (P38998)
Xu, H.; West, A.H.; Cook, P.F.
Determinants of substrate specificity for saccharopine dehydrogenase from Saccharomyces cerevisiae
Biochemistry
46
7625-7636
2007
Saccharomyces cerevisiae
Burk, D.L.; Hwang, J.; Kwok, E.; Marrone, L.; Goodfellow, V.; Dmitrienko, G.I.; Berghuis, A.M.
Structural studies of the final enzyme in the alpha-aminoadipate pathway-saccharopine dehydrogenase from Saccharomyces cerevisiae
J. Mol. Biol.
373
745-754
2007
Saccharomyces cerevisiae (P38998)
Ekanayake, D.K.; Andi, B.; Bobyk, K.D.; West, A.H.; Cook, P.F.
Glutamates 78 and 122 in the active site of saccharopine dehydrogenase contribute to reactant binding and modulate the basicity of the acid-base catalysts
J. Biol. Chem.
285
20756-20768
2010
Saccharomyces cerevisiae
Bobyk, K.D.; Kim, S.G.; Kumar, V.P.; Kim, S.K.; West, A.H.; Cook, P.F.
The oxidation state of active site thiols determines activity of saccharopine dehydrogenase at low pH
Arch. Biochem. Biophys.
513
71-80
2011
Saccharomyces cerevisiae
Kumar, V.P.; West, A.H.; Cook, P.F.
Supporting role of lysine 13 and glutamate 16 in the acid-base mechanism of saccharopine dehydrogenase from Saccharomyces cerevisiae
Arch. Biochem. Biophys.
522
57-61
2012
Saccharomyces cerevisiae
Kumar, V.P.; Thomas, L.M.; Bobyk, K.D.; Andi, B.; Cook, P.F.; West, A.H.
Evidence in support of lysine 77 and histidine 96 as acid-base catalytic residues in saccharopine dehydrogenase from Saccharomyces cerevisiae
Biochemistry
51
857-866
2012
Saccharomyces cerevisiae (P38998)
Sheng, X.; Gao, J.; Liu, Y.; Liu, C.
Theoretical study on the proton shuttle mechanism of saccharopine dehydrogenase
J. Mol. Graph. Model.
44
17-25
2013
Saccharomyces cerevisiae
Al-Saryi, N.; Al-Hejjaj, M.; Van Roermund, C.; Hulmes, G.; Ekal, L.; Payton, C.; Wanders, R.; Hettema, E.
Two NAD-linked redox shuttles maintain the peroxisomal redox balance in Saccharomyces cerevisiae
Sci. Rep.
7
11868
2017
Saccharomyces cerevisiae (P38998), Saccharomyces cerevisiae ATCC 204508 (P38998)
EXTERNAL LINKS (specific for EC-Number 1.5.1.7)
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