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L-lysine + 2-oxoglutarate + NADH
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 + alpha-ketoadipate + NADH
?
-
-
-
-
?
L-lysine + alpha-ketobutyrate + NADH
?
-
-
-
-
?
L-lysine + alpha-ketomalonate + NADH
?
-
-
-
-
?
L-lysine + alpha-ketovalerate + NADH
?
-
-
-
-
?
L-lysine + glyoxylate + NADH
?
-
-
-
-
?
L-lysine + pyruvate + NADH
?
-
-
-
-
?
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 + H+
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
-
-
-
-
?
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
-
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
-
-
-
-
-
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
-
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
-
-
-
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
-
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
-
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
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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
-
-
-
-
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 + 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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0.11 - 267
2-oxoglutarate
5.3
alpha-ketoadipate
-
at pH 7.0
153
alpha-Ketobutyrate
-
at pH 7.0
24
alpha-ketomalonate
-
at pH 7.0
94
alpha-ketovalerate
-
at pH 7.0
6.4
glyoxylate
-
at pH 7.0
0.2 - 14
N6-(L-1,3-dicarboxypropyl)-L-lysine
additional information
additional information
-
detailed kinetic analysis including pH-dependance and deuterium kinetic effects
-
0.11
2-oxoglutarate

-
at pH 7.0
0.11
2-oxoglutarate
-
wild-type, 25°C, pH 7.2
0.11
2-oxoglutarate
-
mutant enzyme C205S, at pH 7.0 and 25°C; wild type enzyme, at pH 7.0 and 25°C
0.11
2-oxoglutarate
-
wild type enzyme, in 100 mM HEPES, pH 7.0, at 25°C
0.18
2-oxoglutarate
-
mutant E78A, 25°C, pH 7.2
0.23
2-oxoglutarate
-
mutant E78Q, 25°C, pH 7.2
0.3
2-oxoglutarate
-
mutant E122Q, 25°C, pH 7.2
0.38
2-oxoglutarate
-
mutant enzyme C205V, at pH 7.0 and 25°C
0.55
2-oxoglutarate
-
mutant E122A, 25°C, pH 7.2
2
2-oxoglutarate
-
mutant E78Q/E122Q, 25°C, pH 7.2
4.8 - 5
2-oxoglutarate
-
mutant E78A/E122A, 25°C, pH 7.2
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
0.62
L-lysine

-
mutant E78A, 25°C, pH 7.2
0.89
L-lysine
-
mutant enzyme C205S, at pH 7.0 and 25°C
0.89
L-lysine
-
wild type enzyme, in 100 mM HEPES, pH 7.0, at 25°C
1.1
L-lysine
-
25°C, pH 7.0
1.1
L-lysine
-
wild-type, 25°C, pH 7.2
1.1
L-lysine
-
wild type enzyme, at pH 7.0 and 25°C
3
L-lysine
-
mutant enzyme C205V, at pH 7.0 and 25°C
4
L-lysine
-
mutant E78Q, 25°C, pH 7.2
11
L-lysine
-
mutant E122Q, 25°C, pH 7.2
25
L-lysine
-
mutant enzyme K77M, in 100 mM HEPES, pH 7.0, at 25°C
27.1
L-lysine
-
mutant E78Q/E122Q, 25°C, pH 7.2
36.5
L-lysine
-
mutant E122A, 25°C, pH 7.2
96
L-lysine
-
mutant enzyme K77M/H96Q, in 100 mM HEPES, pH 7.0, at 25°C
190.7
L-lysine
-
mutant E78A/E122A, 25°C, pH 7.2
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
2
N6-(L-1,3-dicarboxypropyl)-L-lysine
-
mutant E78Q, 25°C, pH 7.2
6.7
N6-(L-1,3-dicarboxypropyl)-L-lysine
-
25°C, pH 7.0
6.7
N6-(L-1,3-dicarboxypropyl)-L-lysine
-
wild-type, 25°C, pH 7.2
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
0.1
NAD+

-
-
0.9
NAD+
-
wild-type, 25°C, pH 7.2
0.9
NAD+
-
wild type enzyme, at pH 7.0 and 25°C
1.1
NAD+
-
mutant E78Q, 25°C, pH 7.2
1.2
NAD+
-
mutant enzyme C205V, at pH 7.0 and 25°C
1.8
NAD+
-
mutant enzyme C205S, at pH 7.0 and 25°C
3.3
NAD+
-
mutant E122Q, 25°C, pH 7.2
0.01
NADH

-
mutant enzyme C205S, at pH 7.0 and 25°C
0.014
NADH
-
mutant E78Q, 25°C, pH 7.2
0.019
NADH
-
25°C, pH 7.0
0.019
NADH
-
wild-type, 25°C, pH 7.2
0.019
NADH
-
wild type enzyme, at pH 7.0 and 25°C
0.025
NADH
-
mutant E122Q, 25°C, pH 7.2
0.036
NADH
-
mutant E78A, 25°C, pH 7.2
0.05
NADH
-
mutant enzyme C205V, at pH 7.0 and 25°C
0.062
NADH
-
mutant E122A, 25°C, pH 7.2
0.12
NADH
-
mutant E78Q/E122Q, 25°C, pH 7.2
0.133
NADH
-
mutant E78A/E122A, 25°C, pH 7.2
0.23
NADH
-
2-oxoglutarate
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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
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
Meyerozyma guilliermondii, Meyerozyma guilliermondii H17
brenda
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
brenda
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
brenda
Fujioka, M.
Active-site residues of saccharopine dehydrogenase (NAD+, lysine-forming) from bakers yeast
Biochem. Soc. Trans.
9
281-282
1981
Saccharomyces cerevisiae
brenda
Fujioka, M.; Takata, Y.
Role of arginine residue in saccharopine dehydrogenase (L-lysine forming) from bakers yeast
Biochemistry
20
468-472
1981
Saccharomyces cerevisiae
brenda
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
brenda
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
brenda
Fujioka, M.; Takata, Y.
Stereospecificity of hydrogen transfer in the saccharopine dehydrogenase reaction
Biochim. Biophys. Acta
570
210-212
1979
Saccharomyces cerevisiae
brenda
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
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Hanke, R.; Hilgenberg, W.
Charakterisierung der Saccharopin-Dehydrogenase aus Phycomyces blakesleeanus
Z. Pflanzenphysiol.
92
23-31
1979
Phycomyces blakesleeanus
-
brenda
Sugimoto, K.; Fujioka, M.
The reaction of pyruvate with saccharopine dehydrogenase
Eur. J. Biochem.
90
301-307
1978
Saccharomyces cerevisiae
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Ogawa, H.; Fujioka, M.
Purification and characterization of saccharopine dehydrogenase from bakers yeast
J. Biol. Chem.
253
3666-3670
1978
Saccharomyces cerevisiae
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Fujioka, M.
Saccharopine dehydrogenase. Substrate inhibition studies
J. Biol. Chem.
250
8986-8989
1975
Saccharomyces cerevisiae
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Fujioka, M.; Nakatani, Y.
Saccharopine dehydrogenase. A kinetic study of coenzyme binding
J. Biol. Chem.
249
6886-6891
1974
Saccharomyces cerevisiae
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Fujioka, M.; Nakatani, Y.
Saccharopine dehydrogenase. Interaction with substrate analogues
Eur. J. Biochem.
25
301-307
1972
Saccharomyces cerevisiae
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Fujioka, M.; Nakatani, Y.
A kinetic study of saccharopine dehydrogenase reaction
Eur. J. Biochem.
16
180-186
1970
Saccharomyces cerevisiae
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Broquist, H.P.
Saccharopine dehydrogenase
Methods Enzymol.
17B
124-129
1971
Saccharomyces cerevisiae
-
brenda
Xu, H.; West, A.H.; Cook, P.F.
Overall kinetic mechanism of saccharopine dehydrogenase from Saccharomyces cerevisiae
Biochemistry
45
12156-12166
2006
Saccharomyces cerevisiae
brenda
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
brenda
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)
brenda
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
brenda
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)
brenda
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
brenda
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
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