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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
-
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+
-
-
-
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 + 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+
-
-
-
?
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
N6-(L-1,3-dicarboxypropyl)-L-lysine + NAD+ + H2O
L-lysine + 2-oxoglutarate + NADH + H+
-
-
-
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+
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
-
-
?
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+
-
-
-
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 + H+
-
-
-
r
N6-(L-1,3-dicarboxypropyl)-L-lysine + NAD+ + H2O
L-lysine + 2-oxoglutarate + NADH + H+
-
-
-
r
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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 enzyme, at pH 7.0 and 25°C
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
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 enzyme, at pH 7.0 and 25°C
1.1
L-lysine
-
wild-type, 25°C, pH 7.2
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 enzyme, at pH 7.0 and 25°C
6.7
N6-(L-1,3-dicarboxypropyl)-L-lysine
-
wild-type, 25°C, pH 7.2
14
N6-(L-1,3-dicarboxypropyl)-L-lysine
-
mutant E122Q, 25°C, pH 7.2
0.1
NAD+
-
-
0.9
NAD+
-
wild type enzyme, at pH 7.0 and 25°C
0.9
NAD+
-
wild-type, 25°C, pH 7.2
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 enzyme, at pH 7.0 and 25°C
0.019
NADH
-
wild-type, 25°C, pH 7.2
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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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
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
-
saccharopine dehydrogenase is the last enzyme in the alpha-aminoadipate pathway of L-lysine biosynthesis
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+
metabolism
saccharopine dehydrogenase regulates the last step of fungal lysine biosynthesis
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+
-
metabolism
-
saccharopine dehydrogenase regulates the last step of fungal lysine biosynthesis
-
physiological function
saccharopine dehydrogenase, encoded by the LYS1 gene, requires NAD+ for the production of lysine. Intraperoxisomal NAD+ is required for saccharopine dehydrogenase activity
physiological function
-
saccharopine dehydrogenase, encoded by the LYS1 gene, requires NAD+ for the production of lysine. Intraperoxisomal NAD+ is required for saccharopine dehydrogenase activity
-
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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
additional information
enzyme overexpression from endogenous gene Fvsdh resulting in 1.1-3.0fold increased enzyme content in randomly selected transgenic strains, lysine contents are also increased from 1.12 to 1.3fold in these five transformants, except for strain T3, in which the lysine contents are the same as the control. Effects on other genes in SDH overexpressing cells: expression of the two genes, AAT and AAR, is increased in all five transformants compared with that in the wild-type. The expression of the HCS gene is increased in four transformants except for T5. The expression of the HAH gene is increased in T1, T3, and T5 but decreased in T2 and is almost the same as that of the wild-type in T4. The expression of the HIDH gene is increased in four transformants except for T4. The expression of the SDR gene is increased in four transformants except for T5, overview
additional information
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enzyme overexpression from endogenous gene Fvsdh resulting in 1.1-3.0fold increased enzyme content in randomly selected transgenic strains, lysine contents are also increased from 1.12 to 1.3fold in these five transformants, except for strain T3, in which the lysine contents are the same as the control. Effects on other genes in SDH overexpressing cells: expression of the two genes, AAT and AAR, is increased in all five transformants compared with that in the wild-type. The expression of the HCS gene is increased in four transformants except for T5. The expression of the HAH gene is increased in T1, T3, and T5 but decreased in T2 and is almost the same as that of the wild-type in T4. The expression of the HIDH gene is increased in four transformants except for T4. The expression of the SDR gene is increased in four transformants except for T5, overview
additional information
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enzyme overexpression from endogenous gene Fvsdh resulting in 1.1-3.0fold increased enzyme content in randomly selected transgenic strains, lysine contents are also increased from 1.12 to 1.3fold in these five transformants, except for strain T3, in which the lysine contents are the same as the control. Effects on other genes in SDH overexpressing cells: expression of the two genes, AAT and AAR, is increased in all five transformants compared with that in the wild-type. The expression of the HCS gene is increased in four transformants except for T5. The expression of the HAH gene is increased in T1, T3, and T5 but decreased in T2 and is almost the same as that of the wild-type in T4. The expression of the HIDH gene is increased in four transformants except for T4. The expression of the SDR gene is increased in four transformants except for T5, overview
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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
additional information
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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
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