1.5.1.7: saccharopine dehydrogenase (NAD+, L-lysine-forming)
This is an abbreviated version!
For detailed information about saccharopine dehydrogenase (NAD+, L-lysine-forming), go to the full flat file.
Reaction
Synonyms
dehydrogenase, saccharopine (nicotinamide adenine dinucleotide, lysine forming), epsilon-N-(L-glutaryl-2)-L-lysine:NAD oxidoreductase (L-lysine forming), Fvsdh, LYS1, Lys1p, 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), N6-(glutaryl-2)-L-lysine:nicotinamide adenine dinucleotide (NAD+) oxidoreductase (L-lysine-forming), NAD+-linked saccharopine dehydrogenase, saccharopine dehydrogenase, saccharopine dehydrogenase (L-lysine-forming), SDH
ECTree
1.5.1.7 saccharopine dehydrogenase (NAD+, L-lysine-forming)Advanced search results
results (
results (Engineering
Engineering on EC 1.5.1.7 - saccharopine dehydrogenase (NAD+, L-lysine-forming)
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PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
C205S
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the Km for N6-(L-1,3-dicarboxypropyl)-L-lysine decreases by more than 30fold for the C205S mutant
C205V
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the Km for N6-(L-1,3-dicarboxypropyl)-L-lysine decreases by 5fold for the C205V mutant
E122A
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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
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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
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the mutation decreases the turnover number by about 15fold
E78A
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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
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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
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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
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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
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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
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
Flammulina velutipes Dan3
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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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