Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
aminoadipate semialdehyde-glutamate reductase
-
-
-
-
aminoadipic semialdehyde-glutamate reductase
-
-
-
-
aminoadipic semialdehyde-glutamic reductase
-
-
-
-
dehydrogenase, saccharopine (nicotinamide adenine dinucleotide phosphate, glutamate-forming)
-
-
-
-
epsilon-N-(L-glutaryl-2)-L-lysine:NAD+(P) oxidoreductase (L-2-aminoadipate-semialdehyde forming)
-
-
-
-
lysine-ketoglutarate reductase/saccharopine dehydrogenase
saccharopine dehydrogenase
saccharopine dehydrogenase (L-glutamate forming)
-
-
spermidine synthase-saccharopine dehydrogenase
LKR/SDH
-
lysine-ketoglutarate reductase/saccharopine dehydrogenase
-
lysine-ketoglutarate reductase/saccharopine dehydrogenase
-
lysine-ketoglutarate reductase/saccharopine dehydrogenase
-
lysine-ketoglutarate reductase/saccharopine dehydrogenase
-
lysine-ketoglutarate reductase/saccharopine dehydrogenase
A0A3L6FCN0
-
nSpe-Sdh
-
nSpe-Sdh
Agaricus bisporus Sylvan A15
-
-
saccharopine dehydrogenase
-
saccharopine dehydrogenase
Agaricus bisporus Sylvan A15
-
-
saccharopine dehydrogenase
-
saccharopine dehydrogenase
-
saccharopine dehydrogenase
-
saccharopine dehydrogenase
-
saccharopine dehydrogenase
-
-
saccharopine dehydrogenase
A0A3L6FCN0
-
saccharopine reductase
-
-
-
-
saccharopine reductase
-
-
saccharopine reductase
-
-
SDH
-
SDH
Agaricus bisporus Sylvan A15
-
-
spermidine synthase-saccharopine dehydrogenase
-
spermidine synthase-saccharopine dehydrogenase
Agaricus bisporus Sylvan A15
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
2-aminoadipate 6-semialdehyde + L-glutamate + NADPH
N6-(L-1,3-dicarboxypropyl)-L-lysine + NADP+ + H2O
2-aminoadipate 6-semialdehyde + L-glutamate + NADPH + H+
N6-(L-1,3-dicarboxypropyl)-L-lysine + NADP+ + H2O
-
-
-
-
r
L-glutamate + 2-aminoadipate 6-semialdehyde + NADPH + H+
saccharopine + NADP+ + H2O
-
piperidine-6-carboxylic acid and alpha-aminoadipate are precursors for synthesis of alpha-aminoadipate 6-semialdehyde via 3 different pathways, penultimate step in L-lysine biosynthesis
-
-
?
N6-(L-1,3-dicarboxypropyl)-L-lysine + NAD+ + H2O
L-glutamate + (S)-2-amino-6-oxohexanoate + NADH + H+
-
-
-
-
r
N6-(L-1,3-dicarboxypropyl)-L-lysine + NADP+ + H2O
L-glutamate + (S)-2-amino-6-oxohexanoate + NADPH + H+
N6-(L-1,3-dicarboxypropyl)-L-lysine + NADP+ + H2O
L-glutamate + 2-aminoadipate 6-semialdehyde + NADPH + H+
saccharopine + NADP+ + H2O
L-glutamate + 2-aminoadipate 6-semialdehyde + NADPH + H+
-
reverse reaction direction used for activity assay, end product is piperidine-6-carboxylic acid in assays using cell extract
-
-
r
additional information
?
-
2-aminoadipate 6-semialdehyde + L-glutamate + NADPH
N6-(L-1,3-dicarboxypropyl)-L-lysine + NADP+ + H2O
-
lysine biosynthesis
-
?
2-aminoadipate 6-semialdehyde + L-glutamate + NADPH
N6-(L-1,3-dicarboxypropyl)-L-lysine + NADP+ + H2O
-
lysine biosynthesis
-
?
2-aminoadipate 6-semialdehyde + L-glutamate + NADPH
N6-(L-1,3-dicarboxypropyl)-L-lysine + NADP+ + H2O
-
-
?
2-aminoadipate 6-semialdehyde + L-glutamate + NADPH
N6-(L-1,3-dicarboxypropyl)-L-lysine + NADP+ + H2O
-
-
-
r
2-aminoadipate 6-semialdehyde + L-glutamate + NADPH
N6-(L-1,3-dicarboxypropyl)-L-lysine + NADP+ + H2O
-
-
-
-
r
2-aminoadipate 6-semialdehyde + L-glutamate + NADPH
N6-(L-1,3-dicarboxypropyl)-L-lysine + NADP+ + H2O
-
-
N6-(L-1,3-dicarboxypropyl)-L-lysine is identical with saccharopine
r
2-aminoadipate 6-semialdehyde + L-glutamate + NADPH
N6-(L-1,3-dicarboxypropyl)-L-lysine + NADP+ + H2O
-
-
N6-(L-1,3-dicarboxypropyl)-L-lysine is identical with saccharopine
r
2-aminoadipate 6-semialdehyde + L-glutamate + NADPH
N6-(L-1,3-dicarboxypropyl)-L-lysine + NADP+ + H2O
-
-
N6-(L-1,3-dicarboxypropyl)-L-lysine is identical with saccharopine
r
2-aminoadipate 6-semialdehyde + L-glutamate + NADPH
N6-(L-1,3-dicarboxypropyl)-L-lysine + NADP+ + H2O
-
lysine biosynthesis
-
?
2-aminoadipate 6-semialdehyde + L-glutamate + NADPH
N6-(L-1,3-dicarboxypropyl)-L-lysine + NADP+ + H2O
-
lysine biosynthesis
-
?
2-aminoadipate 6-semialdehyde + L-glutamate + NADPH
N6-(L-1,3-dicarboxypropyl)-L-lysine + NADP+ + H2O
-
lysine biosynthesis
-
?
N6-(L-1,3-dicarboxypropyl)-L-lysine + NADP+ + H2O
L-glutamate + (S)-2-amino-6-oxohexanoate + NADPH + H+
-
-
-
r
N6-(L-1,3-dicarboxypropyl)-L-lysine + NADP+ + H2O
L-glutamate + (S)-2-amino-6-oxohexanoate + NADPH + H+
Agaricus bisporus Sylvan A15
-
-
-
r
N6-(L-1,3-dicarboxypropyl)-L-lysine + NADP+ + H2O
L-glutamate + (S)-2-amino-6-oxohexanoate + NADPH + H+
reaction of the SDH domain
-
-
r
N6-(L-1,3-dicarboxypropyl)-L-lysine + NADP+ + H2O
L-glutamate + (S)-2-amino-6-oxohexanoate + NADPH + H+
reaction of the SDH domain
-
-
r
N6-(L-1,3-dicarboxypropyl)-L-lysine + NADP+ + H2O
L-glutamate + (S)-2-amino-6-oxohexanoate + NADPH + H+
reaction of the SDH domain
-
-
r
N6-(L-1,3-dicarboxypropyl)-L-lysine + NADP+ + H2O
L-glutamate + (S)-2-amino-6-oxohexanoate + NADPH + H+
reaction of the SDH domain
-
-
r
N6-(L-1,3-dicarboxypropyl)-L-lysine + NADP+ + H2O
L-glutamate + (S)-2-amino-6-oxohexanoate + NADPH + H+
-
-
-
?
N6-(L-1,3-dicarboxypropyl)-L-lysine + NADP+ + H2O
L-glutamate + (S)-2-amino-6-oxohexanoate + NADPH + H+
-
-
-
r
N6-(L-1,3-dicarboxypropyl)-L-lysine + NADP+ + H2O
L-glutamate + (S)-2-amino-6-oxohexanoate + NADPH + H+
A0A3L6FCN0
reaction of the SDH domain
-
-
r
N6-(L-1,3-dicarboxypropyl)-L-lysine + NADP+ + H2O
L-glutamate + 2-aminoadipate 6-semialdehyde + NADPH + H+
-
-
-
?
N6-(L-1,3-dicarboxypropyl)-L-lysine + NADP+ + H2O
L-glutamate + 2-aminoadipate 6-semialdehyde + NADPH + H+
enzyme catalyzes the penultimate step in lysine biosynthesis
-
-
?
N6-(L-1,3-dicarboxypropyl)-L-lysine + NADP+ + H2O
L-glutamate + 2-aminoadipate 6-semialdehyde + NADPH + H+
-
-
-
-
?
additional information
?
-
the bifunctional enzyme lysine-ketoglutarate reductase/saccharopine dehydrogenase (LKR/SDH) comprises a LKR domain, which condenses lysine and 2-oxoglutarate into saccharopine, and the SDH domain, that hydrolyzes saccharopine to form glutamate and alpha-aminoadipate semialdehyde, the latter of which is oxidized to alpha-aminoadipate by aminoadipate semialdehyde dehydrogenase (AASADH)
-
-
-
additional information
?
-
the bifunctional enzyme lysine-ketoglutarate reductase/saccharopine dehydrogenase (LKR/SDH) comprises a LKR domain, which condenses lysine and 2-oxoglutarate into saccharopine, and the SDH domain, that hydrolyzes saccharopine to form glutamate and alpha-aminoadipate semialdehyde, the latter of which is oxidized to alpha-aminoadipate by aminoadipate semialdehyde dehydrogenase (AASADH)
-
-
-
additional information
?
-
the bifunctional enzyme lysine-ketoglutarate reductase/saccharopine dehydrogenase (LKR/SDH) comprises a LKR domain, which condenses lysine and 2-oxoglutarate into saccharopine, and the SDH domain, that hydrolyzes saccharopine to form glutamate and alpha-aminoadipate semialdehyde, the latter of which is oxidized to alpha-aminoadipate by aminoadipate semialdehyde dehydrogenase (AASADH)
-
-
-
additional information
?
-
the bifunctional enzyme lysine-ketoglutarate reductase/saccharopine dehydrogenase (LKR/SDH) comprises a LKR domain, which condenses lysine and 2-oxoglutarate into saccharopine, and the SDH domain, that hydrolyzes saccharopine to form glutamate and alpha-aminoadipate semialdehyde, the latter of which is oxidized to alpha-aminoadipate by aminoadipate semialdehyde dehydrogenase (AASADH)
-
-
-
additional information
?
-
A0A3L6FCN0
the bifunctional enzyme lysine-ketoglutarate reductase/saccharopine dehydrogenase (LKR/SDH) comprises a LKR domain, which condenses lysine and 2-oxoglutarate into saccharopine, and the SDH domain, that hydrolyzes saccharopine to form glutamate and alpha-aminoadipate semialdehyde, the latter of which is oxidized to alpha-aminoadipate by aminoadipate semialdehyde dehydrogenase (AASADH)
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
2-aminoadipate 6-semialdehyde + L-glutamate + NADPH
N6-(L-1,3-dicarboxypropyl)-L-lysine + NADP+ + H2O
L-glutamate + 2-aminoadipate 6-semialdehyde + NADPH + H+
saccharopine + NADP+ + H2O
-
piperidine-6-carboxylic acid and alpha-aminoadipate are precursors for synthesis of alpha-aminoadipate 6-semialdehyde via 3 different pathways, penultimate step in L-lysine biosynthesis
-
-
?
N6-(L-1,3-dicarboxypropyl)-L-lysine + NADP+ + H2O
L-glutamate + (S)-2-amino-6-oxohexanoate + NADPH + H+
N6-(L-1,3-dicarboxypropyl)-L-lysine + NADP+ + H2O
L-glutamate + 2-aminoadipate 6-semialdehyde + NADPH + H+
enzyme catalyzes the penultimate step in lysine biosynthesis
-
-
?
2-aminoadipate 6-semialdehyde + L-glutamate + NADPH
N6-(L-1,3-dicarboxypropyl)-L-lysine + NADP+ + H2O
-
lysine biosynthesis
-
?
2-aminoadipate 6-semialdehyde + L-glutamate + NADPH
N6-(L-1,3-dicarboxypropyl)-L-lysine + NADP+ + H2O
-
lysine biosynthesis
-
?
2-aminoadipate 6-semialdehyde + L-glutamate + NADPH
N6-(L-1,3-dicarboxypropyl)-L-lysine + NADP+ + H2O
-
lysine biosynthesis
-
?
2-aminoadipate 6-semialdehyde + L-glutamate + NADPH
N6-(L-1,3-dicarboxypropyl)-L-lysine + NADP+ + H2O
-
lysine biosynthesis
-
?
2-aminoadipate 6-semialdehyde + L-glutamate + NADPH
N6-(L-1,3-dicarboxypropyl)-L-lysine + NADP+ + H2O
-
lysine biosynthesis
-
?
N6-(L-1,3-dicarboxypropyl)-L-lysine + NADP+ + H2O
L-glutamate + (S)-2-amino-6-oxohexanoate + NADPH + H+
-
-
-
r
N6-(L-1,3-dicarboxypropyl)-L-lysine + NADP+ + H2O
L-glutamate + (S)-2-amino-6-oxohexanoate + NADPH + H+
Agaricus bisporus Sylvan A15
-
-
-
r
N6-(L-1,3-dicarboxypropyl)-L-lysine + NADP+ + H2O
L-glutamate + (S)-2-amino-6-oxohexanoate + NADPH + H+
reaction of the SDH domain
-
-
r
N6-(L-1,3-dicarboxypropyl)-L-lysine + NADP+ + H2O
L-glutamate + (S)-2-amino-6-oxohexanoate + NADPH + H+
reaction of the SDH domain
-
-
r
N6-(L-1,3-dicarboxypropyl)-L-lysine + NADP+ + H2O
L-glutamate + (S)-2-amino-6-oxohexanoate + NADPH + H+
reaction of the SDH domain
-
-
r
N6-(L-1,3-dicarboxypropyl)-L-lysine + NADP+ + H2O
L-glutamate + (S)-2-amino-6-oxohexanoate + NADPH + H+
reaction of the SDH domain
-
-
r
N6-(L-1,3-dicarboxypropyl)-L-lysine + NADP+ + H2O
L-glutamate + (S)-2-amino-6-oxohexanoate + NADPH + H+
-
-
-
?
N6-(L-1,3-dicarboxypropyl)-L-lysine + NADP+ + H2O
L-glutamate + (S)-2-amino-6-oxohexanoate + NADPH + H+
-
-
-
r
N6-(L-1,3-dicarboxypropyl)-L-lysine + NADP+ + H2O
L-glutamate + (S)-2-amino-6-oxohexanoate + NADPH + H+
A0A3L6FCN0
reaction of the SDH domain
-
-
r
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
malfunction
A0A3L6FCN0
immature endosperms of high-lysine maize mutants, in addition to the bifunctional LKR/SDH polypeptide, also present a small proportion of an active monofunctional SDH
evolution
after the appearance of the Spe-Sdh gene, the association of the Spe and Sdh genes remained throughout evolution, phylogenetic analysis. The linker region between Spe and Sdh (approximately 60 nucleotides) may have evolved specifically in Basidiomycota to regulate Basidiomycotaspecific processes
evolution
the enzyme domains and activities LKR and SDH belong to a single about 120 kDa bifunctional polypeptide
evolution
A0A3L6FCN0
the enzyme domains and activities LKR and SDH belong to a single about 120 kDa bifunctional polypeptide. In most plants, the enzyme is encoded by a single gene
evolution
the enzyme domains and activities LKR and SDH belong to a single about 120 kDa bifunctional polypeptide. In most plants, the enzyme is encoded by a single gene
evolution
the enzyme domains and activities LKR and SDH belong to a single about 120 kDa bifunctional polypeptide. In most plants, the enzyme is encoded by a single gene
evolution
the enzyme domains and activities LKR and SDH belong to a single about 120 kDa bifunctional polypeptide. In most plants, the enzyme is encoded by a single gene
evolution
Agaricus bisporus Sylvan A15
-
after the appearance of the Spe-Sdh gene, the association of the Spe and Sdh genes remained throughout evolution, phylogenetic analysis. The linker region between Spe and Sdh (approximately 60 nucleotides) may have evolved specifically in Basidiomycota to regulate Basidiomycotaspecific processes
-
metabolism
the central enzymes of the saccharopine pathway (SACPATH) catalyze a transamination-like reaction involving the enzymes lysine-ketoglutarate reductase/saccharopine dehydrogenase (LKR/SDH) and the enzyme alpha-aminoadipate semialdehyde dehydrogenase (AASADH), pathway overview. SACPATH involves the conversion of lysine into alpha-aminoadipate by three enzymatic reactions catalyzed by the bifunctional enzyme LKR/SDH and AASADH. The LKR domain condenses lysine and alpha-ketoglutarate into saccharopine, and the SDH domain hydrolyzes saccharopine to form glutamate and alpha-aminoadipate semialdehyde, the latter of which is oxidized to alpha-aminoadipate by AASADH. The SDH domain hydrolyzes saccharopine into alpha-aminoadipate semialdehyde and glutamate using NAD(P)+ as cofactors, see also EC 1.5.1.10. Stress-induced protein hydrolysis results in increased free lysine levels. Increased lysine pool can also result from the induction of the aspartate (AK) pathway for lysine biosynthesis
metabolism
A0A3L6FCN0
the central enzymes of the saccharopine pathway (SACPATH) catalyze a transamination-like reaction involving the enzymes lysine-ketoglutarate reductase/saccharopine dehydrogenase (LKR/SDH) and the enzyme alpha-aminoadipate semialdehyde dehydrogenase (AASADH), pathway overview. SACPATH involves the conversion of lysine into alpha-aminoadipate by three enzymatic reactions catalyzed by the bifunctional enzyme LKR/SDH and AASADH. The LKR domain condenses lysine and alpha-ketoglutarate into saccharopine, and the SDH domain hydrolyzes saccharopine to form glutamate and alpha-aminoadipate semialdehyde, the latter of which is oxidized to alpha-aminoadipate by AASADH. The SDH domain hydrolyzes saccharopine into alpha-aminoadipate semialdehyde and glutamate using NAD(P)+ as cofactors, see also EC 1.5.1.9. Stress-induced protein hydrolysis results in increased free lysine levels. Increased lysine pool can also result from the induction of the aspartate (AK) pathway for lysine biosynthesis
metabolism
the central enzymes of the saccharopine pathway (SACPATH) catalyze a transamination-like reaction involving the enzymes lysine-ketoglutarate reductase/saccharopine dehydrogenase (LKR/SDH) and the enzyme alpha-aminoadipate semialdehyde dehydrogenase (AASADH), pathway overview. SACPATH involves the conversion of lysine into alpha-aminoadipate by three enzymatic reactions catalyzed by the bifunctional enzyme LKR/SDH and AASADH. The LKR domain condenses lysine and alpha-ketoglutarate into saccharopine, and the SDH domain hydrolyzes saccharopine to form glutamate and alpha-aminoadipate semialdehyde, the latter of which is oxidized to alpha-aminoadipate by AASADH. The SDH domain hydrolyzes saccharopine into alpha-aminoadipate semialdehyde and glutamate using NAD(P)+ as cofactors, see also EC 1.5.1.9. Stress-induced protein hydrolysis results in increased free lysine levels. Increased lysine pool can also result from the induction of the aspartate (AK) pathway for lysine biosynthesis
metabolism
the central enzymes of the saccharopine pathway (SACPATH) catalyze a transamination-like reaction involving the enzymes lysine-ketoglutarate reductase/saccharopine dehydrogenase (LKR/SDH) and the enzyme alpha-aminoadipate semialdehyde dehydrogenase (AASADH), pathway overview. SACPATH involves the conversion of lysine into alpha-aminoadipate by three enzymatic reactions catalyzed by the bifunctional enzyme LKR/SDH and AASADH. The LKR domain condenses lysine and alpha-ketoglutarate into saccharopine, and the SDH domain hydrolyzes saccharopine to form glutamate and alpha-aminoadipate semialdehyde, the latter of which is oxidized to alpha-aminoadipate by AASADH. The SDH domain hydrolyzes saccharopine into alpha-aminoadipate semialdehyde and glutamate using NAD(P)+ as cofactors, see also EC 1.5.1.9. Stress-induced protein hydrolysis results in increased free lysine levels. Increased lysine pool can also result from the induction of the aspartate (AK) pathway for lysine biosynthesis
metabolism
the central enzymes of the saccharopine pathway (SACPATH) catalyze a transamination-like reaction involving the enzymes lysine-ketoglutarate reductase/saccharopine dehydrogenase (LKR/SDH) and the enzyme alpha-aminoadipate semialdehyde dehydrogenase (AASADH), pathway overview. SACPATH involves the conversion of lysine into alpha-aminoadipate by three enzymatic reactions catalyzed by the bifunctional enzyme LKR/SDH and AASADH. The LKR domain condenses lysine and alpha-ketoglutarate into saccharopine, and the SDH domain hydrolyzes saccharopine to form glutamate and alpha-aminoadipate semialdehyde, the latter of which is oxidized to alpha-aminoadipate by AASADH. The SDH domain hydrolyzes saccharopine into alpha-aminoadipate semialdehyde and glutamate using NAD(P)+ as cofactors, see also EC 1.5.1.9. Stress-induced protein hydrolysis results in increased free lysine levels. Increased lysine pool can also result from the induction of the aspartate (AK) pathway for lysine biosynthesis
physiological function
saccharopine reductase catalyzes the reductive amination of L-alpha-aminoadipate-delta-semialdehyde with L-glutamate to give saccharopine
physiological function
enzyme nSpe-Sdh is a bifunctional, chimeric enzyme. SPESDH is involved in Agaricus bisporus postharvest development and is tissue-specially upregulated in cap tissues
physiological function
A0A3L6FCN0
involvement of the SACPATH pathway in plant responses to abiotic and biotic stresses, overview. The induction of LKR activity by phosphorylation in a lysine-dependent manner implies that this enzyme is quickly activated to produce saccharopine once lysine levels start rising. The immediate increase in LKR activity stimulates increases in SDH activity, as the two activities occur within the same polypeptide. The immediate consequence of these two reaction steps is the increase in the concentration of alpha-aminoadipate semialdehyde, which would require an increase in AASADH and perhaps P5CR activities to maintain alpha-aminoadipate semialdehyde concentrations below toxic levels
physiological function
involvement of the SACPATH pathway in plant responses to abiotic and biotic stresses, overview. The induction of LKR activity by phosphorylation in a lysine-dependent manner implies that this enzyme is quickly activated to produce saccharopine once lysine levels start rising. The immediate increase in LKR activity stimulates increases in SDH activity, as the two activities occur within the same polypeptide. The immediate consequence of these two reaction steps is the increase in the concentration of alpha-aminoadipate semialdehyde, which would require an increase in AASADH and perhaps P5CR activities to maintain alpha-aminoadipate semialdehyde concentrations below toxic levels
physiological function
involvement of the SACPATH pathway in plant responses to abiotic and biotic stresses, overview. The induction of LKR activity by phosphorylation in a lysine-dependent manner implies that this enzyme is quickly activated to produce saccharopine once lysine levels start rising. The immediate increase in LKR activity stimulates increases in SDH activity, as the two activities occur within the same polypeptide. The immediate consequence of these two reaction steps is the increase in the concentration of alpha-aminoadipate semialdehyde, which would require an increase in AASADH and perhaps P5CR activities to maintain alpha-aminoadipate semialdehyde concentrations below toxic levels
physiological function
involvement of the SACPATH pathway in plant responses to abiotic and biotic stresses, overview. The induction of LKR activity by phosphorylation in a lysine-dependent manner implies that this enzyme is quickly activated to produce saccharopine once lysine levels start rising. The immediate increase in LKR activity stimulates increases in SDH activity, as the two activities occur within the same polypeptide. The immediate consequence of these two reaction steps is the increase in the concentration of alpha-aminoadipate semialdehyde, which would require an increase in AASADH and perhaps P5CR activities to maintain alpha-aminoadipate semialdehyde concentrations below toxic levels
physiological function
Agaricus bisporus Sylvan A15
-
enzyme nSpe-Sdh is a bifunctional, chimeric enzyme. SPESDH is involved in Agaricus bisporus postharvest development and is tissue-specially upregulated in cap tissues
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
monomer
-
1 * 50000, SDS-PAGE
?
x * 83630, sequence calculation, x * 84000, recombinant His-tagged enzyme, SDS-PAGE
?
Agaricus bisporus Sylvan A15
-
x * 83630, sequence calculation, x * 84000, recombinant His-tagged enzyme, SDS-PAGE
-
dimer
-
alpha2, 2 * 50000, SDS-PAGE
dimer
-
alpha2, 2 * 48900, predicted mass from the gene sequence
additional information
the nSpe-Sdh gene contains a Spermidine_synt_N InterPro domain (IPR035246) at its N-terminal region, existence of a linker region (approximately 60 nucleotides) between Spe and Sdh in Agaricus bisporus
additional information
Agaricus bisporus Sylvan A15
-
the nSpe-Sdh gene contains a Spermidine_synt_N InterPro domain (IPR035246) at its N-terminal region, existence of a linker region (approximately 60 nucleotides) between Spe and Sdh in Agaricus bisporus
-
additional information
the enzyme domains and activities LKR and SDH belong to a single about 120 kDa bifunctional polypeptide. In plants, the LKR and SDH domains of the bifunctional polypeptide are separated from each other by an about 130 amino acid interdomain
additional information
the enzyme domains and activities LKR and SDH belong to a single about 120 kDa bifunctional polypeptide. In plants, the LKR and SDH domains of the bifunctional polypeptide are separated from each other by an about 130 amino acid interdomain
additional information
the enzyme domains and activities LKR and SDH belong to a single about 120 kDa bifunctional polypeptide
additional information
the enzyme domains and activities LKR and SDH belong to a single about 120 kDa bifunctional polypeptide. In plants, the LKR and SDH domains of the bifunctional polypeptide are separated from each other by an about 130 amino acid interdomain
additional information
comparison of enzyme structures from Saccharomyces cerevisiae and Magnoporthe grisea
additional information
-
comparison of enzyme structures from Saccharomyces cerevisiae and Magnoporthe grisea
additional information
A0A3L6FCN0
the enzyme domains and activities LKR and SDH belong to a single about 120 kDa bifunctional polypeptide. In plants, the LKR and SDH domains of the bifunctional polypeptide are separated from each other by an about 130 amino acid interdomain
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
C154S
site-directed mutagenesis
C154S/Y99F
site-directed mutagenesis
D126A
site-directed mutagenesis
D126A/C154S
site-directed mutagenesis
D126A/Y99F
site-directed mutagenesis
Y99F
site-directed mutagenesis
additional information
construction of 3 Spe3-Lys9 mutants, with defects in the spe3-part, the lys9-part, or both, which are auxotrophic for lysine and spermidine, spermidine, and lysine, respectively, transcription levels and phenotype overview, the polyamine auxotrophy due to defect spe3 cannot be overcome by spermine addition, while the mutan with lys 9 defect grows slowly at 30°C with lysine addition, but dies upon lysine starvation, the mutant with defects in both gene parts is avirulent and lethal
additional information
-
construction of 3 Spe3-Lys9 mutants, with defects in the spe3-part, the lys9-part, or both, which are auxotrophic for lysine and spermidine, spermidine, and lysine, respectively, transcription levels and phenotype overview, the polyamine auxotrophy due to defect spe3 cannot be overcome by spermine addition, while the mutan with lys 9 defect grows slowly at 30°C with lysine addition, but dies upon lysine starvation, the mutant with defects in both gene parts is avirulent and lethal
additional information
-
construction of an enzyme-deficient mutant strain: disruption and inactivation of gene lys7 by double-recombination method leads to lysine auxotrophy and accumulation of piperideine-6-carboxylic acid, and with L-lysine as sole N-source and supplementation of DL-alpha-aminoadipic acid, also of pipecolic acid, transformation of the mutant strain with lys7 can restore enzyme activity
additional information
kinetic parameters of the mutants in the reaction direction of glutamate formation exhibit modest decreases. The pH-rate profiles obtained with all mutant enzymes decrease at low and high pH, suggesting acid and base catalytic groups are still present in all enzymes. Solvent kinetic deuterium isotope effects are all larger than those observed for wild-type enzyme
additional information
-
kinetic parameters of the mutants in the reaction direction of glutamate formation exhibit modest decreases. The pH-rate profiles obtained with all mutant enzymes decrease at low and high pH, suggesting acid and base catalytic groups are still present in all enzymes. Solvent kinetic deuterium isotope effects are all larger than those observed for wild-type enzyme
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
once the protecting veil is broken during storage, the expression levels decrease to an initial storage level and remain relatively constant until the end of the storage, indicating the possible involvement of nSpe-Sdh in postharvest mushroom development
the enzymes LKR/SDH and AASADH are co-upregulated at the transcriptional level by exogenously applied lysine in plants, animals, and bacteria
the enzymes LKR/SDH and AASADH are co-upregulated at the transcriptional level by exogenously applied lysine in plants, animals, and bacteria. Hyperosmotic treatment of rapeseed leaf disks induces an increase in LKR/SDH transcript abundance and enzymatic activity, which correlates with decreased levels of free lysine and increased levels of pipecolate. The LKR/SDH activity and pipecolate concentration decrease with the return of the leaf disks to hypoosmotic conditions
the expression of nSPE-SDH mRNA and protein are both significantly upregulated with the cap expansion of Agaricus bisporus during storage. The up-regulation of the expression of nSPE-SDH mRNA and protein was both tissue especially in cap tissues
once the protecting veil is broken during storage, the expression levels decrease to an initial storage level and remain relatively constant until the end of the storage, indicating the possible involvement of nSpe-Sdh in postharvest mushroom development
once the protecting veil is broken during storage, the expression levels decrease to an initial storage level and remain relatively constant until the end of the storage, indicating the possible involvement of nSpe-Sdh in postharvest mushroom development
Agaricus bisporus Sylvan A15
-
-
the enzymes LKR/SDH and AASADH are co-upregulated at the transcriptional level by exogenously applied lysine in plants, animals, and bacteria
A0A3L6FCN0
the enzymes LKR/SDH and AASADH are co-upregulated at the transcriptional level by exogenously applied lysine in plants, animals, and bacteria
the enzymes LKR/SDH and AASADH are co-upregulated at the transcriptional level by exogenously applied lysine in plants, animals, and bacteria
the enzymes LKR/SDH and AASADH are co-upregulated at the transcriptional level by exogenously applied lysine in plants, animals, and bacteria
the expression of nSPE-SDH mRNA and protein are both significantly upregulated with the cap expansion of Agaricus bisporus during storage. The up-regulation of the expression of nSPE-SDH mRNA and protein was both tissue especially in cap tissues
the expression of nSPE-SDH mRNA and protein are both significantly upregulated with the cap expansion of Agaricus bisporus during storage. The up-regulation of the expression of nSPE-SDH mRNA and protein was both tissue especially in cap tissues
Agaricus bisporus Sylvan A15
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
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 (Q96TW2), Penicillium chrysogenum
brenda
Mukhopadhyay, A.; Mungre, S.M.; Desmukh, D.R.
Comparison of lysine and tryptophan catabolizing enzymes in rat and bovine tissues
Experientia
46
874-876
1990
Bos taurus, Rattus norvegicus
brenda
Schmidt, H.; Bode, R.; Birnbaum, D.
Regulation of the lysine biosynthesis in Pichia guilliermondii
Antonie van Leeuwenhoek
56
337-347
1989
Meyerozyma guilliermondii
brenda
Broquist, H.P.
Aminoadipic semialdehyde-glutamate reductase
Methods Enzymol.
17B
121-124
1971
Saccharomyces cerevisiae
-
brenda
Jones, E.E.; Broquist, H.P.
Saccharopine, an intermediate of the aminoadipic acid pathway of lysine biosynthesis. 3. Aminoadipic semialdehyde-glutamate reductase
J. Biol. Chem.
241
3430-3434
1966
Saccharomyces cerevisiae
brenda
Storts, D.R.; Bhattacharjee, J.K.
Purification and properties of saccharopine dehydrogenase (glutamate forming) in the Saccharomyces cerevisiae lysine biosynthetic pathway
J. Bacteriol.
169
416-418
1987
Saccharomyces cerevisiae
brenda
Kinzel, J.J.; Bhattacharjee, J.K.
Role of pipecolic acid in the biosynthesis of lysine in Rhodotorula glutinis
J. Bacteriol.
138
410-417
1979
Rhodotorula glutinis
brenda
Johansson, E.; Steffens, J.J.; Emptage, M.; Lindqvist, Y.; Schneider, G.
Cloning, expression, purification and crystallization of saccharopine reductase from Magnaporthe grisea
Acta Crystallogr. Sect. D
56
662-664
2000
Pyricularia grisea
-
brenda
Naranjo, L.; Martin de Valmaseda, E.; Casqueiro, J.; Ullan, R.V.; Lamas-Maceiras, M.; Banuelos, O.; Martin, J.F.
Inactivation of the lys7 gene, encoding saccharopine reductase in Penicillium chrysogenum, leads to accumulation of the secondary metabolite precursors piperideine-6-carboxylic acid and pipecolic acid from alpha-aminoadipic acid
Appl. Environ. Microbiol.
70
1031-1039
2004
Penicillium chrysogenum
brenda
Kingsbury, J.M.; Yang, Z.; Ganous, T.M.; Cox, G.M.; McCusker, J.H.
Novel chimeric spermidine synthase-saccharopine dehydrogenase gene (SPE3-LYS9) in the human pathogen Cryptococcus neoformans
Eukaryot. Cell
3
752-763
2004
Cryptococcus neoformans (Q6RXX2), Cryptococcus neoformans
brenda
Andi, B.; Cook, P.F.; West, A.H.
Crystal structure of the his-tagged saccharopine reductase from Saccharomyces cerevisiae at 1.7-A resolution
Cell Biochem. Biophys.
46
17-26
2006
Saccharomyces cerevisiae
brenda
Vashishtha, A.K.; West, A.H.; Cook, P.F.
Overall kinetic mechanism of saccharopine dehydrogenase (L-glutamate forming) from Saccharomyces cerevisiae
Biochemistry
47
5417-5423
2008
Saccharomyces cerevisiae
brenda
Vashishtha, A.K.; West, A.H.; Cook, P.F.
Chemical mechanism of saccharopine reductase from Saccharomyces cerevisiae
Biochemistry
48
5899-5907
2009
Saccharomyces cerevisiae
brenda
Almasi, J.; Bushnell, E.; Gauld, J.
A QM/MM-based computational investigation on the catalytic mechanism of saccharopine reductase
Molecules
16
8569-8589
2011
Pyricularia oryzae (Q9P4R4)
brenda
Vashishtha, A.K.; West, A.H.; Cook, P.F.
Probing the chemical mechanism of saccharopine reductase from Saccharomyces cerevisiae using site-directed mutagenesis
Arch. Biochem. Biophys.
584
98-106
2015
Saccharomyces cerevisiae (P38999), Saccharomyces cerevisiae
brenda
Arruda, P.; Barreto, P.
Lysine catabolism through the saccharopine pathway enzymes and intermediates involved in plant responses to abiotic and biotic stress
Front. Plant Sci.
11
587
2020
Oryza sativa (A0A0K0K9B1), Zea mays (A0A3L6FCN0), Brassica napus (Q9FVF4), Arabidopsis thaliana (Q9SMZ4), Homo sapiens (Q9UDR5)
brenda
Xi, Z.; Yang, K.; Sheng, J.; Zhang, X.; Guo, J.; Meng, D.
Novel chimeric spermidine synthase-saccharopine dehydrogenase gene with a possible role in postharvest development of the button mushroom (Agaricus bisporus)
J. Hortic. Sci. Biotechnol.
95
712-721
2020
Agaricus bisporus (D7GL19), Agaricus bisporus Sylvan A15 (D7GL19)
-
brenda