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N6-(L-1,3-dicarboxypropyl)-L-lysine + NAD+ + H2O
L-Glu + 2-aminoadipate 6-semialdehyde + NADH
N6-(L-1,3-dicarboxypropyl)-L-lysine + NAD+ + H2O
L-glutamate + (S)-2-amino-6-oxohexanoate + NADH + H+
N6-(L-1,3-dicarboxypropyl)-L-lysine + NAD+ + H2O
L-glutamate + 2-aminoadipate 6-semialdehyde + NADH + H+
saccharopine + NAD+ + H2O
L-glutamate + alpha-aminoadipate semialdehyde + NADH + H+
additional information
?
-
N6-(L-1,3-dicarboxypropyl)-L-lysine + NAD+ + H2O
L-Glu + 2-aminoadipate 6-semialdehyde + NADH
-
-
-
-
?
N6-(L-1,3-dicarboxypropyl)-L-lysine + NAD+ + H2O
L-Glu + 2-aminoadipate 6-semialdehyde + NADH
-
the bifunctional reductase/saccharopine dehydrogenase contains the first two enzyme of lysine catabolism, is concertedly regulated by metabolic and stress-associated signals. The level of the bifunctional enzyme is strongly enhanced by abscisic acid, jasmonate, and sugar starvation, whereas excess sugars and nitrogen starvation reduce its level
-
-
?
N6-(L-1,3-dicarboxypropyl)-L-lysine + NAD+ + H2O
L-glutamate + (S)-2-amino-6-oxohexanoate + NADH + H+
reaction of the SDH domain
-
-
r
N6-(L-1,3-dicarboxypropyl)-L-lysine + NAD+ + H2O
L-glutamate + (S)-2-amino-6-oxohexanoate + NADH + H+
reaction of the SDH domain
-
-
r
N6-(L-1,3-dicarboxypropyl)-L-lysine + NAD+ + H2O
L-glutamate + (S)-2-amino-6-oxohexanoate + NADH + H+
reaction of the SDH domain
-
-
r
N6-(L-1,3-dicarboxypropyl)-L-lysine + NAD+ + H2O
L-glutamate + (S)-2-amino-6-oxohexanoate + NADH + H+
-
-
-
-
?
N6-(L-1,3-dicarboxypropyl)-L-lysine + NAD+ + H2O
L-glutamate + (S)-2-amino-6-oxohexanoate + NADH + H+
-
-
-
?
N6-(L-1,3-dicarboxypropyl)-L-lysine + NAD+ + H2O
L-glutamate + (S)-2-amino-6-oxohexanoate + NADH + H+
reaction of the SDH domain
-
-
r
N6-(L-1,3-dicarboxypropyl)-L-lysine + NAD+ + H2O
L-glutamate + (S)-2-amino-6-oxohexanoate + NADH + H+
-
-
-
?
N6-(L-1,3-dicarboxypropyl)-L-lysine + NAD+ + H2O
L-glutamate + (S)-2-amino-6-oxohexanoate + NADH + H+
A0A3L6FCN0
reaction of the SDH domain
-
-
r
N6-(L-1,3-dicarboxypropyl)-L-lysine + NAD+ + H2O
L-glutamate + 2-aminoadipate 6-semialdehyde + NADH + H+
-
-
-
-
?
N6-(L-1,3-dicarboxypropyl)-L-lysine + NAD+ + H2O
L-glutamate + 2-aminoadipate 6-semialdehyde + NADH + H+
-
-
-
-
r
N6-(L-1,3-dicarboxypropyl)-L-lysine + NAD+ + H2O
L-glutamate + 2-aminoadipate 6-semialdehyde + NADH + H+
-
involved in lysine catabolism
-
-
r
N6-(L-1,3-dicarboxypropyl)-L-lysine + NAD+ + H2O
L-glutamate + 2-aminoadipate 6-semialdehyde + NADH + H+
-
-
-
-
r
N6-(L-1,3-dicarboxypropyl)-L-lysine + NAD+ + H2O
L-glutamate + 2-aminoadipate 6-semialdehyde + NADH + H+
-
involved in lysine catabolism
-
-
?
N6-(L-1,3-dicarboxypropyl)-L-lysine + NAD+ + H2O
L-glutamate + 2-aminoadipate 6-semialdehyde + NADH + H+
-
involved in lysine catabolism
-
-
r
N6-(L-1,3-dicarboxypropyl)-L-lysine + NAD+ + H2O
L-glutamate + 2-aminoadipate 6-semialdehyde + NADH + H+
-
-
-
-
r
N6-(L-1,3-dicarboxypropyl)-L-lysine + NAD+ + H2O
L-glutamate + 2-aminoadipate 6-semialdehyde + NADH + H+
-
involved in lysine catabolism
-
-
r
N6-(L-1,3-dicarboxypropyl)-L-lysine + NAD+ + H2O
L-glutamate + 2-aminoadipate 6-semialdehyde + NADH + H+
-
-
-
-
r
N6-(L-1,3-dicarboxypropyl)-L-lysine + NAD+ + H2O
L-glutamate + 2-aminoadipate 6-semialdehyde + NADH + H+
-
involved in lysine catabolism
-
-
r
N6-(L-1,3-dicarboxypropyl)-L-lysine + NAD+ + H2O
L-glutamate + 2-aminoadipate 6-semialdehyde + NADH + H+
-
-
-
-
r
N6-(L-1,3-dicarboxypropyl)-L-lysine + NAD+ + H2O
L-glutamate + 2-aminoadipate 6-semialdehyde + NADH + H+
-
involved in lysine catabolism
-
-
r
N6-(L-1,3-dicarboxypropyl)-L-lysine + NAD+ + H2O
L-glutamate + 2-aminoadipate 6-semialdehyde + NADH + H+
-
-
-
-
?
N6-(L-1,3-dicarboxypropyl)-L-lysine + NAD+ + H2O
L-glutamate + 2-aminoadipate 6-semialdehyde + NADH + H+
-
-
-
-
r
N6-(L-1,3-dicarboxypropyl)-L-lysine + NAD+ + H2O
L-glutamate + 2-aminoadipate 6-semialdehyde + NADH + H+
-
N6-(L-1,3-dicarboxypropyl)-L-lysine is identical with saccharopine, high specificity
-
-
r
N6-(L-1,3-dicarboxypropyl)-L-lysine + NAD+ + H2O
L-glutamate + 2-aminoadipate 6-semialdehyde + NADH + H+
-
involved in lysine catabolism
-
-
r
N6-(L-1,3-dicarboxypropyl)-L-lysine + NAD+ + H2O
L-glutamate + 2-aminoadipate 6-semialdehyde + NADH + H+
-
-
-
-
?
N6-(L-1,3-dicarboxypropyl)-L-lysine + NAD+ + H2O
L-glutamate + 2-aminoadipate 6-semialdehyde + NADH + H+
-
-
-
-
r
N6-(L-1,3-dicarboxypropyl)-L-lysine + NAD+ + H2O
L-glutamate + 2-aminoadipate 6-semialdehyde + NADH + H+
-
involved in lysine catabolism
-
-
r
N6-(L-1,3-dicarboxypropyl)-L-lysine + NAD+ + H2O
L-glutamate + 2-aminoadipate 6-semialdehyde + NADH + H+
-
-
-
-
r
N6-(L-1,3-dicarboxypropyl)-L-lysine + NAD+ + H2O
L-glutamate + 2-aminoadipate 6-semialdehyde + NADH + H+
-
-
-
-
r
N6-(L-1,3-dicarboxypropyl)-L-lysine + NAD+ + H2O
L-glutamate + 2-aminoadipate 6-semialdehyde + NADH + H+
-
involved in lysine catabolism
-
-
r
N6-(L-1,3-dicarboxypropyl)-L-lysine + NAD+ + H2O
L-glutamate + 2-aminoadipate 6-semialdehyde + NADH + H+
-
-
-
-
r
N6-(L-1,3-dicarboxypropyl)-L-lysine + NAD+ + H2O
L-glutamate + 2-aminoadipate 6-semialdehyde + NADH + H+
-
involved in lysine catabolism
-
-
r
N6-(L-1,3-dicarboxypropyl)-L-lysine + NAD+ + H2O
L-glutamate + 2-aminoadipate 6-semialdehyde + NADH + H+
-
-
-
-
?
N6-(L-1,3-dicarboxypropyl)-L-lysine + NAD+ + H2O
L-glutamate + 2-aminoadipate 6-semialdehyde + NADH + H+
-
-
-
-
r
N6-(L-1,3-dicarboxypropyl)-L-lysine + NAD+ + H2O
L-glutamate + 2-aminoadipate 6-semialdehyde + NADH + H+
-
involved in lysine catabolism
-
-
?
N6-(L-1,3-dicarboxypropyl)-L-lysine + NAD+ + H2O
L-glutamate + 2-aminoadipate 6-semialdehyde + NADH + H+
-
involved in lysine catabolism
-
-
r
N6-(L-1,3-dicarboxypropyl)-L-lysine + NAD+ + H2O
L-glutamate + 2-aminoadipate 6-semialdehyde + NADH + H+
-
-
-
-
r
N6-(L-1,3-dicarboxypropyl)-L-lysine + NAD+ + H2O
L-glutamate + 2-aminoadipate 6-semialdehyde + NADH + H+
-
involved in lysine catabolism
-
-
r
N6-(L-1,3-dicarboxypropyl)-L-lysine + NAD+ + H2O
L-glutamate + 2-aminoadipate 6-semialdehyde + NADH + H+
-
-
-
-
?
N6-(L-1,3-dicarboxypropyl)-L-lysine + NAD+ + H2O
L-glutamate + 2-aminoadipate 6-semialdehyde + NADH + H+
-
-
-
-
?
N6-(L-1,3-dicarboxypropyl)-L-lysine + NAD+ + H2O
L-glutamate + 2-aminoadipate 6-semialdehyde + NADH + H+
-
-
-
-
r
N6-(L-1,3-dicarboxypropyl)-L-lysine + NAD+ + H2O
L-glutamate + 2-aminoadipate 6-semialdehyde + NADH + H+
-
involved in lysine catabolism
-
-
r
N6-(L-1,3-dicarboxypropyl)-L-lysine + NAD+ + H2O
L-glutamate + 2-aminoadipate 6-semialdehyde + NADH + H+
-
-
-
-
r
N6-(L-1,3-dicarboxypropyl)-L-lysine + NAD+ + H2O
L-glutamate + 2-aminoadipate 6-semialdehyde + NADH + H+
-
involved in lysine catabolism
-
-
r
saccharopine + NAD+ + H2O
L-glutamate + alpha-aminoadipate semialdehyde + NADH + H+
-
-
-
-
r
saccharopine + NAD+ + H2O
L-glutamate + alpha-aminoadipate semialdehyde + NADH + H+
-
-
-
-
r
saccharopine + NAD+ + H2O
L-glutamate + alpha-aminoadipate semialdehyde + NADH + H+
-
-
-
-
r
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). Monofunctional SDH has also been found in animals and in Arabidopsis thaliana
-
-
-
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 enzyme is bifunctional catalyzing the reaction of EC 1.5.1.8, saccharopine dehydrogenase (NADP+, L-lysine-forming) in the reverse direction, and EC 1.5.1.9, saccharopine dehydrogenase (NAD+, L-glutamate-forming)
-
-
?
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.
N6-(L-1,3-dicarboxypropyl)-L-lysine + NAD+ + H2O
L-Glu + 2-aminoadipate 6-semialdehyde + NADH
-
the bifunctional reductase/saccharopine dehydrogenase contains the first two enzyme of lysine catabolism, is concertedly regulated by metabolic and stress-associated signals. The level of the bifunctional enzyme is strongly enhanced by abscisic acid, jasmonate, and sugar starvation, whereas excess sugars and nitrogen starvation reduce its level
-
-
?
N6-(L-1,3-dicarboxypropyl)-L-lysine + NAD+ + H2O
L-glutamate + (S)-2-amino-6-oxohexanoate + NADH + H+
N6-(L-1,3-dicarboxypropyl)-L-lysine + NAD+ + H2O
L-glutamate + 2-aminoadipate 6-semialdehyde + NADH + H+
saccharopine + NAD+ + H2O
L-glutamate + alpha-aminoadipate semialdehyde + NADH + H+
N6-(L-1,3-dicarboxypropyl)-L-lysine + NAD+ + H2O
L-glutamate + (S)-2-amino-6-oxohexanoate + NADH + H+
reaction of the SDH domain
-
-
r
N6-(L-1,3-dicarboxypropyl)-L-lysine + NAD+ + H2O
L-glutamate + (S)-2-amino-6-oxohexanoate + NADH + H+
reaction of the SDH domain
-
-
r
N6-(L-1,3-dicarboxypropyl)-L-lysine + NAD+ + H2O
L-glutamate + (S)-2-amino-6-oxohexanoate + NADH + H+
reaction of the SDH domain
-
-
r
N6-(L-1,3-dicarboxypropyl)-L-lysine + NAD+ + H2O
L-glutamate + (S)-2-amino-6-oxohexanoate + NADH + H+
-
-
-
-
?
N6-(L-1,3-dicarboxypropyl)-L-lysine + NAD+ + H2O
L-glutamate + (S)-2-amino-6-oxohexanoate + NADH + H+
-
-
-
?
N6-(L-1,3-dicarboxypropyl)-L-lysine + NAD+ + H2O
L-glutamate + (S)-2-amino-6-oxohexanoate + NADH + H+
reaction of the SDH domain
-
-
r
N6-(L-1,3-dicarboxypropyl)-L-lysine + NAD+ + H2O
L-glutamate + (S)-2-amino-6-oxohexanoate + NADH + H+
-
-
-
?
N6-(L-1,3-dicarboxypropyl)-L-lysine + NAD+ + H2O
L-glutamate + (S)-2-amino-6-oxohexanoate + NADH + H+
A0A3L6FCN0
reaction of the SDH domain
-
-
r
N6-(L-1,3-dicarboxypropyl)-L-lysine + NAD+ + H2O
L-glutamate + 2-aminoadipate 6-semialdehyde + NADH + H+
-
involved in lysine catabolism
-
-
r
N6-(L-1,3-dicarboxypropyl)-L-lysine + NAD+ + H2O
L-glutamate + 2-aminoadipate 6-semialdehyde + NADH + H+
-
involved in lysine catabolism
-
-
?
N6-(L-1,3-dicarboxypropyl)-L-lysine + NAD+ + H2O
L-glutamate + 2-aminoadipate 6-semialdehyde + NADH + H+
-
involved in lysine catabolism
-
-
r
N6-(L-1,3-dicarboxypropyl)-L-lysine + NAD+ + H2O
L-glutamate + 2-aminoadipate 6-semialdehyde + NADH + H+
-
involved in lysine catabolism
-
-
r
N6-(L-1,3-dicarboxypropyl)-L-lysine + NAD+ + H2O
L-glutamate + 2-aminoadipate 6-semialdehyde + NADH + H+
-
involved in lysine catabolism
-
-
r
N6-(L-1,3-dicarboxypropyl)-L-lysine + NAD+ + H2O
L-glutamate + 2-aminoadipate 6-semialdehyde + NADH + H+
-
involved in lysine catabolism
-
-
r
N6-(L-1,3-dicarboxypropyl)-L-lysine + NAD+ + H2O
L-glutamate + 2-aminoadipate 6-semialdehyde + NADH + H+
-
involved in lysine catabolism
-
-
r
N6-(L-1,3-dicarboxypropyl)-L-lysine + NAD+ + H2O
L-glutamate + 2-aminoadipate 6-semialdehyde + NADH + H+
-
involved in lysine catabolism
-
-
r
N6-(L-1,3-dicarboxypropyl)-L-lysine + NAD+ + H2O
L-glutamate + 2-aminoadipate 6-semialdehyde + NADH + H+
-
involved in lysine catabolism
-
-
r
N6-(L-1,3-dicarboxypropyl)-L-lysine + NAD+ + H2O
L-glutamate + 2-aminoadipate 6-semialdehyde + NADH + H+
-
involved in lysine catabolism
-
-
r
N6-(L-1,3-dicarboxypropyl)-L-lysine + NAD+ + H2O
L-glutamate + 2-aminoadipate 6-semialdehyde + NADH + H+
-
involved in lysine catabolism
-
-
?
N6-(L-1,3-dicarboxypropyl)-L-lysine + NAD+ + H2O
L-glutamate + 2-aminoadipate 6-semialdehyde + NADH + H+
-
involved in lysine catabolism
-
-
r
N6-(L-1,3-dicarboxypropyl)-L-lysine + NAD+ + H2O
L-glutamate + 2-aminoadipate 6-semialdehyde + NADH + H+
-
involved in lysine catabolism
-
-
r
N6-(L-1,3-dicarboxypropyl)-L-lysine + NAD+ + H2O
L-glutamate + 2-aminoadipate 6-semialdehyde + NADH + H+
-
involved in lysine catabolism
-
-
r
N6-(L-1,3-dicarboxypropyl)-L-lysine + NAD+ + H2O
L-glutamate + 2-aminoadipate 6-semialdehyde + NADH + H+
-
involved in lysine catabolism
-
-
r
saccharopine + NAD+ + H2O
L-glutamate + alpha-aminoadipate semialdehyde + NADH + H+
-
-
-
-
r
saccharopine + NAD+ + H2O
L-glutamate + alpha-aminoadipate semialdehyde + NADH + H+
-
-
-
-
r
saccharopine + NAD+ + H2O
L-glutamate + alpha-aminoadipate semialdehyde + NADH + H+
-
-
-
-
r
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Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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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.
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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
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. Monofunctional SDH has also been found in animals and in Arabidopsis thaliana
metabolism
the enzyme is involved in L-lysine breakdown. In Nilaparvata lugens, the degradation of L-lysine is independent from the yeast-like endosymbionts of the organism, in contrast to degradation of other amino acids, overview
metabolism
-
the enzyme is involved in L-lysine degradation
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 1.5.1.10. 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
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
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
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
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
physiological function
-
gene silencing by RNAi indicates that the tick LKR/SDH plays an integral role in the osmotic regulation of water balance and development of eggs in ovary of engorged females
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
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Hutzler, J.; Dancis, J.
Lysine-ketoglutarate reductase in human tissues
Biochim. Biophys. Acta
377
42-51
1975
Homo sapiens
brenda
Fellows, F.C.I.; Lewis, M.H.R.
Lysine metabolism in mammals
Biochem. J.
136
329-334
1973
Bos taurus, Canis lupus familiaris, Felis catus, Ovis aries, Homo sapiens, Rattus norvegicus, Sus scrofa
brenda
Markovitz, P.J.; Chuang, D.T.; Cox, R.P.
Familial hyperlysinemias. Purification and characterization of the bifunctional aminoadipic semialdehyde synthase with lysine-ketoglutarate reductase and saccharopine dehydrogenase activities
J. Biol. Chem.
259
11643-11646
1984
Bos taurus, Papio hamadryas
brenda
Markovitz, P.J.; Chuang, D.T.
The bifunctional aminoadipic semialdehyde synthase in lysine degradation. Separation of reductase and dehydrogenase domains by limited proteolysis and column chromatography
J. Biol. Chem.
262
9353-9358
1987
Bos taurus
brenda
Blemings, K.P.; Crenshaw, T.D.; Swick, R.W.; Benevenga, N.J.
Lysine-alpha-ketoglutarate reductase and saccharopine dehydrogenase are located only in the mitochondrial matrix in rat liver
J. Nutr.
124
1215-1221
1994
Rattus norvegicus
brenda
Gaziola, S.A.; Teixeira, C.M.; Lugli, J.; Sodek, L.; Azevedo, R.A.
The enzymology of lysine catabolism in rice seeds. Isolation, characterization, and regulatory properties of a lysine 2-oxoglutarate reductase/saccharopine dehydrogenase bifunctional polypeptide
Eur. J. Biochem.
247
364-371
1997
Oryza sativa
brenda
Miron, D.; Ben-Yaacov, S.; Karchi, H.; Galili, G.
In vitro dephosphorylation inhibits the activity of soybean lysine-ketoglutarate reductase in a lysine-regulated manner
Plant J.
12
1453-1458
1997
Glycine max
-
brenda
Fjellstedt, T.A.; Robinson, J.C.
Properties of partially purified saccharopine dehydrogenase from human placenta
Arch. Biochem. Biophys.
171
191-196
1975
Homo sapiens
brenda
Hutzler, J.; Dancis, J.
Saccharopine cleavage by a dehydrogenase of human liver
Biochim. Biophys. Acta
206
205-214
1970
Homo sapiens
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
Goncalves-Butruille, M.; Szajner, P.; Torigoi, E.; Leite, A.; Arruda, P.
Purification and Characterization of the Bifunctional Enzyme Lysine-Ketoglutarate Reductase-Saccharopine Dehydrogenase from Maize
Plant Physiol.
110
765-771
1996
Zea mays
brenda
Zhu, X.; Tang, G.; Galili, G.
Characterization of the two saccharopine dehydrogenase isozymes of lysine catabolism encoded by the single composite AtLKR/SDH locus of Arabidopsis
Plant Physiol.
124
1363-1371
2000
Arabidopsis thaliana
brenda
Cunha Lima, S.T.; Azevedo, R.A.; Santoro, L.G.; Gaziola, S.A.; Lea, P.J.
Isolation of the bifunctional enzyme lysine 2-oxoglutarate reductase-saccharopine dehydrogenase from Phaseolus vulgaris
Amino Acids
24
179-186
2003
Phaseolus vulgaris
brenda
Fornazier, R.F.; Gaziola, S.A.; Helm, C.V.; Lea, P.J.; Azevedo, R.A.
Isolation and characterization of enzymes involved in lysine catabolism from sorghum seeds
J. Agric. Food Chem.
53
1791-1798
2005
Sorghum bicolor, Sorghum bicolor Moench
brenda
Stepansky, A.; Galili, G.
Synthesis of the Arabidopsis bifunctional lysine-ketoglutarate reductase/saccharopine dehydrogenase enzyme of lysine catabolism is concertedly regulated by metabolic and stress-associated signals
Plant Physiol.
133
1407-1415
2003
Arabidopsis sp.
brenda
Schildhauer, J.; Wiedemuth, K.; Humbeck, K.
Supply of nitrogen can reverse senescence processes and affect expression of genes coding for plastidic glutamine synthetase and lysine-ketoglutarate reductase/saccharopine dehydrogenase
Plant Biol.
10 Suppl 1
76-84
2008
Arabidopsis thaliana, Hordeum vulgare
brenda
Battur, B.; Boldbaatar, D.; Umemiya-Shirafuji, R.; Liao, M.; Battsetseg, B.; Taylor, D.; Baymbaa, B.; Fujisaki, K.
LKR/SDH plays important roles throughout the tick life cycle including a long starvation period
PLoS ONE
4
e7136
2009
Haemaphysalis longicornis
brenda
Leon-Ramirez, C.G.; Valdes-Santiago, L.; Campos-Gongora, E.; Ortiz-Castellanos, L.; Arechiga-Carvajal, E.T.; Ruiz-Herrera, J.
A molecular probe for Basidiomycota: the spermidine synthase-saccharopine dehydrogenase chimeric gene
FEMS Microbiol. Lett.
312
77-83
2010
Ustilago maydis (C0MP55)
brenda
Anderson, O.D.; Coleman-Derr, D.; Gu, Y.Q.; Heath, S.
Structural and transcriptional analysis of plant genes encoding the bifunctional lysine ketoglutarate reductase saccharopine dehydrogenase enzyme
BMC Plant Biol.
10
113
2010
Triticum turgidum (D8WKY4)
brenda
Serrano, G.C.; Rezende e Silva Figueira, T.; Kiyota, E.; Zanata, N.; Arruda, P.
Lysine degradation through the saccharopine pathway in bacteria: LKR and SDH in bacteria and its relationship to the plant and animal enzymes
FEBS Lett.
586
905-911
2012
Nostoc punctiforme, Ruegeria pomeroyi, Nostoc punctiforme ATCC 29133
brenda
Schmidt, D.; Rizzi, V.; Gaziola, S.A.; Medici, L.O.; Vincze, E.; Kozak, M.; Lea, P.J.; Azevedo, R.A.
Lysine metabolism in antisense C-hordein barley grains
Plant Physiol. Biochem.
87
73-83
2015
Hordeum vulgare
brenda
Wan, P.; Yuan, S.; Tang, Y.; Li, K.; Yang, L.; Fu, Q.; Li, G.
Pathways of amino acid degradation in Nilaparvata lugens (Stal) with special reference to lysine-ketoglutarate reductase/saccharopine dehydrogenase (LKR/SDH)
PLoS ONE
10
e0127789
2015
Nilaparvata lugens (A0A089MUZ6)
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