1.5.1.10: saccharopine dehydrogenase (NADP+, L-glutamate-forming)
This is an abbreviated version!
For detailed information about saccharopine dehydrogenase (NADP+, L-glutamate-forming), go to the full flat file.
Word Map on EC 1.5.1.10
-
1.5.1.10
-
alpha-aminoadipate
-
auxotrophs
-
magnaporthe
-
grisea
-
homocitrate
-
pipecolic
-
swainsonine
-
homoisocitrate
-
piperideine-6-carboxylic
-
chrysogenum
-
unlinked
-
rossmann
-
penicillium
-
ph-rate
-
endophytic
-
embedding
-
6-dehydrogenase
-
substrate-assisted
-
seven-stranded
-
diaminopimelate
-
oxytropis
-
acid-base
-
leaky
-
all-helical
-
anisotropic
-
l-pipecolate
-
dl-alpha-aminoadipate
-
gene-enzyme
- 1.5.1.10
- alpha-aminoadipate
-
auxotrophs
-
magnaporthe
- grisea
- homocitrate
-
pipecolic
- swainsonine
- homoisocitrate
-
piperideine-6-carboxylic
- chrysogenum
-
unlinked
-
rossmann
-
penicillium
-
ph-rate
-
endophytic
-
embedding
-
6-dehydrogenase
-
substrate-assisted
-
seven-stranded
- diaminopimelate
- oxytropis
-
acid-base
-
leaky
-
all-helical
-
anisotropic
- l-pipecolate
- dl-alpha-aminoadipate
-
gene-enzyme
Reaction
Synonyms
aminoadipate semialdehyde-glutamate reductase, aminoadipic semialdehyde-glutamate reductase, aminoadipic semialdehyde-glutamic reductase, ASS, dehydrogenase, saccharopine (nicotinamide adenine dinucleotide phosphate, glutamate-forming), epsilon-N-(L-glutaryl-2)-L-lysine:NAD+(P) oxidoreductase (L-2-aminoadipate-semialdehyde forming), LKR/SDH, lysine-ketoglutarate reductase/saccharopine dehydrogenase, nSpe-Sdh, saccharopine dehydrogenase, saccharopine dehydrogenase (L-glutamate forming), saccharopine reductase, SDH, spermidine synthase-saccharopine dehydrogenase, SR1
ECTree
Advanced search results
General Information
General Information on EC 1.5.1.10 - saccharopine dehydrogenase (NADP+, L-glutamate-forming)
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
evolution
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
metabolism
physiological function
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
-
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
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
-