EC Number |
General Information |
Reference |
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1.5.1.10 | 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 |
-, 765188 |
1.5.1.10 | evolution |
the enzyme domains and activities LKR and SDH belong to a single about 120 kDa bifunctional polypeptide |
763097 |
1.5.1.10 | 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 |
763097 |
1.5.1.10 | malfunction |
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 |
763097 |
1.5.1.10 | 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 |
763097 |
1.5.1.10 | 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 |
763097 |
1.5.1.10 | 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 |
-, 765188 |
1.5.1.10 | 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 |
763097 |
1.5.1.10 | physiological function |
saccharopine reductase catalyzes the reductive amination of L-alpha-aminoadipate-delta-semialdehyde with L-glutamate to give saccharopine |
741780 |