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1  an imine, which is reduced by NADPH to give saccharopine.
2 n the embryo along with an elevated level of saccharopine.
3 ) adds to the enzyme followed by addition of saccharopine.
4 es using analogues of AASA, L-glutamate, and saccharopine.
5                                              Saccharopine, a nonproteinogenic amino acid originally i
6 ly) with NAT1 N-acetylation activity whereas saccharopine abundance was strongly inversely correlated
7  an mdh3/gpd1Delta double mutant accumulates saccharopine and displays lysine bradytrophy.
8 -Kg, suggesting the existence of both E:NADH:saccharopine and E:NAD:saccharopine complexes.
9 ornithine were used as dead-end analogues of saccharopine and showed competitive inhibition vs saccha
10 aropine and showed competitive inhibition vs saccharopine and uncompetitive inhibition vs NADP.
11 charopine, while L-AASA is noncompetitive vs saccharopine and uncompetitive vs NADP.
12 e formation and excretion as fructoselysine, saccharopine, and Nepsilon-acetyllysine, lysine lead to
13 ccepted a proton from the secondary amine of saccharopine, and products are released.
14 accepts a proton from the secondary amine of saccharopine as it is oxidized.
15 direction of lysine formation, once NAD+ and saccharopine bind, a group with a pKa of 6.2 accepts a p
16 stence of both E:NADH:saccharopine and E:NAD:saccharopine complexes.
17                 Saccharopine reductase (SR) [saccharopine dehydrogenase (l-glutamate forming), EC 1.5
18                          Three structures of saccharopine dehydrogenase (l-lysine-forming) (SDH) have
19 ional enzyme, lysine ketoglutarate reductase/saccharopine dehydrogenase (LKR/SDH).
20 etoglutarate reductase (LKR, EC 1.5.1.8) and saccharopine dehydrogenase (SDH, ED 1.5.1.9) from an Ara
21                                              Saccharopine dehydrogenase [N6-(glutaryl-2)-L-lysine:NAD
22 lity of intraperoxisomal NAD(+) required for saccharopine dehydrogenase activity can be sustained by
23 tempt to define the substrate specificity of saccharopine dehydrogenase and to identify functional gr
24 In yeast, lysine-ketoglutarate reductase and saccharopine dehydrogenase are encoded by the LYS1 and L
25 osed of three domains with a fold similar to saccharopine dehydrogenase but with a distinct active si
26                                              Saccharopine dehydrogenase catalyzes the NAD-dependent o
27  have been measured for the histidine-tagged saccharopine dehydrogenase from Saccharomyces cerevisiae
28         Lysine biosynthesis is restored when saccharopine dehydrogenase is mislocalised to the cytoso
29 alyzed by lysine-ketoglutarate reductase and saccharopine dehydrogenase, respectively, resulting in t
30                          In the direction of saccharopine formation, data also suggest that, at high
31 amide adenine dinucleotide (NAD) followed by saccharopine in the physiologic reaction direction.
32                                              Saccharopine is noncompetitive versus lysine or alpha-Kg
33                                              Saccharopine is noncompetitive vs NADPH, alpha-AASA, and
34                        Product inhibition by saccharopine is uncompetitive versus NADH, suggesting a
35 is competitive vs NADP and noncompetitive vs saccharopine, L-glutamate is noncompetitive vs both NADP
36 ryo LKR/SDH suppression through crosses, the saccharopine level in embryo was reduced and resulted in
37  in which substrate (alpha-ketoglutarate and saccharopine) may bind.
38                          In the direction of saccharopine oxidation, N-oxalylglycine, L-pipecolic aci
39                          In the direction of saccharopine oxidation, NADPH is competitive vs NADP and
40                                          The saccharopine pathway intermediates and phosphorylated su
41                                              Saccharopine reductase (SR) [saccharopine dehydrogenase
42 tudies were carried out for histidine-tagged saccharopine reductase from Saccharomyces cerevisiae at
43 tes, namely, threonine, lysine, leucine, and saccharopine, that were associated with both PM(2.5) con
44                       Lysine is converted to saccharopine, through condensation with alpha-ketoglutar
45  H2O as it attacks the Schiff base carbon of saccharopine to form the carbinolamine intermediate.
46 ucleotide-dependent oxidative deamination of saccharopine to generate alpha-Kg and lysine using NAD+
47 s the NAD-dependent oxidative deamination of saccharopine to give l-lysine and alpha-ketoglutarate.
48 sis, the NAD(+)-dependent dehydrogenation of saccharopine to lysine, is another NAD(+)-dependent reac
49 glutamate is noncompetitive vs both NADP and saccharopine, while L-AASA is noncompetitive vs saccharo