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1 n the embryo along with an elevated level of saccharopine.
2 ) adds to the enzyme followed by addition of saccharopine.
3 es using analogues of AASA, L-glutamate, and saccharopine.
4 an imine, which is reduced by NADPH to give saccharopine.
7 ornithine were used as dead-end analogues of saccharopine and showed competitive inhibition vs saccha
12 direction of lysine formation, once NAD+ and saccharopine bind, a group with a pKa of 6.2 accepts a p
17 etoglutarate reductase (LKR, EC 1.5.1.8) and saccharopine dehydrogenase (SDH, ED 1.5.1.9) from an Ara
19 lity of intraperoxisomal NAD(+) required for saccharopine dehydrogenase activity can be sustained by
20 tempt to define the substrate specificity of saccharopine dehydrogenase and to identify functional gr
21 In yeast, lysine-ketoglutarate reductase and saccharopine dehydrogenase are encoded by the LYS1 and L
23 have been measured for the histidine-tagged saccharopine dehydrogenase from Saccharomyces cerevisiae
25 alyzed by lysine-ketoglutarate reductase and saccharopine dehydrogenase, respectively, resulting in t
31 is competitive vs NADP and noncompetitive vs saccharopine, L-glutamate is noncompetitive vs both NADP
32 ryo LKR/SDH suppression through crosses, the saccharopine level in embryo was reduced and resulted in
37 tudies were carried out for histidine-tagged saccharopine reductase from Saccharomyces cerevisiae at
40 ucleotide-dependent oxidative deamination of saccharopine to generate alpha-Kg and lysine using NAD+
41 s the NAD-dependent oxidative deamination of saccharopine to give l-lysine and alpha-ketoglutarate.
42 sis, the NAD(+)-dependent dehydrogenation of saccharopine to lysine, is another NAD(+)-dependent reac
43 glutamate is noncompetitive vs both NADP and saccharopine, while L-AASA is noncompetitive vs saccharo
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