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1  interconversion of ribulose 5-phosphate and arabinose 5-phosphate.
2 t catalyzes the aldol-type condensation of D-arabinose 5-phosphate (A 5-P) and phosphoenolpyruvate (P
3 nthase) that catalyzes the condensation of D-arabinose 5-phosphate (A 5-P) with phosphoenolpyruvate (
4 s, pyrophosphate, a TK cofactor analog and d-arabinose-5-phosphate, a substrate analog.
5 pyruvate (PEP) and the corresponding aldose: arabinose 5-phosphate (A5P) and erythrose 4-phosphate (E
6 KDO8P synthase catalyzes the condensation of arabinose 5-phosphate (A5P) and phosphoenolpyruvate (PEP
7 thase (KDO8PS) catalyzes the condensation of arabinose 5-phosphate (A5P) and phosphoenolpyruvate (PEP
8 DO8P) synthase catalyzes the condensation of arabinose 5-phosphate (A5P) and phosphoenolpyruvate (PEP
9 incubated with phosphoenolpyruvate (PEP) and arabinose 5-phosphate (A5P) shows the formed product, 3-
10 ndensation of phosphoenolpyruvate (PEP) with arabinose 5-phosphate (A5P) to form KDO8P and inorganic
11 densation of phosphoenolpyruvate (PEP) and D-arabinose 5-phosphate (A5P) to produce KDO8P and inorgan
12 s combinations of phosphoenolpyruvate (PEP), arabinose 5-phosphate (A5P), and erythrose 4-phosphate (
13 rsion of d-ribulose 5-phosphate (Ru5P) and d-arabinose 5-phosphate (A5P), has been identified from th
14  the conversion of ribulose 5-phosphate into arabinose 5-phosphate (A5P), the first committed step in
15 nthase, binds in a manner similar to that of arabinose 5-phosphate (A5P), which is the natural substr
16  between D-ribulose 5-phosphate (Ru5P) and D-arabinose 5-phosphate (A5P).
17 that the condensation step between PEP and D-arabinose-5-phosphate (A5P) should proceed in a stepwise
18 ubstrates, 2-phosphoenolpyruvate (PEP) and d-arabinose-5-phosphate (A5P), are also in space group I23
19 o an increase in K(m) for both substrates, d-arabinose 5-phosphate and phosphoenolpyruvate.
20                  Uncompetitive inhibition by arabinose 5-phosphate (Ara5P), a dead-end inhibitory ana
21 e 8-phosphate from phosphoenolpyruvate and D-arabinose 5-phosphate as determined from (1)H-nuclear ma
22 n phosphorylated monosaccharide analogues, D-arabinose 5-phosphate, D-ribose 5-phosphate, and 2-deoxy
23 quence similarity between GutQ and KdsD, a D-arabinose 5-phosphate isomerase (API) from the 3-deoxy-D
24                                              Arabinose 5-phosphate isomerase (API), encoded by Y. pes
25                          A gene encoding for arabinose 5-phosphate isomerase (API), which catalyzes t
26 combinant c3406 protein, found it to possess arabinose 5-phosphate isomerase activity, and characteri
27                     KpsF was shown to be the arabinose-5-phosphate isomerase, an enzyme not previousl
28 nt homology to the sugar isomerase domain of arabinose 5-phosphate isomerases but lacking the tandem
29 ine beta-synthase domains found in the other arabinose 5-phosphate isomerases of E. coli.
30                                              Arabinose-5-phosphate isomerases (APIs) catalyze the int
31  reactions between phosphoenolpyruvate and d-arabinose 5-phosphate or d-erythrose 4-phosphate, respec
32 erconversion of d-ribulose-5-phosphate and D-arabinose-5-phosphate, the first step in the biosynthesi
33 et condensation of phosphoenolpyruvate and d-arabinose 5-phosphate to form KDO8P and inorganic phosph

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