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1 s susceptible to S-cyanylation that included SEDOHEPTULOSE 1,7-BISPHOSPHATASE (SBPase), the PEPTIDYL-
2 nnection cellulolytic clostridia rely on the sedoheptulose 1,7-bisphosphate (SBP) pathway, using pyro
3 cycle enzymes triose-phosphate isomerase and sedoheptulose 1,7-bisphosphate phosphatase.
4  to accumulation of fructose 1-phosphate and sedoheptulose 1-phosphate but not glucose 6-phosphate, f
5 ponding labels into fructose 1-phosphate and sedoheptulose 1-phosphate in FK866-treated cells.
6 oxyacetone phosphate and glyceraldehyde, and sedoheptulose 1-phosphate was derived from dihydroxyacet
7 e dark, and in the dark with the addition of sedoheptulose-1,7-bisphosphatase (normally inactive in t
8 ven enzymes that participate in the pathway, sedoheptulose-1,7-bisphosphatase (SBPase) is expressed i
9 atory members of the cycle, our knowledge of sedoheptulose-1,7-bisphosphatase (SBPase) is particularl
10 d to sedoheptulose-7-phosphate by the enzyme sedoheptulose-1,7-bisphosphatase (SHB17), whose activity
11  chloroplast fructose-1,6-bisphosphatase and sedoheptulose-1,7-bisphosphatase activity showed that th
12 o calculate the flux control coefficients of sedoheptulose-1,7-bisphosphatase over photosynthetic ass
13                    The effect of introducing sedoheptulose-1,7-bisphosphatase to the system are relat
14 PCOP enzymes and underinvestment in Rubisco, sedoheptulose-1,7-bisphosphatase, and fructose-1,6-bisph
15 ich the activity of the Calvin cycle enzyme, sedoheptulose-1,7-bisphosphatase, is reduced by an antis
16 ydryl groups of fructose-1,6-bisphosphatase, sedoheptulose-1,7-bisphosphatase, phosphoribulokinase, N
17 o-autotrophs and catalyzes the hydrolysis of sedoheptulose-1,7-bisphosphate (SBP) to sedoheptulose-7-
18 e crystal structure of Shb17 in complex with sedoheptulose-1,7-bisphosphate reveals that the substrat
19  of the seven-carbon bisphosphorylated sugar sedoheptulose-1,7-bisphosphate.
20 e levels of these enzyme substrates, such as sedoheptulose-6-phosphate (pentose phosphate pathway) an
21 nerated from an open-chain C(7) precursor, D-sedoheptulose 7-phosphate (5), by a DHQ synthase-like cy
22     In this reversible pathway, PFK converts sedoheptulose 7-phosphate (S7P) to SBP, after which fruc
23 ucose 6-phosphate, fructose 6-phosphate, and sedoheptulose 7-phosphate as previously thought.
24 ed by LmbR using D-fructose 6-phosphate or D-sedoheptulose 7-phosphate as the C(3) donor and D-ribose
25                                              Sedoheptulose 7-phosphate cyclases are enzymes that util
26 iosynthetic step catalyzes the conversion of sedoheptulose 7-phosphate into d-glycero-d-manno-heptose
27     These enzymes catalyze the conversion of sedoheptulose 7-phosphate to 2-epi-valiolone, which is p
28 -regulation of cell wall biosynthesis (via D-sedoheptulose 7-phosphate) and nucleotide metabolism (vi
29 ers was characterized by the accumulation of sedoheptulose 7-phosphate, failure to recycle ribose 5-p
30  the pentose phosphate pathway intermediate, sedoheptulose 7-phosphate, to generate cyclic precursors
31 es are ultimately derived from a C(7) sugar, sedoheptulose 7-phosphate, which is cyclized to 2-epi-5-
32 s of sedoheptulose-1,7-bisphosphate (SBP) to sedoheptulose-7-phosphate (S7P).
33  sedoheptulose bisphosphate is hydrolyzed to sedoheptulose-7-phosphate by the enzyme sedoheptulose-1,
34 e is GmhA, which catalyzes the conversion of sedoheptulose-7-phosphate into D-glycero-D-manno-heptopy
35                                              Sedoheptulose-7-phosphate is ultimately converted by kno
36 lites such as fructose-6-phosphate, glycine, sedoheptulose-7-phosphate, and Ser.
37 ting for their specificity for seven-carbon (sedoheptulose) and six-carbon (fructose) sugar bisphosph
38 l structure of the Chlamydomonas reinhardtii sedoheptulose bisphosphatase (EC 3.1.3.37) there are two
39  Examination of the redox modulation of this sedoheptulose bisphosphatase confirms that it resembles
40 boxylase/oxygenase, phosphoribulokinase, and sedoheptulose bisphosphatase.
41  in modulation in the algal and higher plant sedoheptulose bisphosphatases.
42                A metabolically inert pool of sedoheptulose bisphosphate can slowly equilibrate keepin
43             In the pathway's committed step, sedoheptulose bisphosphate is hydrolyzed to sedoheptulos
44  can slowly equilibrate keeping the label in sedoheptulose lower than in other stromal metabolites.