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1 ibrium constants of the binding of substrate fructose 6-phosphate.
2 apparent cooperativity in the interaction of fructose 6-phosphate.
3 itive inhibitor for the allosteric activator fructose 6-phosphate.
4 conversion of fructose 1,6-bisphosphate into fructose 6-phosphate.
5 e interconversion of mannose 6-phosphate and fructose 6-phosphate.
6 isomerization of D-glucose 6-phosphate to D-fructose 6-phosphate.
7 ne might be a precursor to 3-amino-3-deoxy-D-fructose 6-phosphate.
8 donor substrates, namely l-erythrulose and d-fructose-6-phosphate.
9 isomerization of D-glucose-6-phosphate to D-fructose-6-phosphate.
10 terconversion of D-glucose-6-phosphate and D-fructose-6-phosphate.
11 ncentration and by addition of its substrate fructose-6-phosphate.
12 ical conditions proceeds to the formation of fructose-6-phosphate.
13 e interconversion of glucose-6-phosphate and fructose-6-phosphate.
14 lycerate, as well as glucose-6-phosphate and fructose-6-phosphate.
15 mes alcohol dehydrogenase and pyrophosphate, fructose 6-phosphate 1-phosphotransferase, and approxima
16 en developed using the enzyme pyrophosphate--fructose-6-phosphate 1-phosphotransferase (EC 2.7.1.90)
20 g of the Walker motif residues of rat testis fructose 6-phosphate, 2-kinase:fructose-2,6-bisphosphata
22 ptophan residues, of the bifunctional enzyme fructose 6-phosphate,2-kinase-fructose 2,6-bisphosphatas
26 -3 proteins, raising the question of whether fructose-6-phosphate,2-kinase/fructose-2,6-bisphosphatas
27 mmercially available TK substrates, namely d-fructose-6-phosphate a physiological donor and glycolald
28 the conversion of glucosamine-6-phosphate to fructose-6-phosphate, a reaction that under physiologica
29 The method utilizes the recently discovered fructose-6-phosphate aldolase (FSA), which is functional
30 om dihydroxyacetone and aminoethanol using D-fructose-6-phosphate aldolase and L-rhamnulose-1-phospha
33 nzyme for hexosamine biosynthesis, glutamine:fructose-6-phosphate amidotransferase (GFA) in human ske
36 g enzyme for hexosamine synthesis, glutamine:fructose-6-phosphate amidotransferase (GFA), specificall
38 e rate-limiting enzyme of the HBP, glutamine:fructose-6-phosphate amidotransferase (GFA), was overexp
44 to glucosamine through the enzyme glutamine:fructose-6-phosphate amidotransferase (GFAT) was blocked
45 with approximately 75% homology to glutamine-fructose-6-phosphate amidotransferase (GFAT) was termed
46 novirus-mediated overexpression of glutamine:fructose-6-phosphate amidotransferase (GFAT), the first
47 ted by azaserine, an inhibitor of glutamine: fructose-6-phosphate amidotransferase (GFAT), which is t
48 tance, we measured the activity of glutamine:fructose-6-phosphate amidotransferase (GFAT; rate-limiti
49 P) via regulation of expression of glutamine:fructose-6-phosphate amidotransferase 1 (GFAT1), the rat
50 e hexosamine biosynthesis pathway (glutamine:fructose-6-phosphate amidotransferase [GFA]) makes the c
51 enzyme in hexosamine biosynthesis (glutamine:fructose-6-phosphate amidotransferase [GFA]) was overexp
54 of the rate-limiting enzyme GFAT (glutamine:fructose-6-phosphate amidotransferase) did not protect a
56 eversed by antisense inhibition of glutamine:fructose-6-phosphate amidotransferase, the rate-limiting
59 glutamine, were determined to be 0.8 mm for fructose 6-phosphate and 1.2 mm for glutamine, which are
61 e, one could observe substrate inhibition by fructose 6-phosphate and apparent cooperativity in the i
63 monophosphorylated sugars, including beta-D-fructose 6-phosphate and beta-D-mannose 6-phosphate, a p
64 C8 backbone of MTL moiety is derived from D-fructose 6-phosphate and D-ribose 5-phosphate via a tran
66 ncrease in glucose 6-phosphate, no change in fructose 6-phosphate and fructose 1,6-diphosphate, an in
68 m values for the two substrates of reaction, fructose 6-phosphate and glutamine, were determined to b
69 hosphomannose isomerase, which interconverts fructose 6-phosphate and mannose 6-phosphate (Man-6-P),
70 maximal in the presence of divalent cations, fructose 6-phosphate and orthophosphate, which together
72 allowing independent bindings of substrates, fructose-6-phosphate and ATP, with higher affinities tha
73 ed to estimate the dissociation constants of fructose-6-phosphate and fructose-2,6-bisphosphate, whic
74 wo other maize AGPase allosteric activators (fructose-6-phosphate and glucose-6-phosphate) did not al
75 by ATP and (i) manno(fructo)kinase, to form fructose 6-phosphate, and (ii) phosphofructokinase, to f
78 synthesis and purification of the substrate, fructose 6-phosphate, and methods for a radiometric assa
79 ose 1-phosphate but not glucose 6-phosphate, fructose 6-phosphate, and sedoheptulose 7-phosphate as p
80 The dissociation constants of the substrate, fructose 6-phosphate, and the allosteric ligands, as wel
81 s of hexose phosphates (glucose-6-phosphate, fructose-6-phosphate, and fructose-1,6-bisphosphate) wer
82 trates including glyceraldehyde-3-phosphate, fructose-6-phosphate, and glucose-6-phosphate; (ii) has
83 xyacetone phosphate, glucose-6-phosphate and fructose-6-phosphate as additional CggR ligands that can
85 apparent Michaelis-Menten constant (K(m)) of fructose 6-phosphate at different temperatures and (ii)
88 products of the reaction (orthophosphate and fructose 6-phosphate) bind to the active site in a manne
90 e conversion of fructose 1,6-bisphosphate to fructose 6-phosphate by a fructose bisphosphatase (FBPas
91 us taken into the cells is phosphorylated to fructose 6-phosphate by ATP and a cytosolic fructo(manno
92 phosphate) and MPI (mannose 6-phosphate <--> fructose 6-phosphate) deficiencies reduce the metabolic
94 ition to its function as the proton donor to fructose-6-phosphate during formation of the transient p
95 oxal resulted in complete desensitization to fructose 6-phosphate (F6P) activation, and partial desen
96 lex with three zinc cations and the products fructose 6-phosphate (F6P) and phosphate (Pi) reveals lo
97 version of D-glucose 6-phosphate (G6P) and D-fructose 6-phosphate (F6P) and plays important roles in
99 interconverts glucose 6-phosphate (G6P) and fructose 6-phosphate (F6P) but, outside the cell, is a m
100 not the Zn(2+) complexes), the 1-OH group of fructose 6-phosphate (F6P) coordinates to the metal at s
101 inase (PFK) catalyzes the phosphorylation of fructose 6-phosphate (F6P) to give fructose 1,6-bisphosp
105 constants were determined for the activator fructose-6-phosphate (F6P) and substrate adenosine 5'-tr
106 ), intermediates (glucose-6-phosphate (G6P), fructose-6-phosphate (F6P), fructose-1,6-bisphosphate (F
108 0) fructose-1,6-bisphosphate (FBP; 1 mm) and fructose-6-phosphate (F6P; 1 mm) caused a transient incr
109 ree-step biochemical conversion of GlcNAc to fructose 6-phosphate first described in Escherichia coli
110 phoenzyme intermediate and release of beta-D-fructose 6-phosphate, followed by hydrolysis of the phos
111 place Mg2+ from site 3 and the 1-OH group of fructose 6-phosphate from in-line geometry with respect
112 e active pocket, slowing down the release of fructose-6-phosphate from the phosphoenzyme intermediate
113 th respect to the total free energy of MgADP/fructose 6-phosphate (Fru-6-P) activation in the control
114 hospho(enol)pyruvate (PEP) on the binding of fructose 6-phosphate (Fru-6-P) and MgATP to phosphofruct
115 ings between these ligands and the substrate fructose 6-phosphate (Fru-6-P) have also been determined
116 cat) = 250 s(-)1) that binds the cosubstrate fructose 6-phosphate (Fru-6-P) with relatively low affin
117 fied to block binding of both the substrate, fructose 6-phosphate (Fru-6-P), and the allosteric inhib
118 (EcPFK) that interact with bound substrate, fructose 6-phosphate (Fru-6-P), are examined for their p
120 hosphoenolpyruvate (PEP), and the substrate, fructose 6-phosphate (Fru-6-P), in phosphofructokinase f
121 analysis of the three-ligand interaction of fructose 6-phosphate (Fru-6-P), phosphoenolpyruvate (PEP
126 me, catalyzing the interconversion of beta-D-fructose- 6-phosphate (Fru-6-P) and fructose-2,6-bisphos
130 s a 3-fold smaller K(0.5) for the substrate, fructose-6-phosphate (Fru-6-P), as compared to the wild-
131 r that could phosphorylate either glucose or fructose 6-phosphate (fructose-6-P) as a substrate to a
132 from l-glutamine to the acceptor substrate, fructose 6-phosphate, generating the products glucosamin
134 e interconversion of glucose 6-phosphate and fructose 6-phosphate, has been suggested to operate via
135 ression enhanced glucose 1-phosphate but not fructose 6-phosphate hydrolysis in intact microsomes, pr
136 se 6-phosphates d-allulose 6-phosphate and d-fructose 6-phosphate in a catabolic pathway for d-allose
138 se, the feedback inhibition of hexokinase by fructose-6-phosphate, in a first refinement of the model
140 t the value of the dissociation constant for fructose 6-phosphate is 3.3 (+/-0.5) x 10(-7) m, approxi
142 osamine biosynthesis pathway (HBP), in which fructose-6-phosphate is converted to glucosamine 6-phosp
143 accumulation of the glycolytic intermediate fructose 6-phosphate, leading to engagement of the hexos
144 2-fold elevation in glucose 6-phosphate and fructose 6-phosphate levels, whereas fructose 1,6-bispho
145 und mannose and fucose residues stemmed from fructose 6-phosphate, not glucose 1-phosphate; therefore
146 ransaldol reaction catalyzed by LmbR using D-fructose 6-phosphate or D-sedoheptulose 7-phosphate as t
147 fector preference from 3-phosphoglycerate to fructose-6 phosphate or fructose-1,6-bis-phosphate, effe
148 amino group from the L-glutamine amide to D-fructose 6-phosphate, producing glutamic acid and glucos
149 ddition of glycolytic compounds like G6P and fructose-6-phosphate rescues the alphaMG growth defect o
151 se 1-phosphate <--> glucose 6-phosphate <--> fructose 6-phosphate, showed a large decrease in 3H:14C
152 tructure shows an EDTA molecule bound to the fructose-6-phosphate site of the 6-phosphofructo-2-kinas
156 y activated by both fructose-1-phosphate and fructose-6-phosphate; the strength of the activation res
158 te pathway to glyceraldehyde 3-phosphate and fructose 6-phosphate, thus bypassing fructose-1,6-bispho
160 tivator, MgADP, also altered the affinity of fructose 6-phosphate to the enzyme by forming a ternary
162 catalyzes the ATP-independent conversion of fructose-6-phosphate to fructose-1,6-bisphosphate in gly
167 with the 2-Pase domain to secure binding of fructose-6-phosphate to the active pocket, slowing down
168 thway, which splits xylulose-5-phosphate (or fructose-6-phosphate) to acetate precursor acetyl phosph
169 f the corresponding human gene for glutamine-fructose-6-phosphate transaminase (GFPT), located at 2p1
171 Mutations in the gene encoding glutamine-fructose-6-phosphate transaminase 1 (GFPT1) cause the ne
174 he formation of glucosamine 6-phosphate from fructose 6-phosphate using glutamine as the ammonia sour
175 erization of d-tagatose 6-phosphate C-4 to d-fructose 6-phosphate via a member of Pfam family PF08013
180 from exchange of the lower three carbons of fructose-6-phosphate with unlabeled three-carbon precurs
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