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1 ne might be a precursor to 3-amino-3-deoxy-D-fructose 6-phosphate.
2 ibrium constants of the binding of substrate fructose 6-phosphate.
3 apparent cooperativity in the interaction of fructose 6-phosphate.
4 itive inhibitor for the allosteric activator fructose 6-phosphate.
5 conversion of fructose 1,6-bisphosphate into fructose 6-phosphate.
6 e interconversion of mannose 6-phosphate and fructose 6-phosphate.
7  isomerization of D-glucose 6-phosphate to 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 ical conditions proceeds to the formation of fructose-6-phosphate.
12 e interconversion of glucose-6-phosphate and fructose-6-phosphate.
13 ncentration and by addition of its substrate 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)
17                      Pyrophosphate-dependent fructose-6-phosphate 1-phosphotransferase (PFP) catalyze
18        Constitutive expression of FBPase and fructose-6-phosphate-1-kinase coupled with the absence o
19                       A bifunctional enzyme, fructose-6-phosphate 2-kinase-fructose 2, 6-bisphosphata
20 g of the Walker motif residues of rat testis fructose 6-phosphate, 2-kinase:fructose-2,6-bisphosphata
21                       A bifunctional enzyme, fructose-6-phosphate, 2-kinase:fructose-2, 6-bisphosphat
22 ptophan residues, of the bifunctional enzyme fructose 6-phosphate,2-kinase-fructose 2,6-bisphosphatas
23                                              Fructose-6-phosphate,2-kinase and fructose-2,6-bisphosph
24                       A bifunctional enzyme, fructose-6-phosphate,2-kinase/fructose 2, 6-bisphosphata
25                                              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                      Glucose-6-phosphate and fructose-6-phosphate accumulated in the roots under sing
30  in high yields and up to gram scale using d-fructose-6-phosphate aldolase (EcFSA).
31  with a cascade reaction combining FLS and d-fructose-6-phosphate aldolase (FSA) A129S variant.
32  The method utilizes the recently discovered fructose-6-phosphate aldolase (FSA), which is functional
33 om dihydroxyacetone and aminoethanol using D-fructose-6-phosphate aldolase and L-rhamnulose-1-phospha
34                    The activity of glutamine:fructose-6-phosphate amido-transferase (GFAT), the first
35 athway, which is controlled by the glutamine:fructose-6-phosphate amidotransfera-se (GFAT).
36            Specific inhibitors of glutamine: fructose 6-phosphate amidotransferase (GFAT), an enzyme
37 creased expression and activity of glutamine fructose 6-phosphate amidotransferase (GFAT), the enzyme
38 ation of the rate limiting enzyme, glutamine-fructose 6-phosphate amidotransferase 1 (GFAT1).
39 nzyme for hexosamine biosynthesis, glutamine:fructose-6-phosphate amidotransferase (GFA) in human ske
40                                    Glutamine:fructose-6-phosphate amidotransferase (GFA) is the rate-
41                                    Glutamine:fructose-6-phosphate amidotransferase (GFA) is the rate-
42 g enzyme for hexosamine synthesis, glutamine:fructose-6-phosphate amidotransferase (GFA), specificall
43                                    Glutamine:fructose-6-phosphate amidotransferase (GFA), the first a
44 e rate-limiting enzyme of the HBP, glutamine:fructose-6-phosphate amidotransferase (GFA), was overexp
45 hosphate by the rate-liming enzyme glutamine:fructose-6-phosphate amidotransferase (GFA).
46                                    Glutamine-fructose-6-phosphate amidotransferase (GFAT) catalyzes t
47                                    Glutamine:fructose-6-phosphate amidotransferase (GFAT) catalyzes t
48                                    Glutamine:fructose-6-phosphate amidotransferase (GFAT) is the enzy
49                                    Glutamine:fructose-6-phosphate amidotransferase (GFAT) is the rate
50  to glucosamine through the enzyme glutamine:fructose-6-phosphate amidotransferase (GFAT) was blocked
51 with approximately 75% homology to glutamine-fructose-6-phosphate amidotransferase (GFAT) was termed
52 novirus-mediated overexpression of glutamine:fructose-6-phosphate amidotransferase (GFAT), the first
53 ted by azaserine, an inhibitor of glutamine: fructose-6-phosphate amidotransferase (GFAT), which is t
54 tance, we measured the activity of glutamine:fructose-6-phosphate amidotransferase (GFAT; rate-limiti
55 Mechanistically, we identify the glucosamine:fructose-6-phosphate amidotransferase (GFPT) among the s
56 rolled by its rate-limiting enzyme glutamine fructose-6-phosphate amidotransferase (GFPT/GFAT) that i
57 P) via regulation of expression of glutamine:fructose-6-phosphate amidotransferase 1 (GFAT1), the rat
58  mTORC2-modulated metabolic enzyme glutamine fructose-6-phosphate amidotransferase 1 at Ser243.
59           Overexpression of Gfat1 (glutamine:fructose-6-phosphate amidotransferase 1), the rate-limit
60 CR revealed that the mRNAs of Akt, glutamine fructose-6-phosphate amidotransferase 1, and the mTORC2
61 e hexosamine biosynthesis pathway (glutamine:fructose-6-phosphate amidotransferase [GFA]) makes the c
62 enzyme in hexosamine biosynthesis (glutamine:fructose-6-phosphate amidotransferase [GFA]) was overexp
63                       Azaserine, a glutamine:fructose-6-phosphate amidotransferase inhibitor, reverse
64                                    Glutamine:fructose-6-phosphate amidotransferase(GFAT) is the rate-
65  of the rate-limiting enzyme GFAT (glutamine:fructose-6-phosphate amidotransferase) did not protect a
66  enzyme in the hexosamine pathway (glutamine:fructose-6-phosphate amidotransferase).
67 eversed by antisense inhibition of glutamine:fructose-6-phosphate amidotransferase, the rate-limiting
68 N-acetylglucosaminyl hydrolase, or glutamine fructose-6-phosphate amidotransferase.
69                                    Glutamine-fructose-6-phosphate aminotransferase (Gfa1) is an essen
70 ichia coli and found that one, the glutamine fructose-6-phosphate aminotransferase (GFAT) of glucosam
71 lation, abundance of OGT, OGA, and glutamine:fructose-6-phosphate aminotransferase (GFAT2), activity
72 that T cell-specific deficiency in glutamine:fructose-6-phosphate aminotransferase 1 (GFAT1), the rat
73  first enzyme in chitin synthesis (glutamine fructose-6-phosphate aminotransferase) is reported.
74  glutamine, were determined to be 0.8 mm for fructose 6-phosphate and 1.2 mm for glutamine, which are
75 t with other glycolytic metabolites, such as fructose 6-phosphate and 3-phosphoglycerate, impaired me
76      Glucosamine 6-phosphate is converted to fructose 6-phosphate and ammonia by the action of the en
77 e, one could observe substrate inhibition by fructose 6-phosphate and apparent cooperativity in the i
78 e was a mixed inhibitor with respect to both fructose 6-phosphate and ATP.
79  monophosphorylated sugars, including beta-D-fructose 6-phosphate and beta-D-mannose 6-phosphate, a p
80  C8 backbone of MTL moiety is derived from D-fructose 6-phosphate and D-ribose 5-phosphate via a tran
81 sphosphatases (PFKFB1-4), which interconvert fructose 6-phosphate and Fru-2,6-BP.
82 ncrease in glucose 6-phosphate, no change in fructose 6-phosphate and fructose 1,6-diphosphate, an in
83                                         Both fructose 6-phosphate and glutamine protect the enzyme fr
84 m values for the two substrates of reaction, fructose 6-phosphate and glutamine, were determined to b
85 hosphomannose isomerase, which interconverts fructose 6-phosphate and mannose 6-phosphate (Man-6-P),
86 maximal in the presence of divalent cations, fructose 6-phosphate and orthophosphate, which together
87       Diabetes elevated glucose 6-phosphate, fructose 6-phosphate and oxidised (NAD+ and NADP+) and r
88 allowing independent bindings of substrates, fructose-6-phosphate and ATP, with higher affinities tha
89 ed to estimate the dissociation constants of fructose-6-phosphate and fructose-2,6-bisphosphate, whic
90 wo other maize AGPase allosteric activators (fructose-6-phosphate and glucose-6-phosphate) did not al
91  by ATP and (i) manno(fructo)kinase, to form fructose 6-phosphate, and (ii) phosphofructokinase, to f
92  mutase interconverting glucose 6-phosphate, fructose 6-phosphate, and glucose 1-phosphate.
93  mannose 6-phosphate, galactose 6-phosphate, fructose 6-phosphate, and inorganic phosphate.
94 synthesis and purification of the substrate, fructose 6-phosphate, and methods for a radiometric assa
95 ose 1-phosphate but not glucose 6-phosphate, fructose 6-phosphate, and sedoheptulose 7-phosphate as p
96 The dissociation constants of the substrate, fructose 6-phosphate, and the allosteric ligands, as wel
97 s of hexose phosphates (glucose-6-phosphate, fructose-6-phosphate, and fructose-1,6-bisphosphate) wer
98 trates including glyceraldehyde-3-phosphate, fructose-6-phosphate, and glucose-6-phosphate; (ii) has
99 xyacetone phosphate, glucose-6-phosphate and fructose-6-phosphate as additional CggR ligands that can
100 se 6-phosphate at 1.16 A resolution and with fructose 6-phosphate at 1.5 A resolution.
101 apparent Michaelis-Menten constant (K(m)) of fructose 6-phosphate at different temperatures and (ii)
102 ps of the glycolysis: the phosphorylation of fructose 6-phosphate at position 1.
103 xed with the cyclic form of its substrate, D-fructose 6-phosphate, at 2.1 A resolution.
104 products of the reaction (orthophosphate and fructose 6-phosphate) bind to the active site in a manne
105                               In the case of fructose-6-phosphate binding, the increased anisotropy w
106 e conversion of fructose 1,6-bisphosphate to fructose 6-phosphate by a fructose bisphosphatase (FBPas
107 us taken into the cells is phosphorylated to fructose 6-phosphate by ATP and a cytosolic fructo(manno
108 phosphate) and MPI (mannose 6-phosphate <--> fructose 6-phosphate) deficiencies reduce the metabolic
109                      Protection studies with fructose 6-phosphate demonstrate that the value of the d
110         The product of both enzymes, 1-deoxy-fructose-6-phosphate (DF6P), is then cleaved by the aldo
111 ition to its function as the proton donor to fructose-6-phosphate during formation of the transient p
112 oxal resulted in complete desensitization to fructose 6-phosphate (F6P) activation, and partial desen
113 lex with three zinc cations and the products fructose 6-phosphate (F6P) and phosphate (Pi) reveals lo
114 version of D-glucose 6-phosphate (G6P) and D-fructose 6-phosphate (F6P) and plays important roles in
115 bacterium tumefaciens enzyme is activated by fructose 6-phosphate (F6P) and pyruvate.
116  interconverts glucose 6-phosphate (G6P) and fructose 6-phosphate (F6P) but, outside the cell, is a m
117 not the Zn(2+) complexes), the 1-OH group of fructose 6-phosphate (F6P) coordinates to the metal at s
118                  Finally, phosphorylation of fructose 6-phosphate (F6P) in the cytosol can allow some
119 inase (PFK) catalyzes the phosphorylation of fructose 6-phosphate (F6P) to give fructose 1,6-bisphosp
120 finities for S7P and the canonical substrate fructose 6-phosphate (F6P).
121 y covalent binding of the enzyme substrate d-fructose 6-phosphate (F6P).
122  ordered mechanism with MgATP binding before fructose 6-phosphate (F6P).
123 rconversion of glucose 6-phosphate (G6P) and fructose 6-phosphate (F6P).
124  constants were determined for the activator fructose-6-phosphate (F6P) and substrate adenosine 5'-tr
125 le for members of this family, none exhibits fructose-6-phosphate (F6P) at the active site.
126 ), intermediates (glucose-6-phosphate (G6P), fructose-6-phosphate (F6P), fructose-1,6-bisphosphate (F
127  pair, which enhances methanol conversion to fructose-6-phosphate (F6P).
128 0) fructose-1,6-bisphosphate (FBP; 1 mm) and fructose-6-phosphate (F6P; 1 mm) caused a transient incr
129 ree-step biochemical conversion of GlcNAc to fructose 6-phosphate first described in Escherichia coli
130 phoenzyme intermediate and release of beta-D-fructose 6-phosphate, followed by hydrolysis of the phos
131 place Mg2+ from site 3 and the 1-OH group of fructose 6-phosphate from in-line geometry with respect
132 e active pocket, slowing down the release of fructose-6-phosphate from the phosphoenzyme intermediate
133 th respect to the total free energy of MgADP/fructose 6-phosphate (Fru-6-P) activation in the control
134 hospho(enol)pyruvate (PEP) on the binding of fructose 6-phosphate (Fru-6-P) and MgATP to phosphofruct
135 ings between these ligands and the substrate fructose 6-phosphate (Fru-6-P) have also been determined
136 cat) = 250 s(-)1) that binds the cosubstrate fructose 6-phosphate (Fru-6-P) with relatively low affin
137 fied to block binding of both the substrate, fructose 6-phosphate (Fru-6-P), and the allosteric inhib
138  (EcPFK) that interact with bound substrate, fructose 6-phosphate (Fru-6-P), are examined for their p
139                               The substrate, fructose 6-phosphate (Fru-6-P), binds along the other di
140 hosphoenolpyruvate (PEP), and the substrate, fructose 6-phosphate (Fru-6-P), in phosphofructokinase f
141  analysis of the three-ligand interaction of fructose 6-phosphate (Fru-6-P), phosphoenolpyruvate (PEP
142 cherichia coli phosphofructokinase (PFK) for fructose 6-phosphate (Fru-6-P).
143  ability of the enzyme to bind the substrate fructose 6-phosphate (Fru-6-P).
144 nversion of glucose 6-phosphate (Glc-6-P) to fructose 6-phosphate (Fru-6-P).
145 ely low affinity for the acceptor substrate, fructose 6-phosphate (Fru-6-P, K(m) 0.2-1 mm).
146 me, catalyzing the interconversion of beta-D-fructose- 6-phosphate (Fru-6-P) and fructose-2,6-bisphos
147 four active sites, which bind the substrates fructose-6-phosphate (Fru-6-P) and MgATP.
148 strong direct interaction between AMPPCP and fructose-6-phosphate (Fru-6-P) is found.
149               The affinity for the substrate fructose-6-phosphate (Fru-6-P) of a single wild-type act
150 s a 3-fold smaller K(0.5) for the substrate, fructose-6-phosphate (Fru-6-P), as compared to the wild-
151 r that could phosphorylate either glucose or fructose 6-phosphate (fructose-6-P) as a substrate to a
152  from l-glutamine to the acceptor substrate, fructose 6-phosphate, generating the products glucosamin
153 ons for the synthesis of metabolites such as fructose-6-phosphate, glycine, sedoheptulose-7-phosphate
154                            3-Amino-3-deoxy-D-fructose 6-phosphate has previously been demonstrated to
155 e interconversion of glucose 6-phosphate and fructose 6-phosphate, has been suggested to operate via
156 ression enhanced glucose 1-phosphate but not fructose 6-phosphate hydrolysis in intact microsomes, pr
157 se 6-phosphates d-allulose 6-phosphate and d-fructose 6-phosphate in a catabolic pathway for d-allose
158 as well as fructose-1,6-bisphosphate but not fructose 6-phosphate in vitro.
159 se, the feedback inhibition of hexokinase by fructose-6-phosphate, in a first refinement of the model
160     In addition, hGFAT2 is able to isomerize fructose-6-phosphate into glucose-6-phosphate even in th
161 insulin resistance by increasing the flux of fructose-6-phosphate into the hexosamine pathway.
162 t the value of the dissociation constant for fructose 6-phosphate is 3.3 (+/-0.5) x 10(-7) m, approxi
163                  In fact, compared to 3-PGA, fructose-6-phosphate is a more efficient activator in tw
164 osamine biosynthesis pathway (HBP), in which fructose-6-phosphate is converted to glucosamine 6-phosp
165  accumulation of the glycolytic intermediate fructose 6-phosphate, leading to engagement of the hexos
166  2-fold elevation in glucose 6-phosphate and fructose 6-phosphate levels, whereas fructose 1,6-bispho
167 und mannose and fucose residues stemmed from fructose 6-phosphate, not glucose 1-phosphate; therefore
168 ransaldol reaction catalyzed by LmbR using D-fructose 6-phosphate or D-sedoheptulose 7-phosphate as t
169 fector preference from 3-phosphoglycerate to fructose-6 phosphate or fructose-1,6-bis-phosphate, effe
170  amino group from the L-glutamine amide to D-fructose 6-phosphate, producing glutamic acid and glucos
171 ddition of glycolytic compounds like G6P and fructose-6-phosphate rescues the alphaMG growth defect o
172                               The binding of fructose-6-phosphate resulted in a significant increase
173 -dependent fructose uptake and catabolism to fructose 6-phosphate, rewiring microglial metabolism tow
174 se 1-phosphate <--> glucose 6-phosphate <--> fructose 6-phosphate, showed a large decrease in 3H:14C
175 tructure shows an EDTA molecule bound to the fructose-6-phosphate site of the 6-phosphofructo-2-kinas
176              The A. tumefaciens ADPGlc PPase/fructose 6-phosphate structural model along with sequenc
177                           In the presence of fructose-6-phosphate, the protein inhibits glucokinase i
178                  In contrast, the binding of fructose-6-phosphate, the reaction product, to the resti
179 y activated by both fructose-1-phosphate and fructose-6-phosphate; the strength of the activation res
180 lease and transfer ammonia from glutamine to fructose 6-phosphate through a channel.
181 te pathway to glyceraldehyde 3-phosphate and fructose 6-phosphate, thus bypassing fructose-1,6-bispho
182 idotransferase 1 (GFAT1), uses glutamine and fructose 6-phosphate to eventually synthesize uridine di
183                       Systematic addition of fructose 6-phosphate to phosphofructokinase in the absen
184 tivator, MgADP, also altered the affinity of fructose 6-phosphate to the enzyme by forming a ternary
185                                   Binding of fructose 6-phosphate to the enzyme displayed a two-step
186  catalyzes the ATP-independent conversion of fructose-6-phosphate to fructose-1,6-bisphosphate in gly
187 step of the glycolytic pathway by converting fructose-6-phosphate to fructose-1,6-bisphosphate.
188 hat catalyzes the irreversible conversion of fructose-6-phosphate to fructose-1,6-bisphosphate.
189        The kinetics for the isomerization of fructose-6-phosphate to glucose-6-phosphate (F6P --> G6P
190           AbMtlD catalyzes the conversion of fructose-6-phosphate to mannitol in two consecutive step
191 Reduction and dephosphorylation catalysis of fructose-6-phosphate to mannitol is dependent on the tra
192                    The enzyme phosphorylates fructose-6-phosphate to produce fructose-1,6-bisphosphat
193  with the 2-Pase domain to secure binding of fructose-6-phosphate to the active pocket, slowing down
194 thway, which splits xylulose-5-phosphate (or fructose-6-phosphate) to acetate precursor acetyl phosph
195 f the corresponding human gene for glutamine-fructose-6-phosphate transaminase (GFPT), located at 2p1
196                                    Glutamine-fructose-6-phosphate transaminase 1 (GFAT) is the rate-l
197     Mutations in the gene encoding glutamine-fructose-6-phosphate transaminase 1 (GFPT1) cause the ne
198                                    Glutamine-fructose-6-phosphate transaminase 1 (GFPT1) is a key rat
199                       GFA1 encodes glutamine-fructose-6-phosphate transaminase.
200 he formation of glucosamine 6-phosphate from fructose 6-phosphate using glutamine as the ammonia sour
201 erization of d-tagatose 6-phosphate C-4 to d-fructose 6-phosphate via a member of Pfam family PF08013
202                                              Fructose 6-phosphate was found to be a potent activator
203 ate was uncompetitive, whereas inhibition by fructose 6-phosphate was mixed.
204  domains binds the allosteric regulator, and fructose 6-phosphate was modeled into this region.
205            The apparent K(m) of GFAT1Alt for fructose-6-phosphate was approximately twofold higher th
206  from exchange of the lower three carbons of fructose-6-phosphate with unlabeled three-carbon precurs

 
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