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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)
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  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
31                    The activity of glutamine:fructose-6-phosphate amido-transferase (GFAT), the first
32            Specific inhibitors of glutamine: fructose 6-phosphate amidotransferase (GFAT), an enzyme
33 nzyme for hexosamine biosynthesis, glutamine:fructose-6-phosphate amidotransferase (GFA) in human ske
34                                    Glutamine:fructose-6-phosphate amidotransferase (GFA) is the rate-
35                                    Glutamine:fructose-6-phosphate amidotransferase (GFA) is the rate-
36 g enzyme for hexosamine synthesis, glutamine:fructose-6-phosphate amidotransferase (GFA), specificall
37                                    Glutamine:fructose-6-phosphate amidotransferase (GFA), the first a
38 e rate-limiting enzyme of the HBP, glutamine:fructose-6-phosphate amidotransferase (GFA), was overexp
39 hosphate by the rate-liming enzyme glutamine:fructose-6-phosphate amidotransferase (GFA).
40                                    Glutamine:fructose-6-phosphate amidotransferase (GFAT) catalyzes t
41                                    Glutamine-fructose-6-phosphate amidotransferase (GFAT) catalyzes t
42                                    Glutamine:fructose-6-phosphate amidotransferase (GFAT) is the enzy
43                                    Glutamine:fructose-6-phosphate amidotransferase (GFAT) is the rate
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
52                       Azaserine, a glutamine:fructose-6-phosphate amidotransferase inhibitor, reverse
53                                    Glutamine:fructose-6-phosphate amidotransferase(GFAT) is the rate-
54  of the rate-limiting enzyme GFAT (glutamine:fructose-6-phosphate amidotransferase) did not protect a
55  enzyme in the hexosamine pathway (glutamine:fructose-6-phosphate amidotransferase).
56 eversed by antisense inhibition of glutamine:fructose-6-phosphate amidotransferase, the rate-limiting
57                                    Glutamine-fructose-6-phosphate aminotransferase (Gfa1) is an essen
58  first enzyme in chitin synthesis (glutamine fructose-6-phosphate aminotransferase) is reported.
59  glutamine, were determined to be 0.8 mm for fructose 6-phosphate and 1.2 mm for glutamine, which are
60      Glucosamine 6-phosphate is converted to fructose 6-phosphate and ammonia by the action of the en
61 e, one could observe substrate inhibition by fructose 6-phosphate and apparent cooperativity in the i
62 e was a mixed inhibitor with respect to both fructose 6-phosphate and ATP.
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
65 sphosphatases (PFKFB1-4), which interconvert fructose 6-phosphate and Fru-2,6-BP.
66 ncrease in glucose 6-phosphate, no change in fructose 6-phosphate and fructose 1,6-diphosphate, an in
67                                         Both fructose 6-phosphate and glutamine protect the enzyme fr
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
71       Diabetes elevated glucose 6-phosphate, fructose 6-phosphate and oxidised (NAD+ and NADP+) and r
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
76  mutase interconverting glucose 6-phosphate, fructose 6-phosphate, and glucose 1-phosphate.
77  mannose 6-phosphate, galactose 6-phosphate, fructose 6-phosphate, and inorganic phosphate.
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
84 se 6-phosphate at 1.16 A resolution and with fructose 6-phosphate at 1.5 A resolution.
85 apparent Michaelis-Menten constant (K(m)) of fructose 6-phosphate at different temperatures and (ii)
86 ps of the glycolysis: the phosphorylation of fructose 6-phosphate at position 1.
87 xed with the cyclic form of its substrate, D-fructose 6-phosphate, at 2.1 A resolution.
88 products of the reaction (orthophosphate and fructose 6-phosphate) bind to the active site in a manne
89                               In the case of fructose-6-phosphate binding, the increased anisotropy w
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
93                      Protection studies with fructose 6-phosphate demonstrate that the value of the d
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
98 bacterium tumefaciens enzyme is activated by fructose 6-phosphate (F6P) and pyruvate.
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
102  ordered mechanism with MgATP binding before fructose 6-phosphate (F6P).
103 y covalent binding of the enzyme substrate d-fructose 6-phosphate (F6P).
104 rconversion of glucose 6-phosphate (G6P) and fructose 6-phosphate (F6P).
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
107  pair, which enhances methanol conversion to fructose-6-phosphate (F6P).
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
119                               The substrate, fructose 6-phosphate (Fru-6-P), binds along the other di
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
122 cherichia coli phosphofructokinase (PFK) for fructose 6-phosphate (Fru-6-P).
123  ability of the enzyme to bind the substrate fructose 6-phosphate (Fru-6-P).
124 nversion of glucose 6-phosphate (Glc-6-P) to fructose 6-phosphate (Fru-6-P).
125 ely low affinity for the acceptor substrate, fructose 6-phosphate (Fru-6-P, K(m) 0.2-1 mm).
126 me, catalyzing the interconversion of beta-D-fructose- 6-phosphate (Fru-6-P) and fructose-2,6-bisphos
127 four active sites, which bind the substrates fructose-6-phosphate (Fru-6-P) and MgATP.
128 strong direct interaction between AMPPCP and fructose-6-phosphate (Fru-6-P) is found.
129               The affinity for the substrate fructose-6-phosphate (Fru-6-P) of a single wild-type act
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
133                            3-Amino-3-deoxy-D-fructose 6-phosphate has previously been demonstrated to
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
137 as well as fructose-1,6-bisphosphate but not fructose 6-phosphate in vitro.
138 se, the feedback inhibition of hexokinase by fructose-6-phosphate, in a first refinement of the model
139 insulin resistance by increasing the flux of fructose-6-phosphate into the hexosamine pathway.
140 t the value of the dissociation constant for fructose 6-phosphate is 3.3 (+/-0.5) x 10(-7) m, approxi
141                  In fact, compared to 3-PGA, fructose-6-phosphate is a more efficient activator in tw
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
150                               The binding of fructose-6-phosphate resulted in a significant increase
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
153              The A. tumefaciens ADPGlc PPase/fructose 6-phosphate structural model along with sequenc
154                           In the presence of fructose-6-phosphate, the protein inhibits glucokinase i
155                  In contrast, the binding of fructose-6-phosphate, the reaction product, to the resti
156 y activated by both fructose-1-phosphate and fructose-6-phosphate; the strength of the activation res
157 lease and transfer ammonia from glutamine to fructose 6-phosphate through a channel.
158 te pathway to glyceraldehyde 3-phosphate and fructose 6-phosphate, thus bypassing fructose-1,6-bispho
159                       Systematic addition of fructose 6-phosphate to phosphofructokinase in the absen
160 tivator, MgADP, also altered the affinity of fructose 6-phosphate to the enzyme by forming a ternary
161                                   Binding of fructose 6-phosphate to the enzyme displayed a two-step
162  catalyzes the ATP-independent conversion of fructose-6-phosphate to fructose-1,6-bisphosphate in gly
163 hat catalyzes the irreversible conversion of fructose-6-phosphate to fructose-1,6-bisphosphate.
164 step of the glycolytic pathway by converting fructose-6-phosphate to fructose-1,6-bisphosphate.
165        The kinetics for the isomerization of fructose-6-phosphate to glucose-6-phosphate (F6P --> G6P
166                    The enzyme phosphorylates fructose-6-phosphate to produce fructose-1,6-bisphosphat
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
170                                    Glutamine-fructose-6-phosphate transaminase 1 (GFAT) is the rate-l
171     Mutations in the gene encoding glutamine-fructose-6-phosphate transaminase 1 (GFPT1) cause the ne
172                                    Glutamine-fructose-6-phosphate transaminase 1 (GFPT1) is a key rat
173                       GFA1 encodes glutamine-fructose-6-phosphate transaminase.
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
176                                              Fructose 6-phosphate was found to be a potent activator
177 ate was uncompetitive, whereas inhibition by fructose 6-phosphate was mixed.
178  domains binds the allosteric regulator, and fructose 6-phosphate was modeled into this region.
179            The apparent K(m) of GFAT1Alt for fructose-6-phosphate was approximately twofold higher th
180  from exchange of the lower three carbons of fructose-6-phosphate with unlabeled three-carbon precurs

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