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1 K showed that the enzyme is not regulated by fructose 1,6 bisphosphate.
2 IA(Glc) (formerly known as III(glc)), and by fructose 1,6-bisphosphate.
3 cerone-P and glyceraldehyde 3-phosphate into fructose 1,6-bisphosphate.
4 exhibited an apparent K(m) of 35 microM for fructose 1,6-bisphosphate.
5 up to 3-fold, with no effect on the K(m) for fructose 1,6-bisphosphate.
6 tone phosphate, forming the much more stable fructose 1,6-bisphosphate.
7 expand the activator specificity to include fructose 1,6-bisphosphate.
8 H379K enzymes were found to be activated by fructose 1,6-bisphosphate.
9 e concentration of a key early intermediate, fructose 1,6-bisphosphate.
10 0.96 +/- 0.07 mm in the presence of Mn2+ and fructose 1,6-bisphosphate.
11 t to Mg2+, and uncompetitive with respect to fructose 1,6-bisphosphate.
12 activity toward inositol monophosphates and fructose 1,6-bisphosphate.
13 this inhibitor is derived from chloroplastic fructose 1,6-bisphosphate.
14 athway by converting fructose-6-phosphate to fructose-1,6-bisphosphate.
15 ion into the concentration of the metabolite fructose-1,6-bisphosphate.
16 rsible conversion of fructose-6-phosphate to fructose-1,6-bisphosphate.
17 T403E) abolishes activation of the enzyme by fructose-1, 6-bisphosphate.
18 above, exhibit kinetic parameters (K(m) for fructose-1,6-bisphosphate, 1.1-1.8 microm; K(a) for Mg(2
19 Ser61 to alanine increases the Km value for fructose 1, 6-bisphosphate 16-fold and product inhibitio
20 s work: a complex with a substrate analogue, fructose 1,6-bisphosphate, a complex with dihydroxyaceto
21 cose, binding of the known effector molecule fructose-1,6-bisphosphate abolishes this interaction.
24 in the active site, many of which abolished fructose 1, 6-bisphosphate aldolase activity, no switch
29 tion of fba and pyk, encoding, respectively, fructose 1,6-bisphosphate aldolase and pyruvate kinase,
31 t structure of the Escherichia coli Class II fructose 1,6-bisphosphate aldolase in the presence of th
33 in attempts to switch the specificity of the fructose 1,6-bisphosphate aldolase to that of the tagato
34 nesis, including bifunctional unidirectional fructose 1,6-bisphosphate aldolase/phosphatase, have bee
36 e structure of the glycolytic enzyme class I fructose-1, 6-bisphosphate aldolase from the human malar
40 keletal muscle and yeast F-actin with muscle fructose-1,6-bisphosphate aldolase (aldolase) and glycer
41 hate (GAP), as it passes between the enzymes fructose-1,6-bisphosphate aldolase (aldolase) and glycer
42 cluding the zinc-dependent glycolytic enzyme fructose-1,6-bisphosphate aldolase (BB0445), the Borreli
44 to our interest in metallodependent class II fructose-1,6-bisphosphate aldolase (FBA-tb), a key enzym
45 tate or glycerol; these results suggest that fructose-1,6-bisphosphate aldolase (FbaA) is a target of
49 report the crystal structures of glycosomal fructose-1,6-bisphosphate aldolase from two major tropic
54 its evolutionary history from all eukaryotic fructose-1, 6-bisphosphate aldolases studied so far.
56 phosphoenolpyruvate (PEP) in the absence of fructose 1,6-bisphosphate, although PEP binding to enzym
57 e phosphatase contained increased amounts of fructose 1,6-bisphosphate and 2-carboxyarabinitol 1-phos
58 igher levels of the glycolytic intermediates fructose 1,6-bisphosphate and 3-phosphoglycerate, and hi
60 relevant intracellular metabolites, such as fructose 1,6-bisphosphate and fructose 2,6-bisphosphate,
62 osterically activated by metabolites such as fructose 1,6-bisphosphate and inhibited by inorganic pho
64 he wild-type enzyme is strongly activated by fructose-1,6-bisphosphate and weakly activated by both f
66 iosynthetic intermediates such as RuBP, ATP, fructose 1,6-bisphosphate, and NADPH enhanced DNA bindin
67 portant substrates, fructose 1-phosphate and fructose 1,6-bisphosphate, and provides an excellent mod
68 ed with the natural substrate of the enzyme, fructose 1,6-bisphosphate, and substantiated a previousl
69 e phosphate, glyceraldehyde 3-phosphate, and fructose 1,6-bisphosphate at 1.5, 2.1, and 1.3 A, respec
70 by thermostability studies, demonstrate that fructose 1,6-bisphosphate binding to the allosteric doma
71 f the tyrosyl-phosphorylated proteins at the fructose 1,6-bisphosphate-binding site converts the tetr
72 histidines and phosphate groups, mostly from fructose-1,6-bisphosphate but also inorganic phosphates
74 drolyze fructose-2,6-bisphosphate as well as fructose-1,6-bisphosphate but not fructose 6-phosphate i
75 mechanism of AMP inhibition with respect to fructose 1,6-bisphosphate changed from noncompetitive (w
76 allosteric mechanism whereby the binding of fructose 1,6-bisphosphate destabilizes an alpha-helix th
78 IN3D-depleted cells have increased levels of Fructose 1,6 Bisphosphate (F1,6-BP), the last six-carbon
80 and all apicomplexans express one or both of fructose 1,6-bisphosphate (F16BP) aldolase and 2-deoxyri
82 miting step in the pathway and the levels of fructose (1,6) bisphosphate (FBP), are predictive of the
83 vity toward ATP and allosteric regulation by fructose 1, 6-bisphosphate (FBP), which has been shown t
85 ls of dihydroxy-acetone phosphate (DHAP) and fructose 1,6-bisphosphate (FBP) and a progressive loss o
87 ation by the glycolytic pathway intermediate fructose 1,6-bisphosphate (FBP) compared to wild-type GK
89 ibitor oxalate, and the allosteric activator fructose 1,6-bisphosphate (FBP) has been determined to a
90 lase family that catalyzes the cleavage of d-fructose 1,6-bisphosphate (FBP) into dihydroxyacetone ph
91 For monitoring glycolysis, the intermediate fructose 1,6-bisphosphate (FBP) is a particularly inform
93 The addition of the allosteric activator fructose 1,6-bisphosphate (FBP) to form the yPK-Tl+-Mn2+
94 lation of fructose 6-phosphate (F6P) to give fructose 1,6-bisphosphate (FBP) using MgATP as the phosp
96 licit major structural reorganization of the fructose 1,6-bisphosphate (FBP), an allosteric activator
97 ic pathway [e.g., phosphoenolpyruvate (PEP), fructose 1,6-bisphosphate (FBP), and citrate] and by the
98 as malate, ribulose 1,5-bisphosphate (RuBP), fructose 1,6-bisphosphate (FBP), and photorespiration in
99 otransferase) is inhibited allosterically by fructose 1,6-bisphosphate (FBP), and this inhibition is
100 f the allosteric regulators of its activity, fructose 1,6-bisphosphate (FBP), at 3.2 and 3.0 A, are p
101 nal approaches to investigate the effects of fructose 1,6-bisphosphate (FBP), phosphate (Pi), and ion
102 mined for myo-inositol 1-phosphate (IMP) and fructose 1,6-bisphosphate (FBP), previously considered t
104 ose pyrophosphorylase is mainly activated by fructose 1,6-bisphosphate (FBP), whereas the Agrobacteri
105 ule effectors, glucose 6-phosphate (G6P) and fructose 1,6-bisphosphate (FBP), which somehow enhance C
111 reduce affinity for the allosteric inhibitor fructose-1,6-bisphosphate (FBP) and formation of the tet
115 Bacteroides species show that ATP-dependent fructose-1,6-bisphosphate (FBP) synthesis is necessary f
118 absence of the natural allosteric activator fructose-1,6-bisphosphate (FBP), maintained high tempera
119 phosphate (G6P), fructose-6-phosphate (F6P), fructose-1,6-bisphosphate (FBP), phosphoenolpyruvate (PE
120 rs AMPK activation by sensing the absence of fructose-1,6-bisphosphate (FBP), with AMPK being progres
123 : ATP 5, ADP 0.01, phosphocreatine (CrP) 10) fructose-1,6-bisphosphate (FBP; 1 mm) and fructose-6-pho
124 es for inhibitor alanine (Ala) and activator fructose-1,6-bisphosphate (Fru-1,6-BP) in human liver py
127 In vivo phosphorylating agents, such as fructose 1,6-bisphosphate, generate phosphorylated forms
128 incorporate 14C from 14CO2 sequentially into fructose 1,6-bisphosphate, hamamelose bisphosphate, hama
129 tion leads to the continuous accumulation of fructose 1,6-bisphosphate in a permanently frozen soluti
130 glucose-labeling studies showed accumulated fructose 1,6-bisphosphate in FK866-treated cells mainly
134 y step in gluconeogenesis, the conversion of fructose 1,6-bisphosphate into fructose 6-phosphate.
135 n Mg(2+) for high activity, and that neither fructose-1,6-bisphosphate nor AMP was a positive alloste
136 glycolysis and the feedforward activation of fructose-1,6-bisphosphate on pyruvate kinase translate f
137 (EMSAs) confirmed a destabilizing effect of fructose-1,6-bisphosphate on the CggR/DNA complex, and a
138 by incubation with the aldolase substrates, fructose 1,6-bisphosphate or glyceraldehyde 3-phosphate.
139 ction into permeabilized 3T3L1 adipocytes of fructose 1,6-bisphosphate or the metabolic inhibitor 2-d
140 ites (such as dihydroxyacetone phosphate and fructose-1,6-bisphosphate), pentose phosphate pathway co
141 ontaining decreased amounts of chloroplastic fructose 1,6-bisphosphate phosphatase contained increase
143 e key processes identified are metabolism of fructose-1,6-bisphosphate, production of glycerol-3-phos
144 presence of glycolytic intermediates such as fructose 1,6-bisphosphate (the intracellular effector),
147 tochondrial PEP without producing glycolytic fructose 1,6-bisphosphate to allosterically activate PKm
148 step in gluconeogenesis is the conversion of fructose 1,6-bisphosphate to fructose 6-phosphate by a f
149 protein encoded by the ALDOA gene, converts fructose-1,6-bisphosphate to dihydroxyacetone phosphate
150 osphorylates fructose-6-phosphate to produce fructose-1,6-bisphosphate using inorganic pyrophosphate
154 ucose-6-phosphate, fructose-6-phosphate, and fructose-1,6-bisphosphate) were profoundly and rapidly e
155 phate, and (ii) phosphofructokinase, to form fructose 1,6-bisphosphate, which is a member of central
156 ut also requires inhibition by the regulator fructose 1,6-bisphosphate, which senses the upper-glycol
157 on is initiated by the glycolytic metabolite fructose-1,6-bisphosphate, which directly binds Cdc19 am
158 e presence of glucose led to accumulation of fructose-1,6-bisphosphate, which has been associated wit
159 te is measured by coupling the production of fructose-1,6-bisphosphate with the oxidation of NADH usi