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1 K showed that the enzyme is not regulated by fructose 1,6 bisphosphate.
2 up to 3-fold, with no effect on the K(m) for fructose 1,6-bisphosphate.
3 tone phosphate, forming the much more stable fructose 1,6-bisphosphate.
4 expand the activator specificity to include fructose 1,6-bisphosphate.
5 H379K enzymes were found to be activated by fructose 1,6-bisphosphate.
6 e concentration of a key early intermediate, fructose 1,6-bisphosphate.
7 0.96 +/- 0.07 mm in the presence of Mn2+ and fructose 1,6-bisphosphate.
8 t to Mg2+, and uncompetitive with respect to fructose 1,6-bisphosphate.
9 activity toward inositol monophosphates and fructose 1,6-bisphosphate.
10 this inhibitor is derived from chloroplastic fructose 1,6-bisphosphate.
11 IA(Glc) (formerly known as III(glc)), and by fructose 1,6-bisphosphate.
12 cerone-P and glyceraldehyde 3-phosphate into fructose 1,6-bisphosphate.
13 exhibited an apparent K(m) of 35 microM for fructose 1,6-bisphosphate.
14 ion into the concentration of the metabolite fructose-1,6-bisphosphate.
15 rsible conversion of fructose-6-phosphate to fructose-1,6-bisphosphate.
16 athway by converting 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.
23 in the active site, many of which abolished fructose 1, 6-bisphosphate aldolase activity, no switch
27 tion of fba and pyk, encoding, respectively, fructose 1,6-bisphosphate aldolase and pyruvate kinase,
29 t structure of the Escherichia coli Class II fructose 1,6-bisphosphate aldolase in the presence of th
31 in attempts to switch the specificity of the fructose 1,6-bisphosphate aldolase to that of the tagato
32 nesis, including bifunctional unidirectional fructose 1,6-bisphosphate aldolase/phosphatase, have bee
33 e structure of the glycolytic enzyme class I fructose-1, 6-bisphosphate aldolase from the human malar
37 keletal muscle and yeast F-actin with muscle fructose-1,6-bisphosphate aldolase (aldolase) and glycer
38 hate (GAP), as it passes between the enzymes fructose-1,6-bisphosphate aldolase (aldolase) and glycer
39 cluding the zinc-dependent glycolytic enzyme fructose-1,6-bisphosphate aldolase (BB0445), the Borreli
41 to our interest in metallodependent class II fructose-1,6-bisphosphate aldolase (FBA-tb), a key enzym
42 tate or glycerol; these results suggest that fructose-1,6-bisphosphate aldolase (FbaA) is a target of
46 report the crystal structures of glycosomal fructose-1,6-bisphosphate aldolase from two major tropic
51 its evolutionary history from all eukaryotic fructose-1, 6-bisphosphate aldolases studied so far.
53 phosphoenolpyruvate (PEP) in the absence of fructose 1,6-bisphosphate, although PEP binding to enzym
54 e phosphatase contained increased amounts of fructose 1,6-bisphosphate and 2-carboxyarabinitol 1-phos
56 relevant intracellular metabolites, such as fructose 1,6-bisphosphate and fructose 2,6-bisphosphate,
58 osterically activated by metabolites such as fructose 1,6-bisphosphate and inhibited by inorganic pho
60 he wild-type enzyme is strongly activated by fructose-1,6-bisphosphate and weakly activated by both f
62 iosynthetic intermediates such as RuBP, ATP, fructose 1,6-bisphosphate, and NADPH enhanced DNA bindin
63 portant substrates, fructose 1-phosphate and fructose 1,6-bisphosphate, and provides an excellent mod
64 ed with the natural substrate of the enzyme, fructose 1,6-bisphosphate, and substantiated a previousl
65 e phosphate, glyceraldehyde 3-phosphate, and fructose 1,6-bisphosphate at 1.5, 2.1, and 1.3 A, respec
66 by thermostability studies, demonstrate that fructose 1,6-bisphosphate binding to the allosteric doma
67 f the tyrosyl-phosphorylated proteins at the fructose 1,6-bisphosphate-binding site converts the tetr
68 histidines and phosphate groups, mostly from fructose-1,6-bisphosphate but also inorganic phosphates
70 drolyze fructose-2,6-bisphosphate as well as fructose-1,6-bisphosphate but not fructose 6-phosphate i
71 mechanism of AMP inhibition with respect to fructose 1,6-bisphosphate changed from noncompetitive (w
72 allosteric mechanism whereby the binding of fructose 1,6-bisphosphate destabilizes an alpha-helix th
74 and all apicomplexans express one or both of fructose 1,6-bisphosphate (F16BP) aldolase and 2-deoxyri
76 miting step in the pathway and the levels of fructose (1,6) bisphosphate (FBP), are predictive of the
77 vity toward ATP and allosteric regulation by fructose 1, 6-bisphosphate (FBP), which has been shown t
78 ls of dihydroxy-acetone phosphate (DHAP) and fructose 1,6-bisphosphate (FBP) and a progressive loss o
79 ation by the glycolytic pathway intermediate fructose 1,6-bisphosphate (FBP) compared to wild-type GK
81 ibitor oxalate, and the allosteric activator fructose 1,6-bisphosphate (FBP) has been determined to a
82 lase family that catalyzes the cleavage of d-fructose 1,6-bisphosphate (FBP) into dihydroxyacetone ph
84 The addition of the allosteric activator fructose 1,6-bisphosphate (FBP) to form the yPK-Tl+-Mn2+
85 lation of fructose 6-phosphate (F6P) to give fructose 1,6-bisphosphate (FBP) using MgATP as the phosp
87 ic pathway [e.g., phosphoenolpyruvate (PEP), fructose 1,6-bisphosphate (FBP), and citrate] and by the
88 otransferase) is inhibited allosterically by fructose 1,6-bisphosphate (FBP), and this inhibition is
89 f the allosteric regulators of its activity, fructose 1,6-bisphosphate (FBP), at 3.2 and 3.0 A, are p
90 nal approaches to investigate the effects of fructose 1,6-bisphosphate (FBP), phosphate (Pi), and ion
91 mined for myo-inositol 1-phosphate (IMP) and fructose 1,6-bisphosphate (FBP), previously considered t
93 ose pyrophosphorylase is mainly activated by fructose 1,6-bisphosphate (FBP), whereas the Agrobacteri
94 ule effectors, glucose 6-phosphate (G6P) and fructose 1,6-bisphosphate (FBP), which somehow enhance C
100 reduce affinity for the allosteric inhibitor fructose-1,6-bisphosphate (FBP) and formation of the tet
106 absence of the natural allosteric activator fructose-1,6-bisphosphate (FBP), maintained high tempera
107 phosphate (G6P), fructose-6-phosphate (F6P), fructose-1,6-bisphosphate (FBP), phosphoenolpyruvate (PE
108 rs AMPK activation by sensing the absence of fructose-1,6-bisphosphate (FBP), with AMPK being progres
111 : ATP 5, ADP 0.01, phosphocreatine (CrP) 10) fructose-1,6-bisphosphate (FBP; 1 mm) and fructose-6-pho
113 incorporate 14C from 14CO2 sequentially into fructose 1,6-bisphosphate, hamamelose bisphosphate, hama
114 tion leads to the continuous accumulation of fructose 1,6-bisphosphate in a permanently frozen soluti
115 glucose-labeling studies showed accumulated fructose 1,6-bisphosphate in FK866-treated cells mainly
119 y step in gluconeogenesis, the conversion of fructose 1,6-bisphosphate into fructose 6-phosphate.
120 n Mg(2+) for high activity, and that neither fructose-1,6-bisphosphate nor AMP was a positive alloste
121 glycolysis and the feedforward activation of fructose-1,6-bisphosphate on pyruvate kinase translate f
122 (EMSAs) confirmed a destabilizing effect of fructose-1,6-bisphosphate on the CggR/DNA complex, and a
123 by incubation with the aldolase substrates, fructose 1,6-bisphosphate or glyceraldehyde 3-phosphate.
124 ction into permeabilized 3T3L1 adipocytes of fructose 1,6-bisphosphate or the metabolic inhibitor 2-d
125 ites (such as dihydroxyacetone phosphate and fructose-1,6-bisphosphate), pentose phosphate pathway co
126 ontaining decreased amounts of chloroplastic fructose 1,6-bisphosphate phosphatase contained increase
128 presence of glycolytic intermediates such as fructose 1,6-bisphosphate (the intracellular effector),
130 step in gluconeogenesis is the conversion of fructose 1,6-bisphosphate to fructose 6-phosphate by a f
131 protein encoded by the ALDOA gene, converts fructose-1,6-bisphosphate to dihydroxyacetone phosphate
132 osphorylates fructose-6-phosphate to produce fructose-1,6-bisphosphate using inorganic pyrophosphate
136 ucose-6-phosphate, fructose-6-phosphate, and fructose-1,6-bisphosphate) were profoundly and rapidly e
137 phate, and (ii) phosphofructokinase, to form fructose 1,6-bisphosphate, which is a member of central
138 e presence of glucose led to accumulation of fructose-1,6-bisphosphate, which has been associated wit
139 te is measured by coupling the production of fructose-1,6-bisphosphate with the oxidation of NADH usi
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