Activation of phosphofructokinase by divalent anions

Foe, Lawrence G.; Trujillo, John L.

doi:10.1016/0003-9861(80)90248-9

Cited by 9 publications

(2 citation statements)

References 28 publications

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“…These results are similar to previous observations that kosmotropes stabilize the native conformation of acidic (negatively charged) proteins, resulting in enhanced enzyme activity (41,42), since WbpA is negatively charged at pH 7.5 (pI 5.5). These results are also consistent with the observed inactivation of phosphofructokinase by chaotropic anions according to their increasing chaotropicity in the Hofmeister series (43). Analysis of the ammonium sulfate concentration data reveals both a concentration-dependent activation effect and, at high concentrations, a salting-out effect (Fig.…”

Section: Table II Effect Of Cations and Anions Of The Various Salts Osupporting

confidence: 89%

Biochemical Characterization of WbpA, a UDP-N-acetyl-d-glucosamine 6-Dehydrogenase Involved in O-antigen Biosynthesis in Pseudomonas aeruginosa PAO1

Miller

Wenzel

Daniels

et al. 2004

Journal of Biological Chemistry

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Section: Table II Effect Of Cations and Anions Of The Various Salts Osupporting

confidence: 89%

Biochemical Characterization of WbpA, a UDP-N-acetyl-d-glucosamine 6-Dehydrogenase Involved in O-antigen Biosynthesis in Pseudomonas aeruginosa PAO1

Miller

Wenzel

Daniels

et al. 2004

Journal of Biological Chemistry

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“…The effect of cations on enzyme activity is systematically analyzed in the characterization of new enzymes in many instances. [36][37][38][39] However, the effect of cations on enzyme stability, mainly if the actions lack of effect on enzyme activity, is not usually considered, although in some cases the cation effects are quite relevant. [40][41][42][43] Ions may be very relevant to stabilize the enzyme surface ionic net, forming some ionic crosslinking on specic areas or stabilizing concrete areas by ionic bridges.…”

Section: Introductionmentioning

confidence: 99%

Stabilizing effects of cations on lipases depend on the immobilization protocol

et al. 2015

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27The effect of an additive on enzyme stability use to be considered an intrinsic feature of 28 the lipase. However, in this paper we have found that the effect of additive on enzyme stability 29 is depended on the immobilization protocol. After assaying the effects of diverse chloride salts 30 with different cations on different lipases activity, no relevant effect was detected. Free enzymes 31 or the covalently immobilized enzymes are not stabilized by these cations for any of the studied 32 lipases. However, Mn 2+ and Ca 2+ (at a concentration of 5 mM) are able to greatly stabilize the 33 lipases from Rhizomucor miehei (RML) and Candida rugosa (CRL) when they are present 34 during the inactivation, but only if the enzymes are immobilized on octyl-agarose (stabilization 35 factor ranging from 20 to 50). The effect was only detected using more than 2.5 mM of the 36 cations, and reached the maximum value at 5 mM, suggesting a saturation mechanism of action. 37The stabilization seemed to be based on a specific mechanism, and required to have the 38 recognition sites saturated by the cations. Mg 2+ has no effect on enzyme stability for both 39 enzymes, but it is able to suppress the stabilization promoted by the other two cations using 40 CRL; while it has no effect on the cation stabilization when using RML. 41 This is the first report of a cation induced enzyme stabilization effect that depends on the 42 lipase immobilization protocol. 43 44

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Enzymes of glucose metabolism in cultured human gliomas: Neoplasia is accompanied by altered hexokinase, phosphofructokinase, and glucose-6-phosphate dehydrogenase levels

et al. 1987

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The enzymes of glycolysis and selected enzymes of the pentose phosphate pathways were measured by fluorometric methods in extracts prepared from cultures of normal cortical human astrocytes and from cultures derived from low-grade (II) or high-grade (IV) gliomas. The hexokinase and phosphofructokinase levels of the low-grade glioma-derived line were not significantly different from those of the normal astrocyte cultures. However, the activities of hexokinase and phosphofructokinase were consistently and significantly increased in the high-grade glioma-derived lines. The activity of glucose-6-phosphate dehydrogenase was significantly decreased in all glioma-derived lines and by more than 90% in the high-grade-derived lines. Other enzymes of the glycolytic pathway were not significantly different from those of normal astrocytes, or they showed a variation inconsistently related to the neoplastic state. Glucose flux is not apparently regulated to a significant degree of hexokinase in glioma-derived lines, since the measured Vmax values are in substantial excess over the measured flux rates. Reversible binding of hexokinase to the particulate fraction was observed in both the normal astrocytes cultures and the high-grade glioma-derived lines. A twofold displacement of particulate hexokinase by ATP, ADP, 1-O-methylglucose, sorbitol-6-phosphate, and dibutyryl cyclic AMP was observed in the high-grade glioma-derived lines. The degree of displacement by various agents and the basal ratio of free/bound was not significantly different between the transformers and the nontransformants. The hexokinase from both the gliomas and the normal astrocytes was noncompetitively inhibited by the glucose analogue 2-deoxy-d-glucose. Phosphofructokinase activity is close to the observed glucose flux rates in both the normal astrocyte and the glioma-derived cultures. The phosphofructokinase activity of normal astrocytes is activated twofold or more by ADP, AMP, fructose-2,6-diphosphate, and Pi. However, these same ligands activate phosphofructokinase by less than twofold in a typical high-grade glioma-derived line. ATP, dibutyryl cyclic AMP, and citrate inhibit glioma and normal astrocytic phosphofructokinase, but the magnitude of the inhibition is much less than in the glioma-derived lines.

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Activation of phosphofructokinase by divalent anions

Cited by 9 publications

References 28 publications

Biochemical Characterization of WbpA, a UDP-N-acetyl-d-glucosamine 6-Dehydrogenase Involved in O-antigen Biosynthesis in Pseudomonas aeruginosa PAO1

Biochemical Characterization of WbpA, a UDP-N-acetyl-d-glucosamine 6-Dehydrogenase Involved in O-antigen Biosynthesis in Pseudomonas aeruginosa PAO1

Stabilizing effects of cations on lipases depend on the immobilization protocol

Enzymes of glucose metabolism in cultured human gliomas: Neoplasia is accompanied by altered hexokinase, phosphofructokinase, and glucose-6-phosphate dehydrogenase levels

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