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Query: EC:3.1.3.1 (alkaline phosphatase)
 47,916 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Several methods for the permeabilization of Saccharomyces cerevisiae M1 were compared. Cells were permeabilized in the presence of 3% toluene/mercaptoethanol, and the activities of 6-phosphofructo-2-kinase, fructose-2,6-bisphosphatase and alkaline phosphatase were measured during growth of yeast on glucose. In the exponential phase of growth, the specific activities of 6-phosphofructo-2-kinase and fructose-2,6-bisphosphatase decrease significantly. The specific activities of 6-phosphofructo-2-kinase and high-affinity fructose-2,6-bisphosphatase increase again during the transition phase and reach maximum values in the stationary phase. In contrast to the specific activities, the activity concentrations of 6-phosphofructo-2-kinase and fructose-2,6-bisphosphatase remain nearly constant in the exponential phase, but increase in the transition and the stationary growth phase. The concentration of fructose-2,6-bisphosphate drops from about 6 microM in the exponential phase to very low levels in the transition phase, but increases slightly in the stationary phase. In Saccharomyces cerevisiae M1 several fructose-2,6-bisphosphate degrading activities were measured differing in the behaviour during growth on glucose, in the pH-optimum and the inhibition by fructose-6-phosphate.
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PMID:Fructose-2,6-bisphosphate metabolism in permeabilized yeast cells. 166 44

Fructose-2,6-bisphosphatase was purified from yeast and separated from 6-phosphofructo-2-kinase and alkaline phosphatase. The enzyme released Pi from the 2-position of fructose 2,6-bisphosphate and formed fructose 6-phosphate in stoichiometric amounts. The enzyme displays hyperbolic kinetics towards fructose 2,6-bisphosphate, with a Km value of 0.3 microM. It is strongly inhibited by fructose 6-phosphate. The inhibition is counteracted by L-glycerol 3-phosphate. Phosphorylation of the enzyme by cyclic-AMP-dependent protein kinase causes inactivation, which is reversible by the action of protein phosphatase 2A.
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PMID:Fructose-2,6-bisphosphatase and 6-phosphofructo-2-kinase are separable in yeast. 282 52

Enzymatic dephosphorylation of the phosphorylated forms of five different yeast enzymes has been studied: fructose-1,6-bisphosphatase, glycogen phosphorylase, neutral trehalase, NAD-glutamate dehydrogenase and 6-phosphofructo-2-kinase. Phosphorylated fructose-1,6-bisphosphatase and phosphorylated 6-phosphofructo-2-kinase were present in extracts of starved yeast cells which had been incubated for 10 min with glucose. Phosphorylated glycogen phosphorylase, neutral trehalase and NAD-glutamate dehydrogenase were obtained by incubation of yeast extract with ATP, cyclic AMP and Mg2+. After incubation with commercially available preparations of alkaline phosphatase, all five phosphorylated enzymes studied showed the changes in catalytic activity that would be expected as a consequence of dephosphorylation. The recently purified yeast enzyme which dephosphorylates phosphorylated fructose-1,6-bisophosphatase (Horn and Holzer (1987) however, was found to be active only with the phosphorylated fructose-1,6-bisphosphatase, but not with the other four phosphorylated enzymes studied. By contrast, a crude extract from yeast showed dephosphorylating activity towards all five substrates. Substrate specificity with the five phosphorylated enzymes studied of different phosphoprotein phosphatases from yeast prepared by others is discussed.
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PMID:Substrate specificity of the phosphorylated fructose-1,6-bisphosphatase dephosphorylating protein phosphatase from Saccharomyces cerevisiae. 284 61

Adenosine [gamma-(S)-16O,17O,18O]triphosphate was used as substrate in the phosphokinase reaction catalyzed by 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase. The product D-fructose 2,6-[2-16O,17O,18O]bisphosphate was then used as substrate in the alkaline phosphatase-mediated transfer of the phospho groups to (S)-butane-1,3-diol, where the configuration at phosphorus has been determined. Although there was approximately equal transfer by alkaline phosphatase of the labeled 2- and the unlabeled 6-phospho groups, the subsequent assignment of configuration of the chiral phospho group from the 2-position was unambiguous. It was found that 6-phosphofructo-2-kinase proceeds by a pathway that results in net inversion of the configuration at phosphorus. The simplest interpretation of this result is that the phospho group is transferred directly between substrates in a ternary complex by an "in-line" mechanism not involving a phosphoenzyme intermediate. This conclusion is consistent with the fact that the enzyme cannot be labeled by [gamma-32P]ATP and with steady-state kinetic data that suggest an ordered sequential mechanism. This finding also indicates that the adenine nucleotide and sugar phosphate isotope exchange reactions catalyzed by the enzyme are not relevant to the normal catalytic pathway of the kinase.
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PMID:The stereochemical course of phospho group transfer catalyzed by rat liver 6-phosphofructo-2-kinase. 297 3

Purified bovine heart 6-phosphofructo-2-kinase can be phosphorylated in the presence of protein kinase C and dephosphorylated by alkaline phosphatase; changes in phosphorylation state have no effect on enzyme activity. By contrast, the rat liver enzyme is a poor substrate for protein kinase C. Unlike the liver enzyme, which is bifunctional and is phosphorylated by fructose 2,6-[2-32P]bisphosphate, the heart enzyme contains 10 times less fructose 2,6-bisphosphatase activity and is phosphorylated at a slower rate and to a lesser extent than the liver enzyme. Both rat liver and bovine heart enzymes catalyse a similar exchange reaction between [U-14C]ADP and ATP.
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PMID:Phosphorylation of purified bovine heart and rat liver 6-phosphofructo-2-kinase by protein kinase C and comparison of the fructose-2,6-bisphosphatase activity of the two enzymes. 303 Feb 81

The phosphorylation status of 6-phosphofructo-2-kinase/fructose-2,6-bisphosphate 2-phosphatase (EC 2.7.1.105/ EC 3.1.3.46) in rosette leaves of Arabidopsis was examined. Immunoblotting with specific antisera detected 96-kDa and 92-kDa bands in the crude protein extracts from rosette leaves of Arabidopsis. Incubation of protein samples with alkaline phosphatase before SDS-PAGE reduced the 96-kDa band with concomitant increase of the 92-kDa band, suggesting that the former is a phosphorylated form of the latter. In accordance with this result, 96-kDa and 92-kDa bands were immuno-precipitated from the crude protein extracts from [(32)P]orthophosphate-labeled rosettes of Arabidopsis; and, the former was heavily labeled, the latter faintly labeled. Analysis of phospho-amino acid residues derived from the [(32)P]-labeled 96-kDa band revealed that the phosphorylation occurred on serine and threonine residues, excluding the possibility that the phosphorylated band represent a phospho-histidine intermediate that is known to form in the phosphatase reaction. The relative level of the 96-kDa band over the 92-kDa band in whole rosette extracts changed diurnally and was highest at the beginning of nighttime. Furthermore, the 96-kDa band was highly enriched in the extracts of very young rosette leaves, suggesting that the phosphorylation status of 6-phosphofructo-2-kinase/fructose-2,6-bisphosphate 2-phosphatase is regulated physiologically and developmentally in Arabidopsis.
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PMID:Phosphorylation of a bifunctional enzyme, 6-phosphofructo-2-kinase/fructose-2,6-bisphosphate 2-phosphatase, is regulated physiologically and developmentally in rosette leaves of Arabidopsis thaliana. 1167 18