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PubMed1986

Effects of various metabolites on two phosphoglucomutase allozyme activities from Drosophila melanogaster.

The effects of various metabolites on the two most common phosphoglucomutase allozymes (PGMA and PGMB) in Drosophila melanogaster have been investigated in vitro. 2,3-Diphosphoglycerate (2,3DPG) inhibited PGMA and PGMB to the same degree in the presence of 25 microM glucose-1,6-diphosphate (G1,6P2). However a higher concentration of G1,6P2 partially reversed the inhibition of PGMA exerted by 2,3DPG, so that in the presence of 150 microM G1,6P2 the inhibition of PGMA was half that of PGMB at pH 6.0. Glycerol-3-phosphate (G3P) had no significant effect at pH 7.4 but exerted an activating effect at pH 6.0 which was more pronounced in the case of PGMB. ATP, citrate, and fructose-1, 6-diphosphate (F1,6P2) inhibited both PGMA and PGMB. The differences found in vitro between these two allozymes can have a significant impact on in vivo function and, therefore, on the maintenance of PGM polymorphism in experimental populations of D. melanogaster studied in the laboratory.

Alleles↗
PubMed1985

Electrophoretic and heat-stability polymorphism at the phosphoglucomutase (Pgm) locus in natural populations of Drosophila melanogaster.

Genetic polymorphism for electrophoretic and heart-sensitive alleles is known at the phosphoglucomutase (Pgm) locus in Drosophila melanogaster. Analysis of the distribution of electrophoretic and thermosensitive (ts) alleles was carried out in natural populations from Canada and West Africa and compared with already known data on Italian populations [Trippa, G., Loverre, A., and Catamo, A. (1976). Nature 260:42]. The data show the existence of five common alleles, Pgm1.00,tr, Pmg1.00,ts, Pgm0.70,ts, Pgm1.20,ts, and Pgm1.50,tr, and two rare alleles, Pgm0.55,ts and Pgm1.20,tr. The most frequent allele is always Pgm1.00,tr; the second most common allele is always of the ts type. The cumulated frequencies of ts alleles in the populations varies between 11 and 32%. The heat stability polymorphism is present in all populations examined and shows again the uniform geographic pattern that has been found for electrophoretic variation at this locus.

Alleles↗
PubMed1984

The Pk-3 gene determines both the heart, M1, and the kidney, M2, pyruvate kinase isozymes in the mouse; and a simple electrophoretic method for separating phosphoglucomutase-3.

We have found that in mice carrying Pk-3r, an allele leading to loss or activity of kidney pyruvate kinase, the activity of heart pyruvate kinase is also diminished. Electrophoretic studies on tissues from mice carrying Pk-3r and/or Pk-3b, an allele determining an electrophoretically detectable variant, show that Pk-3 affects the expression of both the heart, M1, and the kidney, M2, pyruvate kinase isozymes. These results, together with linkage data, indicate that both isozymes are determined by the same structural gene, Pk-3. We also report a simple method for separating phosphoglucomutase-3 (PGM-3) by electrophoresis on cellulose acetate plates.

Animals↗
PubMed1985

Properties of allelic variants of phosphoglucomutase from the sea anemone Metridium senile.

The phosphoglucomutase (Pgm) locus from populations of the sea anemone Metridium senile has three alleles in natural populations from the northeastern coast of North America. Two of the alleles exhibit clinal variation north of Cape Cod, suggesting a possible association of allele frequency with environmental temperature. This clinal pattern is reproducible and stable over at least brief periods of time. The allozymes encoded by each of the six Pgm genotypes have been partially purified and characterized. The symmetrical pH optimum for Vmax is pH 7.5; the apparent Km (Kmapp) of glucose-1-phosphate declines monotonically as the pH increases from 6.5 to 8.5. There are no pronounced differences in heat stabilities of PGM produced by various genotypes, nor are there significant differences in specific activities. There are no differences in the sensitivity of Vmax to temperature. Kmapp values are very low for all genotypes, ranging from about 2 to 12 microM, depending upon the temperature. Kmapp of glucose-1-phosphate declines as the temperature is raised for all genotypes, whether the pH is held constant or allowed to vary with the temperature. Under certain conditions, there are small significant differences among genotypes in Kappm values, but there is no systematic pattern to these differences. The present data provide no biochemical explanation for the maintenance of the Pgm cline by selection for functional differences under different thermal regimes.

Alleles↗
PubMed1979

Genetic and cytogenetic studies of four glycolytic enzymes in Drosophila melanogaster: aldolase, triosephosphate isomerase, 3-phosphoglycerate kinase, and phosphoglucomutase.

Four glycolytic enzymes in Drosophila melanogaster have been genetically and/or cytogenetically mapped. The structural gene for aldolase (Ald) has been genetically mapped to 3-91.5 and cytogenetically localized to 97A-B. Tpi, the structural gene for triosephosphate isomerase, has been genetically mapped to 3-101.3 and cytogenetically localized to 99B-E. Utilizing closer-flanking markers than the previous mapping, Pgk, the structural gene for 3-phosphoglycerate kinase, has been mapped to 2-5.9; cytogenetically it was found to lie in the interval between 22D and 23E3. The cytogenetic locataion of Pgm, the structural gene for phosphoglucomutase which has been located genetically at 3-43.4, was determined to be in 72D1-5.

Alleles↗
PubMed1979

Properties of the two common electrophoretic variants of phosphoglucomutase in Drosophila melanogaster.

Phosphoglucomutase (PGM) of adult stage in Drosophilia melanogaster has been characterized by gel filtration, ion-exchange chromatography, and isoelectric focusing. The two common electrophoretic variants, PGMA and PGMB, differ with respect to their kinetic and stability parameters. PGMA is more thermostable than PGMB but shows the same pH optimum, equal dependence on Mg2+, and identical molecular weight. There is no significant kinetic difference between the two allozymes at the optimum pH values, but at pH 6.0 the Km value for glucose-1,6-diphosphate of PGMB is significantly higher than that of PGMA. This difference might explain the observed selective advantage of the PgmA allele in population studies.

Alleles↗
PubMed1982

Demonstration of antibodies to phosphoglucomutase of parasitic origin in Brugia pahangi-infected cats.

Antibodies inhibitory to the activity of the enzyme phosphoglucomutase (PGM) EC 2.7.5.1. of Brugia pahangi adult worm were demonstrated in sera from five rabbits immunized against this filarioid and from 5 of 27 cats infected with B. pahangi, by isoelectricfocusing and spectrophotometric techniques. This anti-PGM activity was species- and stage-specific. This raises the possibility of using species-specific isoenzymes of parasitic origin as antigens in serological tests.

Animals↗
PubMed1982

Multiple phosphoglucomutase alleles in two species of Mansonia mosquito.

Multiple phosphoglucomutase (E.C.2.7.5.1) alleles are found in the mosquitoes Mansonia crassipes and M. uniformis. The present study reveals 4 Pgm alleles, of which Pgm(B) and Pgm(C) are common to both species while Pgm(A) is present only in M. crassipes and Pgm(D) only in M uniformis. The frequencies in both species accord well with Hardy-Weinberg expectations. The most frequent allele is that controlling a phenotype with an intermediate electrophoretic mobility, viz Pgm(B) in M. crassipes and Pgm(C) in M. Uniformis.

Alleles↗
PubMed1980

Dynamics of phosphoglucomutase heat sensitivity polymorphism in Culicidae.

In 6 species of mosquitoes of the genera Aedes and Culiseta (Culicidae, Diptera) the frequency of phosphoglucomutase (PGM) heat sensitivity alleles is inversely correlated with the temperature of the environment where larvae develop. These data suggest that different selective values are associated with the PGM thermoresistant and thermosensitive genotypes in the different habitats.

Alleles↗
PubMed1980

Multiple phosphoglucomutase alleles in Toxorhynchites splendens (Diptera: Culcidae).

Multiple phosphoglucomutase (E.C. 2.7.5.1) alleles are found in the mosquito Toxorhynchites splendens. The sample studied reveals 3 Pgm alleles whose frequencies are in good accord with Hardy-Weinberg expectations. The most frequent allele is that controlling a phenotype with an intermediate electrophoretic mobility. Each Pgm allele determines a two-band electrophoretic pattern.

Alleles↗
PubMed2002

The influence of cytosolic phosphoglucomutase on photosynthetic carbohydrate metabolism.

The aim of this work was to examine the role of cytosolic phosphoglucomutase (cPGM; EC 5.4.2.2) in photosynthetic carbon partitioning. We have previously described the generation and characterisation of the tuber metabolism of transgenic potato ( Solanum tuberosum cv. Desiree) lines expressing the StcPGM gene in the antisense orientation under the control of the 35S promoter. Here we extend the characterisation of leaf metabolism within these lines, examining properties of gas exchange, carbon partitioning, and the effect of the genetic manipulation on a wide range of metabolites including metabolites of the sucrose-starch transition, glycolysis, the Krebs cycle and amino acid metabolism. The data acquired in the present study surprisingly reveal that the photosynthetic sucrose synthetic capacity of the leaves is largely unaltered but that these plants display a reduced rate of photosynthesis, a dramatic reduction in nucleotide levels, and a general decline of biosynthesis. We conclude that these lines exhibit only moderate changes in sucrose synthesis but more complex changes on a range of diverse metabolic pathways.

Amino Acids↗
PubMed2001

The contribution of plastidial phosphoglucomutase to the control of starch synthesis within the potato tuber.

The aim of this work was to evaluate the extent to which plastidial phosphoglucomutase (PGM) activity controls starch synthesis within potato (Solanum tuberosum L. cv. Desirée) tubers. The reduction in the activity of plastidial PGM led to both a correlative reduction in starch accumulation and an increased sucrose accumulation. The control coefficient of plastidial PGM on the accumulation of starch was estimated to approximate 0.24. The fluxes of carbohydrate metabolism were measured by investigating the metabolism of [U-14C]glucose in tuber discs from wild-type and transgenic plants. In tuber discs the control coefficient of plastidial PGM over starch synthesis was estimated as 0.36, indicating that this enzyme exerts considerable control over starch synthesis within the potato tuber.

Amino Acids↗
PubMed2002

Antisense repression of cytosolic phosphoglucomutase in potato (Solanum tuberosum) results in severe growth retardation, reduction in tuber number and altered carbon metabolism.

The aim of this work was to investigate the role of cytosolic phosphoglucomutase (PGM; EC 5.4.2.2) in the regulation of carbohydrate metabolism. Many in vitro studies have indicated that PGM plays a central role in carbohydrate metabolism; however, until now the importance of this enzyme in plants has not been subject to reverse-genetics investigations. With this intention we cloned the cytosolic isoform of potato PGM (StcPGM) and expressed this in the antisense orientation under the control of the CaMV 35 S promoter in potato plants. We confirmed that these plants contained reduced total PGM activity and that loss in activity was due specifically to a reduction in cytosolic PGM activity. These plants were characterised by a severe phenotype: stunted aerial growth combined with limited root growth and a reduced tuber yield. Analysis of the metabolism of these lines revealed that leaves of these plants were inhibited in sucrose synthesis whereas the tubers exhibited decreased levels of sucrose and starch as well as decreased levels of glycolytic intermediates but possessed unaltered levels of adenylates. Furthermore, a broader metabolite screen utilising GC-MS profiling revealed that these lines contained altered levels of several intermediates of the TCA cycle and of amino acids. In summary, we conclude that cytosolic PGM plays a crucial role in the sucrose synthetic pathway within the leaf and in starch accumulation within the tuber, and as such is important in the maintenance of sink-source relationships.

Amino Acids↗
PubMed1998

Contribution to the knowledge of Hysterothylacium aduncum through electrophoresis of the enzymes glucose phosphate isomerase and phosphoglucomutase.

A total of 163 Hysterothylacium aduncum specimens, obtained from two gadoids and one percid, were studied by electrophoresis of the enzymes glucose phosphate isomerase and phosphoglucomutase. The two loci deviated significantly from the Hardy-Weinberg equilibrium, both when considering all specimens and when distinguishing the hosts. This could suggest that there is no single species in either case.

Alleles↗
PubMed1978

The structural requirements of glucose for phosphorylation by phosphoglucomutase.

During catalysis, the phosphoryl group of phosphoglucomutase (alpha-D-glucose-1,6-bisphosphate:alpha-D-glucose-1-phosphate phosphotransferase, EC 2.7.5.1) is transferred through a nucleophilic displacement reaction to the monophosphate substrates to form the diphosphate. Some non-phosphorylated analogs of glucose have been shown to serve as effective acceptors of the active phosphate albeit at a much reduced rate. Several other analogs exhibit little or no reactivity. The relative reaction rates of the reactive analogs follow the order: thioglucose greater than alpha- or beta-D-glucose greater than D-xylose, greater than L-arabinose greater than myo-inositol. The rate of transfer increased with the increased concentration of glucose or its analogs. The products of the reaction may be acid stable ester phosphate or acid labile glycosyl phosphate as well as inorganic phosphate. S-phosphoryl (hemiacetal) thioglucose was identified as a product of the 1-thioglucose reaction. It was possible to define certain steric requirements for the orientation of the hydroxyl groups in all the reacting sugars. These requirements are limited to 3 hydroxyl groups and pertain to loci or receptors on the active site of the enzyme. These would correspond in topography to carbons 2, 3 and 4 of the glucose molecule in the enzyme substrate complex. These hydroxyl groups should be oriented equatorially and project below, above and below the plane of the pyranose ring for C-2, C-3 and C-4, respectively.

Glucose↗
PubMed1979

Electrophoretic variation of aconitase and phosphoglucomutase detected in Microtus californicus.

Four electrophoretic variants of cytoplasmic aconitase (citrate (isocitrate) hydro-lyase, EC 4.2.1.3) were detected in a population of Microtus californicus when samples were screened by starch gel electrophoresis using Tris/citrate buffers at pH 7.0 and pH 8.7. Variation at what is presumed to be the phosphoglucomutase-3 locus (alpha-D-glucose-1,6-diphosphate:alpha-D-glucose-1-phosphate phosphotransferase, EC 2.7.5.1) was also detected with liver samples but was not detected in kidney samples or red blood cells lysates. This nongenetic variation is due to oxidation of free sulfhydryl groups.

Aconitate Hydratase↗
PubMed1991

Development of an enzymatic method for the assay of serum magnesium using phosphoglucomutase and glucose-6-phosphate dehydrogenase.

We developed an assay for serum magnesium (Mg) by coupling phosphoglucomutase (EC 2.7.5.1) with glucose-6-phosphate dehydrogenase (EC 1.1.1.49). The kinetic generation of NADPH by the action of the above two enzymes upon glucose-1-phosphate (G-1-P) and glucose-1,6-diphosphate (G-1,6-P) was proportional to the concentration of Mg in serum, and was monitored at 340 nm. The average within-run and day-to-day imprecision (% CVs), as determined from 10 replicate analyses for three sera with different Mg concentrations, were 0.8 to 2.1% and 1.9 to 2.7%, respectively. For 60 clinical samples, including several with lipemia and hemolysis, our method showed good agreement with atomic absorption spectrophotometry and the Xylidyl Blue method. We also present data showing that the method is highly sensitive, rapid, relatively free of interference, and amenable to automation.

Cations↗