Inhibition of phosphoglucose isomerase allozymes from the wing polymorphic waterstrider, Limnoporus canaliculatus, by pentose shunt metabolites View Full Text


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Article Info

DATE

1987-04

AUTHORS

Anthony J. Zera

ABSTRACT

Inhibition of phosphoglucose isomerase (PGI) allozymes from the wing-polymorphic waterstrider, Limnoporus canaliculatus, by three pentose-shunt metabolites was studied at several different temperatures. This was done to determine if the allozymes exhibited a differential ability to participate in lipid biosynthesis via differential partitioning of carbon flux through the pentose shunt versus glycolysis. 6-Phosphogluconate and erythrose-4-phosphate proved to be strong competitive inhibitors of PGI, while sedoheptulose-7-phosphate was a very weak inhibitor. The PGI allozymes from L. canaliculatus were differentially inhibited by 6-phosphogluconate at two of the three temperatures studied. However, this property does not appear to be an adaptive difference between the allozymes but, rather, a correlated effect resulting from variation in substrate binding. Estimates of reaction rates for the allozymes indicate that the differences in inhibition result in no detectable differences in reaction velocities. Thus, no evidence in support of the hypothesis that PGI allozymes from Limnoporus canaliculatus were adapted to function in different metabolic capacities via differential inhibition was obtained in this study. However, the importance of this characteristic in allozymic adaptation in natural populations remains an open question. More... »

PAGES

205-223

References to SciGraph publications

  • 1985-10. Temperature-related kinetic differentiation of glucosephosphate isomerase alleloenzymes isolated from the blue mussel,Mytilus edulis in BIOCHEMICAL GENETICS
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  • 1981-08. Extensive variation at the α-glycerophosphate dehydrogenase locus in species of waterstriders (Gerridae: Hemiptera) in BIOCHEMICAL GENETICS
  • 1981-02. Evolutionary genetics of Metridium senile. II. Geographic patterns of allozyme variation in BIOCHEMICAL GENETICS
  • 1981-02. Evolutionary genetics of Metridium senile. I. Kinetic differences in phosphoglucose isomerase allozymes in BIOCHEMICAL GENETICS
  • 1985-10. Temperature-related kinetic differentiation of glucosephosphate isomerase alleloenzymes isolated from the blue mussel,Mytilus edulis in BIOCHEMICAL GENETICS
  • 1981-06. Purification and characterization of two allozymic forms of octopine dehydrogenase from California populations ofMetridium senile in JOURNAL OF COMPARATIVE PHYSIOLOGY A
  • 1970-08. Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4 in NATURE
  • 1980-03. Glucosephosphate isomerase (GPI) of the teleostFundulus heteroclitus (linnaeus): Isozymes, allozymes and their physiological roles in JOURNAL OF COMPARATIVE PHYSIOLOGY A
  • 1983. The Evolution of Enzyme Catalytic Efficiency and Adaptive Inference from Steady-State Kinetic Data in EVOLUTIONARY BIOLOGY
  • 1975. Initial Rate Enzyme Kinetics in NONE
  • Identifiers

    URI

    http://scigraph.springernature.com/pub.10.1007/bf00499314

    DOI

    http://dx.doi.org/10.1007/bf00499314

    DIMENSIONS

    https://app.dimensions.ai/details/publication/pub.1053557020

    PUBMED

    https://www.ncbi.nlm.nih.gov/pubmed/3606558


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