Corn leaf phosphoenolpyruvate carboxylases: inhibition of /sup 14/CO/sub 2/ fixation by SO/sub 3//sup 2 -/ and activation by glucose 6-phosphate

Mukerji, S K

doi:10.1016/0003-9861(77)90317-4

Title: Corn leaf phosphoenolpyruvate carboxylases: inhibition of /sup 14/CO/sub 2/ fixation by SO/sub 3//sup 2 -/ and activation by glucose 6-phosphate

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Abstract

Sulfite ion, the hydrated form of SO/sub 2/ which is an air pollutant, was found to be an inhibitor of phosphoenolpyruvate carboxylase(s) isolated from corn leaves. The inhibition was partial even in the presence of excess SO/sub 3//sup 2 -/. It inhibited the enzyme competitively with respect to HCO/sub 3//sup -/, noncompetitively with respect to phosphoenolpyruvate, and uncompetitively with respect to Mg/sup 2 +/. The kinetics of inhibition suggest that an alternate pathway is operative in the presence of SO/sub 3//sup 2 -/. The enzyme(s) were activated by glucose 6-phosphate which affected primarily the affinity of the enzyme for phosphoenolpyruvate. The binding site of glucose 6-phosphate was apparently distinct from the catalytic site of the enzyme since partial destruction of the catalytic site by heat had no effect on the inhibition by SO/sub 3//sup 2 -/, but glucose 6-phosphate lost its activating effect. The inhibition due to SO/sub 3//sup 2 -/ was relieved by glucose 6-phosphate. 18 references, 7 figures, 3 tables.

Authors:: Mukerji, S K

Publication Date:: Sat Jan 01 00:00:00 EST 1977

Research Org.:: Univ. of California, Davis

OSTI Identifier:: 6352751

Resource Type:: Journal Article

Journal Name:: Arch. Biochem. Biophys.; (United States)

Additional Journal Information:: Journal Volume: 182:1

Country of Publication:: United States

Language:: English

Subject:: 63 RADIATION, THERMAL, AND OTHER ENVIRON. POLLUTANT EFFECTS ON LIVING ORGS. AND BIOL. MAT.; CARBOXY-LYASES; ENZYME INHIBITORS; SULFUR TRIOXIDE; BIOLOGICAL EFFECTS; AIR POLLUTION; BIOCHEMICAL REACTION KINETICS; CARBON DIOXIDE FIXATION; CHEMICAL ACTIVATION; GLUCOSE; LEAVES; MAIZE; PHOSPHATES; SULFUR DIOXIDE; ALDEHYDES; CARBOHYDRATES; CARBON-CARBON LYASES; CEREALS; CHALCOGENIDES; ENZYMES; GRASS; HEXOSES; KINETICS; LYASES; MONOSACCHARIDES; ORGANIC COMPOUNDS; OXIDES; OXYGEN COMPOUNDS; PHOSPHORUS COMPOUNDS; PLANTS; POLLUTION; REACTION KINETICS; SACCHARIDES; SULFUR COMPOUNDS; SULFUR OXIDES; 560303* - Chemicals Metabolism & Toxicology- Plants- (-1987)

Citation Formats


                    Mukerji, S K. Corn leaf phosphoenolpyruvate carboxylases: inhibition of /sup 14/CO/sub 2/ fixation by SO/sub 3//sup 2 -/ and activation by glucose 6-phosphate.  United States: N. p., 1977. 
        Web.  doi:10.1016/0003-9861(77)90317-4.

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                    Mukerji, S K. Corn leaf phosphoenolpyruvate carboxylases: inhibition of /sup 14/CO/sub 2/ fixation by SO/sub 3//sup 2 -/ and activation by glucose 6-phosphate.  United States.  https://doi.org/10.1016/0003-9861(77)90317-4

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                    Mukerji, S K. 1977.  
        "Corn leaf phosphoenolpyruvate carboxylases: inhibition of /sup 14/CO/sub 2/ fixation by SO/sub 3//sup 2 -/ and activation by glucose 6-phosphate".  United States.  https://doi.org/10.1016/0003-9861(77)90317-4.

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@article{osti_6352751,

  title        = {Corn leaf phosphoenolpyruvate carboxylases: inhibition of /sup 14/CO/sub 2/ fixation by SO/sub 3//sup 2 -/ and activation by glucose 6-phosphate},

  author       = {Mukerji, S K},

  abstractNote = {Sulfite ion, the hydrated form of SO/sub 2/ which is an air pollutant, was found to be an inhibitor of phosphoenolpyruvate carboxylase(s) isolated from corn leaves. The inhibition was partial even in the presence of excess SO/sub 3//sup 2 -/. It inhibited the enzyme competitively with respect to HCO/sub 3//sup -/, noncompetitively with respect to phosphoenolpyruvate, and uncompetitively with respect to Mg/sup 2 +/. The kinetics of inhibition suggest that an alternate pathway is operative in the presence of SO/sub 3//sup 2 -/. The enzyme(s) were activated by glucose 6-phosphate which affected primarily the affinity of the enzyme for phosphoenolpyruvate. The binding site of glucose 6-phosphate was apparently distinct from the catalytic site of the enzyme since partial destruction of the catalytic site by heat had no effect on the inhibition by SO/sub 3//sup 2 -/, but glucose 6-phosphate lost its activating effect. The inhibition due to SO/sub 3//sup 2 -/ was relieved by glucose 6-phosphate. 18 references, 7 figures, 3 tables.},

  doi          = {10.1016/0003-9861(77)90317-4},

  url          = {https://www.osti.gov/biblio/6352751},
  journal      = {Arch. Biochem. Biophys.; (United States)},
number       = ,

  volume       = 182:1,

  place        = {United States},

  year         = {Sat Jan 01 00:00:00 EST 1977},

  month        = {Sat Jan 01 00:00:00 EST 1977}

}

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