Small-angle X-ray scattering studies on yeast inorganic pyrophosphatase and its interactions with divalent metal ions, inorganic phosphate, and hydroxymethane bisphosphonate

Thiyagarajan, P; Borso, C S; Banerjee, A; Cooperman, B S

doi:10.1002/bip.360230112

Title: Small-angle X-ray scattering studies on yeast inorganic pyrophosphatase and its interactions with divalent metal ions, inorganic phosphate, and hydroxymethane bisphosphonate

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Abstract

Small-angle x-ray scattering studies have been carried out on the enzyme yeast inorganic pyrophosphatase (PPase), and its overall conformational changes on interaction with divalent metal ions (Mg/sup 2 +/ and Mn/sup 2 +/) and with phosphoryl ligands (inorganic phosphate (P/sub i/) and hydroxymethane bisphosphonate (PCHOHP), a nonhydrolyzable inorganic pyrophosphate analog) were assessed. The enzyme undergoes an apparent reduction in size on simultaneous addition of Mg/sup 2 +/ and high P/sub i/ concentration, although neither Mg/sup 2 +/ nor P/sub i/ added separately induced any measurable conformational changes. By contrast, simultaneous addition of Mn/sup 2 +/ and P/sub i/ to PPase does not result in an observable conformational change. However, the overall structure of the enzyme appears to enlarge in the simultaneous presence of Mn/sup 2 +/ ions and PCHOHP. The significance of the structural changes seen in PPase under various conditions is discussed. 21 references, 3 figures, 1 table.

Authors:: Thiyagarajan, P; Borso, C S; Banerjee, A; Cooperman, B S

Publication Date:: Sun Jan 01 00:00:00 EST 1984

Research Org.:: Argonne National Lab., IL

OSTI Identifier:: 5999724

DOE Contract Number:: W-31-109-ENG-38

Resource Type:: Journal Article

Journal Name:: Biopolymers; (United States)

Additional Journal Information:: Journal Volume: 23

Country of Publication:: United States

Language:: English

Subject:: 59 BASIC BIOLOGICAL SCIENCES; MAGNESIUM COMPOUNDS; BIOLOGICAL EFFECTS; MANGANESE COMPOUNDS; ORGANIC PHOSPHORUS COMPOUNDS; PHOSPHATASES; BIOCHEMICAL REACTION KINETICS; X-RAY DIFFRACTION; CATIONS; EXPERIMENTAL DATA; LIGANDS; MOLECULAR STRUCTURE; MORPHOLOGICAL CHANGES; PHOSPHATES; VALENCE; YEASTS; ALKALINE EARTH METAL COMPOUNDS; CHARGED PARTICLES; COHERENT SCATTERING; DATA; DIFFRACTION; ENZYMES; ESTERASES; FUNGI; HYDROLASES; INFORMATION; IONS; KINETICS; MICROORGANISMS; NUMERICAL DATA; ORGANIC COMPOUNDS; OXYGEN COMPOUNDS; PHOSPHORUS COMPOUNDS; PLANTS; REACTION KINETICS; SCATTERING; TRANSITION ELEMENT COMPOUNDS; 550201* - Biochemistry- Tracer Techniques

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                    Thiyagarajan, P, Borso, C S, Banerjee, A, and Cooperman, B S. Small-angle X-ray scattering studies on yeast inorganic pyrophosphatase and its interactions with divalent metal ions, inorganic phosphate, and hydroxymethane bisphosphonate.  United States: N. p., 1984. 
        Web.  doi:10.1002/bip.360230112.

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                    Thiyagarajan, P, Borso, C S, Banerjee, A, & Cooperman, B S. Small-angle X-ray scattering studies on yeast inorganic pyrophosphatase and its interactions with divalent metal ions, inorganic phosphate, and hydroxymethane bisphosphonate.  United States.  https://doi.org/10.1002/bip.360230112

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                    Thiyagarajan, P, Borso, C S, Banerjee, A, and Cooperman, B S. 1984.  
        "Small-angle X-ray scattering studies on yeast inorganic pyrophosphatase and its interactions with divalent metal ions, inorganic phosphate, and hydroxymethane bisphosphonate".  United States.  https://doi.org/10.1002/bip.360230112.

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@article{osti_5999724,

  title        = {Small-angle X-ray scattering studies on yeast inorganic pyrophosphatase and its interactions with divalent metal ions, inorganic phosphate, and hydroxymethane bisphosphonate},

  author       = {Thiyagarajan, P and Borso, C S and Banerjee, A and Cooperman, B S},

  abstractNote = {Small-angle x-ray scattering studies have been carried out on the enzyme yeast inorganic pyrophosphatase (PPase), and its overall conformational changes on interaction with divalent metal ions (Mg/sup 2 +/ and Mn/sup 2 +/) and with phosphoryl ligands (inorganic phosphate (P/sub i/) and hydroxymethane bisphosphonate (PCHOHP), a nonhydrolyzable inorganic pyrophosphate analog) were assessed. The enzyme undergoes an apparent reduction in size on simultaneous addition of Mg/sup 2 +/ and high P/sub i/ concentration, although neither Mg/sup 2 +/ nor P/sub i/ added separately induced any measurable conformational changes. By contrast, simultaneous addition of Mn/sup 2 +/ and P/sub i/ to PPase does not result in an observable conformational change. However, the overall structure of the enzyme appears to enlarge in the simultaneous presence of Mn/sup 2 +/ ions and PCHOHP. The significance of the structural changes seen in PPase under various conditions is discussed. 21 references, 3 figures, 1 table.},

  doi          = {10.1002/bip.360230112},

  url          = {https://www.osti.gov/biblio/5999724},
  journal      = {Biopolymers; (United States)},
number       = ,

  volume       = 23,

  place        = {United States},

  year         = {Sun Jan 01 00:00:00 EST 1984},

  month        = {Sun Jan 01 00:00:00 EST 1984}

}

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