Purified inositol hexakisphosphate kinase is an ATP synthase: Diphosphoinositol pentakisphosphate as a high-energy phosphate donor

Susan M. Voglmaier; Michael E. Bembenek; Adam I. Kaplin; György Dormán; John D. Olszewski; Glenn D. Prestwich; Solomon H. Snyder

doi:10.1073/pnas.93.9.4305

Purified inositol hexakisphosphate kinase is an ATP synthase: Diphosphoinositol pentakisphosphate as a high-energy phosphate donor

Susan M. Voglmaier, Michael E. Bembenek, Adam I. Kaplin, György Dormán, John D. Olszewski, Glenn D. Prestwich, Solomon H. Snyder

School of Medicine

Research output: Contribution to journal › Article › peer-review

124 Scopus citations

Abstract

Diphosphoinositol pentakisphosphate (PP-IP₅) and bis(diphospho)inositol tetrakisphosphate (bis-PP-IP₄) are recently identified inositol phosphates that possess pyrophosphate bonds. We have purified an inositol hexakisphosphate (IP₆) kinase from rat brain supernatants. The pure protein, a monomer of 54 kDa, displays high affinity (K(m) = 0.7 μM) and selectivity for inositol hexakisphosphate as substrate. It can be dissociated from bis(diphospho)inositol tetrakisphosphate synthetic activity. The purified enzyme transfers a phosphate from PP-IP₅ to ADP to form ATP. This ATP synthase activity indicates the high phosphate group transfer potential of PP-IP₅ and may represent a physiological role for PP-IP₅.

Original language	English (US)
Pages (from-to)	4305-4310
Number of pages	6
Journal	Proceedings of the National Academy of Sciences of the United States of America
Volume	93
Issue number	9
DOIs	https://doi.org/10.1073/pnas.93.9.4305
State	Published - Apr 30 1996

Keywords

phosphotransferase
pyrophosphate

ASJC Scopus subject areas

General

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10.1073/pnas.93.9.4305

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Voglmaier, S. M., Bembenek, M. E., Kaplin, A. I., Dormán, G., Olszewski, J. D., Prestwich, G. D., & Snyder, S. H. (1996). Purified inositol hexakisphosphate kinase is an ATP synthase: Diphosphoinositol pentakisphosphate as a high-energy phosphate donor. Proceedings of the National Academy of Sciences of the United States of America, 93(9), 4305-4310. https://doi.org/10.1073/pnas.93.9.4305

Purified inositol hexakisphosphate kinase is an ATP synthase: Diphosphoinositol pentakisphosphate as a high-energy phosphate donor. / Voglmaier, Susan M.; Bembenek, Michael E.; Kaplin, Adam I. et al.
In: Proceedings of the National Academy of Sciences of the United States of America, Vol. 93, No. 9, 30.04.1996, p. 4305-4310.

Research output: Contribution to journal › Article › peer-review

Voglmaier, SM, Bembenek, ME, Kaplin, AI, Dormán, G, Olszewski, JD, Prestwich, GD & Snyder, SH 1996, 'Purified inositol hexakisphosphate kinase is an ATP synthase: Diphosphoinositol pentakisphosphate as a high-energy phosphate donor', Proceedings of the National Academy of Sciences of the United States of America, vol. 93, no. 9, pp. 4305-4310. https://doi.org/10.1073/pnas.93.9.4305

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title = "Purified inositol hexakisphosphate kinase is an ATP synthase: Diphosphoinositol pentakisphosphate as a high-energy phosphate donor",

abstract = "Diphosphoinositol pentakisphosphate (PP-IP5) and bis(diphospho)inositol tetrakisphosphate (bis-PP-IP4) are recently identified inositol phosphates that possess pyrophosphate bonds. We have purified an inositol hexakisphosphate (IP6) kinase from rat brain supernatants. The pure protein, a monomer of 54 kDa, displays high affinity (K(m) = 0.7 μM) and selectivity for inositol hexakisphosphate as substrate. It can be dissociated from bis(diphospho)inositol tetrakisphosphate synthetic activity. The purified enzyme transfers a phosphate from PP-IP5 to ADP to form ATP. This ATP synthase activity indicates the high phosphate group transfer potential of PP-IP5 and may represent a physiological role for PP-IP5.",

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AU - Bembenek, Michael E.

AU - Kaplin, Adam I.

AU - Dormán, György

AU - Olszewski, John D.

AU - Prestwich, Glenn D.

AU - Snyder, Solomon H.

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AB - Diphosphoinositol pentakisphosphate (PP-IP5) and bis(diphospho)inositol tetrakisphosphate (bis-PP-IP4) are recently identified inositol phosphates that possess pyrophosphate bonds. We have purified an inositol hexakisphosphate (IP6) kinase from rat brain supernatants. The pure protein, a monomer of 54 kDa, displays high affinity (K(m) = 0.7 μM) and selectivity for inositol hexakisphosphate as substrate. It can be dissociated from bis(diphospho)inositol tetrakisphosphate synthetic activity. The purified enzyme transfers a phosphate from PP-IP5 to ADP to form ATP. This ATP synthase activity indicates the high phosphate group transfer potential of PP-IP5 and may represent a physiological role for PP-IP5.

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Purified inositol hexakisphosphate kinase is an ATP synthase: Diphosphoinositol pentakisphosphate as a high-energy phosphate donor

Abstract

Keywords

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