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Bioenergetics of the Cell: Quantitative Aspects pp 169–182Cite as

Adenylate kinase: Kinetic behavior in intact cells indicates it is integral to multiple cellular processes

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Part of the book series: Developments in Molecular and Cellular Biochemistry ((DMCB,volume 25))

Abstract

Monitoring the kinetic behavior of adenylate kinase (AK) and creatine kinase (CK) in intact cells by 18O-phosphoryl oxygen exchange analysis has provided new perspectives from which to more fully define the involvement of these phosphotransferases in cellular bioenergetics. A primary function attributable to both AK and CK is their apparent capability to couple ATP utilization with its generation by glycolytic and/or oxidative processes depending on cell metabolic status. This is evidenced by the observation that the sum of the net AK- plus CK-catalyzed phosphoryl transfer is equivalent to about 95% of the total ATP metabolic flux in non-contracting rat diaphragm; under basal conditions almost every newly generated ATP molecule appears to be processed by one or the other of these phosphotransferases prior to its utilization. Although CK accounts for the transfer of a majority of the ATP molecules generated/consumed in the basal state there is a progressive, apparently compensatory, shift in phosphotransfer catalysis from the CK to the AK system with increasing muscle contraction or graded chemical inhibition of CK activity. AK and CK appear therefore to provide similar and interrelated functions. Evidence that high energy phosphoryl transfer in some cell types or metabolic states can also be provided by specific nucleoside mono- and diphosphate kinases and by the phosphotransfer capability inherent to the glycolytic system has been obtained. Measurements by 18O-exchange analyses of net AK- and CK-catalyzed phosphoryl transfer in conjunction with 31P NMR analyses of total unidirectional phosphoryl flux show that each new energy-bearing molecule CK or AK generates subsequently undergoes about 50 or more unidirectional CK-or AK-catalyzed phosphotransfers en route to an ATP consumption site in intact muscle. This evidence of multiple enzyme catalyzed exchanges coincides with the mechanism of vectorial ligand conduction suggested for accomplishing intracellular high energy phosphoryl transfer by the AK and CK systems. AK-catalyzed phosphotransfer also appears to be integral to the transduction of metabolic signals influencing the operation of ion channels regulated by adenine nucleotides such as ATP-inhibitable K+ channels in insulin secreting cells; transition from the ATP to ADP liganded states closely coincides with the rate AK-catalyzes phosphotransfer transforming ATP (+AMP) to (2) ADP.(Mol Cell Biochem 184:: 169–182, 1998)

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Authors and Affiliations

  1. Department of Biochemistry, University of Minnesota, Medical School, Minneapolis, Minnesota, 55455, USA

    Petras P. Dzeja, Robert J. Zeleznikar & Nelson D. Goldberg

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  1. Petras P. Dzeja
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  2. Robert J. Zeleznikar
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Editor information

Editors and Affiliations

  1. Laboratories of Bioenergetics, Institute of Chemical and Biological Physics, Tallinn, Estonia

    Valdur A. Saks

  2. Cellular and Molecular Cardiology, U 446 INSERM, Chatenay-Malabry, France

    Renée Ventura-Clapier

  3. Laboratory of Bioenergetics, Joseph Fourier University, Grenoble, France

    Valdur A. Saks , Xavier Leverve  & André Rossi ,  & 

  4. Laboratory of Bioenergetics, Institute of Biochemistry and Cellular Genetics CNRS, Bordeaux, France

    Michel Rigoulet

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Dzeja, P.P., Zeleznikar, R.J., Goldberg, N.D. (1998). Adenylate kinase: Kinetic behavior in intact cells indicates it is integral to multiple cellular processes. In: Saks, V.A., Ventura-Clapier, R., Leverve, X., Rossi, A., Rigoulet, M. (eds) Bioenergetics of the Cell: Quantitative Aspects. Developments in Molecular and Cellular Biochemistry, vol 25. Springer, Boston, MA. https://doi.org/10.1007/978-1-4615-5653-4_13

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  • DOI: https://doi.org/10.1007/978-1-4615-5653-4_13

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