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AMP Deaminase Isozymes in Human Blood Cells

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Purine Metabolism in Man-IV

Part of the book series: Advances in Experimental Medicine and Biology ((AEMB,volume 165))

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Abstract

AMP deaminase catalyzed the effective irreversible hydrolytic deamination of AMP to IMP and ammonia. This enzyme is widely distributed among mammalian cell types and is found in varying amounts among different tissues. Although AMP deaminase has been implicated in a number of physiological processes, its precise roles in cellular function is not clearly understood. It has been proposed that deamination of AMP is important to the purine nucleotide cycle1, and to the interconversion of adenosine, inosine and guano-sine nucleotides2. The importance of AMP deaminase in the regulation and maintenance of adenylate energy charge and adenylate pool size has also been described3.

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References

  1. J. M. Lowenstein and K. Tornheim, Ammonia production in muscle: the purine nucleotide cycle, Science 171: 397 (1971).

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  2. B. Cunningham and J. M. Lowenstein, Regulation of adenylate deaminase by adenosine triphosphate, Biochim. Biophys. Acta 96: 535 (1965).

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  3. A. G. Chapman and D. E. Atkinson, Stabilization of a adenylate energy charge by the adenylate deaminase reaction, J. Biol. Chem. 248: 8309 (1973).

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  4. N. Ogasawara, H. Goto, Y. Yamada, T. Watanabe and T. Asano, AMP deaminase isozymes in human tissues, Biochim. Biophys. Acta 714: 298 (1982).

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© 1984 Springer Science+Business Media New York

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Ogasawara, N., Goto, H., Yamada, Y. (1984). AMP Deaminase Isozymes in Human Blood Cells. In: De Bruyn, C.H.M.M., Simmonds, H.A., Müller, M.M. (eds) Purine Metabolism in Man-IV. Advances in Experimental Medicine and Biology, vol 165. Springer, Boston, MA. https://doi.org/10.1007/978-1-4757-0390-0_12

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  • DOI: https://doi.org/10.1007/978-1-4757-0390-0_12

  • Publisher Name: Springer, Boston, MA

  • Print ISBN: 978-1-4757-0392-4

  • Online ISBN: 978-1-4757-0390-0

  • eBook Packages: Springer Book Archive

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