Skip to main content

Peptidylglycine monooxygenase

  • Chapter
Springer Handbook of Enzymes

Part of the book series: Springer Handbook of Enzymes ((HDBKENZYMES,volume 27))

  • 75 Accesses

This is a preview of subscription content, log in via an institution to check access.

Access this chapter

Chapter
USD 29.95
Price excludes VAT (USA)
  • Available as PDF
  • Read on any device
  • Instant download
  • Own it forever
eBook
USD 259.00
Price excludes VAT (USA)
  • Available as PDF
  • Read on any device
  • Instant download
  • Own it forever
Softcover Book
USD 329.99
Price excludes VAT (USA)
  • Compact, lightweight edition
  • Dispatched in 3 to 5 business days
  • Free shipping worldwide - see info
Hardcover Book
USD 329.99
Price excludes VAT (USA)
  • Durable hardcover edition
  • Dispatched in 3 to 5 business days
  • Free shipping worldwide - see info

Tax calculation will be finalised at checkout

Purchases are for personal use only

Institutional subscriptions

Preview

Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.

References

  1. Glembotski, C.C.: Further characterization of the peptidyl α-amidating enzyme in rat anterior pituitary secretory granules. Arch. Biochem. Biophys., 241, 673–683 (1985)

    Article  PubMed  CAS  Google Scholar 

  2. Bradbury, A.F.; Smyth, D.G.: Enzyme-catalysed peptide amidation. Isolation of a stable intermediate formed by reaction of the amidating enzyme with an imino acid. Eur. J. Biochem., 169, 579–584 (1987)

    Article  PubMed  CAS  Google Scholar 

  3. Bradbury, A.F.; Finnie, M.D.A.; Smyth, D.G.: Mechanism of C-terminal amide formation by pituitary enzymes. Nature, 298, 686–689 (1982)

    Article  PubMed  CAS  Google Scholar 

  4. Gale, J.S.; Mclntosh, J.E.A.; Mclntosh, R.P.: Peptidyl-glycine α-amidating mono-oxygenase activity towards a gonadotropin-releasing-hormone C-terminal peptide substrate, in subcellular fractions of sheep brain and pituitary. Biochem. J., 251, 251–259 (1988)

    PubMed  CAS  Google Scholar 

  5. Beaudry, G.A.; Mehta, N.M.; Ray, M.I.; Bertelsen, A.H.: Purification and characterization of functional recombinant α-amidating enzyme secreted from mammalian cells. J. Biol. Chem., 265, 17694–17699 (1990)

    PubMed  CAS  Google Scholar 

  6. Perkins, S.N.; Husten, E.J.; Eipper, B.A.: The 108-kDA peptidylglycine a- amidating monooxygenase precursor contains two separable enzymatic activities involved in peptide amidation. Biochem. Biophys. Res. Commun., 171, 926–932 (1990)

    Article  PubMed  CAS  Google Scholar 

  7. Katapodis, A.G.; May, S.W.: A new facile trinitrophenylated substrate for peptide α-amidation and its use to characterize PAM activity in chromaffin granules. Biochem. Biophys. Res. Commun., 151, 499–505 (1988)

    Article  Google Scholar 

  8. Suzuki, K.; Shimoi, H.; Iwasaki, Y.; Kawahara, T.; Matsuura, Y.; Nishikawa, Y.: Elucidation of amidating reaction mechanism by frog amidating enzyme, peptidylglycine α-hydroxylating monooxygenase, expressed in insect cell culture. EMBO J., 9, 4259–4265 (1990)

    PubMed  CAS  Google Scholar 

  9. Murthy, A.S.N.; Mains, R.E.; Eipper, B.A.: Purification and characterization of peptidylglycine α-amidating monooxygenase from bovine neurointermediate pituitary. J. Biol. Chem., 261, 1815–1822 (1986)

    PubMed  CAS  Google Scholar 

  10. Merkler, D.J.; Young, S.D.: Recombinant type A rat 75-kDa a-amidating enzyme catalyzes the conversion of glycine-extended peptides to peptide amides via an α-hydroxyglycine intermediate. Arch. Biochem. Biophys., 289, 192–196 (1991)

    Article  PubMed  CAS  Google Scholar 

  11. Glembotski, C.C.; Eipper, B.A.; Mains, R.E.: Characterization of a peptide αamidation activity from rat anterior pituitary. J. Biol. Chem., 259, 6385–6392 (1984)

    PubMed  CAS  Google Scholar 

  12. Mizuno, K.; Sakata, J.; Kojima, M.; Kangawa, K.; Matsuo, H.: Peptide C-terminal α-amidating enzyme purified to homogeneity from Xenopus laevis skin. Biochem. Biophys. Res. Commun., 137, 984–991 (1986)

    Article  PubMed  CAS  Google Scholar 

  13. Mehta, N.M.; Gilligan, J.P.; Jones, B.N.; Bertelsen, A.H.; Roos, B.A.; Birnbaum, R.S.: Purification of a peptidylglycine α-amidating enzyme from transplantable rat medullary thyroid carcinomas. Arch. Biochem. Biophys., 261, 44–54 (1988)

    Article  PubMed  CAS  Google Scholar 

  14. Bradbury, A.F.; Smyth, D.G.: C-Terminal amide formation in peptide hormones. Biogenetics of Neurohormonal Peptides (Hakanson, R., Thorell, J., eds) Academic Press, London, 171–186 (1985)

    Google Scholar 

  15. Bendig, M.M.: Post-translational processing in Xenopus oocytes includes carboxyl-terminal amidation. J. Biol. Chem., 261, 11935–11937 (1986)

    PubMed  CAS  Google Scholar 

  16. Sakata, J.; Mizuno, J.; Matsuo, H.: Tissue distribution and characterization of peptide C-terminal a-amidating activity in rat. Biochem. Biophys. Res. Commun., 140, 230–236 (1986)

    Article  PubMed  CAS  Google Scholar 

  17. Katapodis, A.G.; May, S.W.: Novel substrates and inhibitors of peptidylglycine a-amidating monooxygenase. Biochemistry, 29, 4541–4548 (1990)

    Article  Google Scholar 

  18. Kojima, M.; Mizuno, K.; Kangawa, K.; Matsuo, H.: Purification and characterization of a peptide C-terminal a-amidating enzyme from porcine atrium. J. Biochem., 105, 440–443 (1989)

    PubMed  CAS  Google Scholar 

  19. Tajima, M.; Iida, T.; Yoshida, S.; Komatsu, K.; Namba, R.; Yanagi, M.; Noguchi, M.; Okamoto, H.: The reaction product of peptidylglycine α-amidating enzyme is a hydroxyl derivative at a-carbon of the carboxyl-terminal glycine. J. Biol. Chem., 265, 9602–9605 (1990)

    PubMed  CAS  Google Scholar 

  20. Scopsi, L.; Lee, R.; Gullo, M.; Collini, P.; Husten, E.J.; Eipper, B.A.: Peptidylglycine a-amidating monooxygenase in neuroendocrine tumors: its identification, characterization, quantification, and relation to the grade of morphologic differentiation, amidated peptide content, and granin immunocytochemistry. Appl. Immunohistochem., 6, 120–132 (1998)

    Article  CAS  Google Scholar 

  21. Chikuma, T.; Kocha, T.; Hanaoka, K.; Kato, T.; Ishii, Y.; Tanaka, A.: Characterization of peptidylglycine α-amidating monooxygenase in bovine hypothalamus. Neurochem. Int., 25, 349–354 (1994)

    Article  PubMed  CAS  Google Scholar 

  22. Iwasaki, Y.; Shimoi, H.; Saiki, H.; Nishikawa, Y.: Tissue-specific molecular diversity of amidating enzymes (peptidylglycine α-hydroxylating monooxygenase and peptidylhydroxyglycine N-C lyase) in Xenopus laevis. Eur. J. Biochem., 214, 811–818 (1993)

    Article  PubMed  CAS  Google Scholar 

  23. Suzuki, K.; Ohta, M.; Okamoto, M.; Nishikawa, Y.: Functional expression and characterization of a Xenopus laevis peptidylglycine α-amidating monooxygenase, AE-II, in insect-cell culture. Eur. J. Biochem., 213, 93–98 (1993)

    Article  PubMed  CAS  Google Scholar 

  24. Shimoi, H.; Kawahara, T.; Suzuki, K.; Iwasaki, Y.; Jeng, A.Y.; Nishikawa, Y.: Characterization of a Xenopus laevis skin peptidylglycine α-hydroxylating monooxygenase expressed in insect-cell culture. Eur. J. Biochem., 209, 189–194 (1992)

    Article  PubMed  CAS  Google Scholar 

  25. Boudreault, A.; Castellucci, V.F.; Chretien, M.; Lazure, C.: Identification, purification, and characterization of the molecular forms of Aplysia californica peptidylglycine a-amidating enzyme. J. Neurochem., 66, 2596–2605 (1996)

    Article  PubMed  CAS  Google Scholar 

  26. Oyarce, A.M.; Eipper, B.A.: Neurosecretory vesicles contain soluble and membrane-associated monofunctional and bifunctional peptidylglycine α amidating monoxygenase proteins. J. Neurochem., 60, 1105–1114 (1993)

    Article  PubMed  CAS  Google Scholar 

  27. Girard, B.; Ouafik, L.; Boudouresque, F.: Characterization and regulation of peptidylglycine α-amidating monooxygenase (PAM) expression in H9c2 cardiac myoblasts. Cell Tissue Res., 298, 489–497 (1999)

    PubMed  CAS  Google Scholar 

  28. Merkler, D.J.; Kulathila, R.; Francisco, W.A.; Ash, D.E.; Bell, J.: The irreversible inactivation of two copper-dependent monooxygenases by sulfite: peptidylglycine α-amidating enzyme and dopamine Β-monooxygenase. FEBS Lett., 366, 165–169 (1995)

    Article  PubMed  CAS  Google Scholar 

  29. Takahashi, K.; Onami, T.; Noguchi, M.: Kinetic isotope effects of peptidylglycine α-hydroxylating mono-oxygenase reaction. Biochem. J., 336, 131–137 (1998)

    PubMed  CAS  Google Scholar 

  30. Bell, J.; Ash, D.E.; Snyder, L.M.; Kulathila, R.; Blackburn, N.J.; Merkler, D.J.: Structural and functional investigations on the role of zinc in bifunctional rat peptidylglycine α-amidating enzyme. Biochemistry, 36, 16239–16246 (1997)

    Article  PubMed  CAS  Google Scholar 

  31. Ping, D.; Mounier, C.E.; May, S.W.: Reaction versus subsite stereospecificity of peptidylglycine α-monooxygenase and peptidylamidoglycolate lyase, the two enzymes involved in peptide amidation. J. Biol. Chem., 270, 29250–29255 (1995)

    Article  PubMed  CAS  Google Scholar 

  32. Jaron, S.; Blackburn, N.J.: Characterization of a half-apo derivative of peptidylglycine monooxygenase. Insight into the reactivity of each active site copper. Biochemistry, 40, 6867–6875 (2001)

    Article  PubMed  CAS  Google Scholar 

  33. Francisco, W.A.; Merkler, D.J.; Blackburn, N.J.; Klinman, J.P.: Kinetic mechanism and intrinsic isotope effects for the peptidylglycine α-amidating enzyme reaction. Biochemistry, 37, 8244–8252 (1998)

    Article  PubMed  CAS  Google Scholar 

  34. Jaron, S.; Mains, R.E.; Eipper, B.A.; Blackburn, N.J.: The catalytic role of the copper ligand H172 of peptidylglycine α-hydroxylating monooxygenase (PHM): a spectroscopic study of the H172A mutant. Biochemistry, 41, 13274–13282 (2002)

    Article  PubMed  CAS  Google Scholar 

  35. Francisco, W.A.; Knapp, M.J.; Blackburn, N.J.; Klinman, J.P.: Hydrogen tunneling in peptidylglycine α-hydroxylating monooxygenase. J. Am. Chem. Soc, 124, 8194–8195 (2002)

    Article  PubMed  CAS  Google Scholar 

Download references

Editor information

Editors and Affiliations

Rights and permissions

Reprints and permissions

Copyright information

© 2006 Springer-Verlag Berlin Heidelberg

About this chapter

Cite this chapter

(2006). Peptidylglycine monooxygenase. In: Schomburg, D., Schomburg, I. (eds) Springer Handbook of Enzymes. Springer Handbook of Enzymes, vol 27. Springer, Berlin, Heidelberg. https://doi.org/10.1007/3-540-30439-8_16

Download citation

Publish with us

Policies and ethics