A new proposal for the mechanism of glycine hydroxylation as catalyzed by peptidylglycine α-hydroxylating monooxygenase (PHM)

Medical Hypotheses

Volumn 62, Issue 3, 2004, Pages 392-400

  Owen, Terence C ^a   Merkler, David J ^a  

^a UNIVERSITY OF SOUTH FLORIDA   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ALPHA AMIDATING ENZYME; CARBONYL DERIVATIVE; COPPER; GLYCINE; HORMONE PRECURSOR; PEPTIDYLGLYCINE ALPHA HYDROXYLATING MONOOXYGENASE; PEROXIDE; UNCLASSIFIED DRUG; UNSPECIFIC MONOOXYGENASE;

CARBOXY TERMINAL SEQUENCE; CATALYSIS; ELECTRON; ENERGY; ENZYME ACTIVE SITE; ENZYME CONFORMATION; ENZYME KINETICS; ENZYME MECHANISM; ENZYME SUBSTRATE; HYDROXYLATION; IN VIVO STUDY; OXIDATION; PRIORITY JOURNAL; REVIEW;

EID: 1642317603     PISSN: 03069877     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.mehy.2003.11.012     Document Type: Article

References (49)

1. Young SD, Tamburini PP. Enzymatic peptidyl α-amidation proceeds through formation of an α-hydroxyglycine intermediate. J Am Chem Soc 1989;111:1933-4.
2. Katopodis AG, Ping D, May SW. A novel enzyme from bovine neurointermediate pituitary catalyzes dealkylation of α-hydroxyglycine derivatives, thereby functioning sequentially with peptidylglycine α-amidating monooxygenase in peptide amidation. Biochemistry 1990;29:6115-20.
3. Bertelsen AH, Beaudry GA, Galella EA, Jones BN, Ray ML, Mehta NM. Cloning and characterization of two alternatively spliced rat α-amidating enzyme cDNAs from rat medullary thyroid carcinoma. Arch Biochem Biophys 1990;279:87-96.
4. Kulathila R, Merkler KA, Merkler DJ. Enzymatic formation of C-terminal amides. Nat Prod Rep 1999;16:145-54.
5. Prigge ST, Mains RE, Eipper BA, Amzel LM. New insights into copper monooxygenases and peptide amidation: structure, mechanism and function. Cell Mol Life Sci 2000;57:1236-59.
6. Merkler DJ, Young SD. Recombinant type A 75 kDa α-amidating enzyme catalyzes the conversion of glycine extended peptides to peptide amides via an α-hydroxyglycine intermediate. Arch Biochem Biophys 1991;289:192-6.
7. Eipper BA, Perkins SN, Husten EJ, Johnson RC, Keutmann HT, Mains RE. Peptidyl-α-hydroxyglycine α-amidating lyase. Purification, characterization, and expression. J Biol Chem 1991;266:7827-33.
8. Kolhekar AS, Keutmann HT, Mains RE, Quon AS, Eipper BA. Peptidylglycine α-hydroxylating monooxygenase:active site residues, disulfide linkages, and a two-domain model of the catalytic core. Biochemistry 1997;36:10901-9.
9. Prigge ST, Kolhekar AS, Eipper BA, Mains RE, Amzel LM. Amidation of bioactive peptides:the structure of peptidyl-glycine α-hydroxylating monooxygenase. Science 1997;278:1300-5.
10. Prigge ST, Kolhekar AS, Eipper BA, Mains RE, Amzel LM. Substrate-mediated electron transfer in peptidylglycine α-hydroxylating monooxygenase. Nat Struct Biol 1999;6: 976-83.
11. Eipper BA, Mains RE, Glembotski CC. Identification in pituitary tissue of a peptide α-amidation activity that acts on glycine-extended peptides and requires molecular oxygen, copper, and ascorbic Acid. Proc Natl Acad Sci USA 1983;80:5144-8.
12. Freeman JC, Villafranca JJ, Merkler DJ. Redox cycling of enzyme-bound copper during peptide amidation. J Am Chem Soc 1993;115:4923-4.
13. Kulathila R, Consalvo AP, Fitzpatrick PF, Freeman JC, Snyder LM, Villafranca JJ, et al. Bifunctional peptidyl-glycine α-amidating enzyme requires two copper atoms for maximal activity. Arch Biochem Biophys 1994;311: 191-5.
14. Boswell JS, Reedy BJ, Kulathila R, Merkler D, Blackburn NJ. Structural investigations on the coordination environment of the active-site copper centers of recombinant bifunctional peptidylglycine α-amidating enzyme. Biochemistry 1996;35:12241-50.
15. Kizer JS, Bateman Jr RC, Miller CR, Humm J, Busby Jr WH, Youngblood WW. Purification and characterization of a peptidyl glycine monooxygenase from porcine pituitary. Endocrinology 1986;118:2262-7.
16. Gilligan JP, Lovato SJ, Mehta NM, Bertelsen AH, Jeng AY, Tamburini PP. Multiple forms of pepttdyl α-amidating enzyme:purification from rat medullary thyroid carcinoma CA-77 cell-conditioned medium. Endocrinology 1989;124:2729-36.
17. Francisco WA, Merkler DJ, Blackburn NJ, Klinman JP. Kinetic mechanism and intrinsic isotope effects for the peptidylglycine α-amidating enzyme reaction. Biochemistry 1998;37:8244-52.
18. Landymore-Lim AE, Bradbury AF, Smyth DG. The amidating enzyme in pituitary will accept a peptide with C-terminal D-alanine as a substrate. Biochem Biophys Res Commun 1983;117:289-93.
19. Tamburini PP, Young SD, Jones BN, Palmesino RA, Consalvo AP. Peptide substrate specificity of the α-amidating enzyme isolated from rat medullary thyroid CA-77 cells, Int J Pept Protein Res 1990;35:153-6.
20. Ramer SE, Cheng H, Palcic MM, Vederas JC. Formation of peptide amides by peptidylglycine α-amidating monooxygenase:a new assay and stereochemistry of hydrogen loss. J Am Chem Soc 1988;110:8526-32.
21. Ping D, Katopodis AG, May SW. Tandem stereochemistry of peptidylglycine α-monooxygenase and peptidylamidoglycolate lyase, the two enzymes involved in peptide amidation. J Am Chem Soc 1992;114:3998-4000.
22. Merkler DJ. C-Terminal amidated peptides:the importance of the amide to bioactivity and production by in vitro enzymatic amidation of glycine-extended peptides. Enzyme Microb Technol 1994;16:450-6.
23. Katopodis AG, May SW. Novel substrates and inhibitors of peptidylglycine α-amidating monooxygenase. Biochemistry 1990;29:4541-8.
24. Wilcox BJ, Ritenour-Rodgers KJ, Asser AS, et al. N-Acylglycine amidation:implications for the biosynthesis of fatty acid primary amides. Biochemistry 1999;38: 3235-45.
25. Merkler DJ, Glufke U, Ritenour-Rodgers KJ, et al. Formation of nicotinamide from nicotinuric acid by peptidylglycine α-amidating monooxygenase (PAM):a possible alternative route from nicotinic acid (niacin) to NADP in mammals. J Am Chem Soc 1999;121:4904-5.
26. King III L, Barnes S, Glufke U, et al. The enzymatic formation of novel bile acid primary amides. Arch Biochem Biophys 2000;374:107-17.
27. DeBlassio JL, deLong MA, Glufke U, et al. Amidation of salicyluric acid and gentisuric acid:a possible role for peptidylglycine α-amidating monooxygenase in the metabolism of aspirin. Arch Biochem Biophys 2000;383:46-55.
28. 4 as substrates for peptidylglycine α-amidating monooxygenase. Arch Biochem Biophys 2003;412:3-12.
29. 13C NMR shift as proof that bifunctional peptidylglycine α-amidating enzyme is a monooxygenase. Biochemistry 1992;31:7282-8.
30. Noguchi M, Seino H, Kochi H, Okamoto H, Tanaka T, Hirama M. The source of the oxygen atom in the α-hydroxyglycine intermediate of the peptidylglycine α-amidating reaction. Biochem J 1992;283:883-8.
31. Karlin KD. Metalloenzymes, structural motifs, and inorganic models. Science 1993;261:701-8.
32. Solomon EI, Sundaram UM, Machonkin TE. Multicopper oxidases and oxygenases. Chem Rev 1996;96:2563-605.
33. Jaron S, Blackburn NJ. Does superoxide channel between the copper centers in peptidylglycine monooxygenase?. A new mechanism based on carbon monoxide reactivity. Biochemistry 1999;38:15086-96.
34. Bell J, Meskini RE, D'Amato D, Mains RE, Eipper BA. Mechanistic implications of peptidyglycine α-hydroxylating monooxygenase via intrinsic tryptophan fluorescence and mutagenesis. Biochemistry 2003;42:7133-42.
35. Francisco WA, Blackburn NJ, Klinman JP. Oxygen and hydrogen isotope effects in an active site tyrosine to phenylalanine mutant of peptidylglycine α-hydroxylating monooxygenase:mechanistic implications. Biochemistry 2003;42:1813-9.
36. Cuttitta F, Carney DN, Mulshine J, Moody TW, Fedorko J, Fischler A, et al. Bombesin-like peptides can function as autocrine growth factors in human small-cell lung cancer. Nature 1985;316:823-6.
37. Sethi T, Langdon S, Smyth J, Rozengurt E. Growth of small cell lung cancer cells:stimulation by multiple neuropeptides and inhibition by broad spectrum antagonists in vitro and in vivo. Cancer Res (Suppl) 1992;52:2737s-42s.
38. Schally AV, Comaru-Schally AM, Plonowski A, Nagy A, Halmos G, Rekasi Z. Peptide analogs in the therapy of prostate cancer. Prostate 2000;45:158-66.
39. Rocchi P, Boudouresque F, Zamora AJ, Muracciole X, Lechevallier E, Martin P-M, et al. Expression of adrenomedullin and peptide amidation activity In human prostate cancer and in human prostate cancer cell lines. Cancer Res 2001;61:1196-206.
40. Jiménez N, Jongsma J, Calvo A, van der Kwast TH, et al. Peptidylglycine α-amidating monooxygenase-and proadenomedullin-derived peptide-associated neuroendocrine differentiation are induced by androgen deprivation in the neoplastic prostate. Int J Cancer 2001;94:28-34.
41. Treston AM, Scott FM, Vos M, et al. Biochemical characterization of peptide α-amidation enzyme activities of human neuroendocrine lung cancer cell lines. Cell Growth Differ 1993;4:911-20.
42. Vos MD, Scott FM, Iwai N, Treston AM. Expression in human lung cancer cell lines of genes of prohormone processing and the neuroendocrine phenotype. J Cell Biochem Suppl 1996;24:257-68.
43. Saldise L, Martínez A, Montuenga LM, et al. Distribution of peptidylglycine α-amidating monooxygenase (PAM) enzymes in normal human lung and in lung epithelial tumors. J Histochem Cytochem 1996;44:3-12.
44. Martínez A, Treston AM, Saldise L, Montuenga LM, Linnoila RI. Expression of peptidylglycine α-amidating monooxygenase (PAM) enzymes in morphological abnormalities adjacent to pulmonary tumors. Am J Pathol 1996;149:707-16.
45. Iwai N, Martínez A, Miller M-J, Vos M, Mulshine JL, Treston AM. Autocrine growth loops dependent on peptidyl α-amidating enzyme as targets for novel tumor cell growth inhibitors. Lung Cancer 1999;23:209-22.
46. Ogonowski AA, May SW, Moore AB, Barrett LT, O'Bryant CL, Pollock SH. Antiinflammatory and analgesic activity of an inhibitor of neuropeptide amidation. Pharmacol Exp Ther 1997;280:846-53.
47. Erion MD, Tan J, Wong M, Jeng AY. Inhibition of peptidylglycine α-amidating monooxygenase by N-substi-tuted homocysteine analogs. J Med Chem 1994;37: 4430-7.
48. Mounier CE, Shi J, Sirimanne SR, Chen BH, et al. Pyruvate-extended amino acid derivatives as highly potent inhibitors of carboxyl-terminal peptide amidation. J Biol Chem 1997;272:5016-23.
49. Schramm VL. Enzymatic transition states and transition state analog design. Annu Rev Biochem 1998;67:693-720.