Formation of nicotinamide from nicotinuric acid by peptidylglycine α- amidating monooxygenase (PAM): A possible alternative route from nicotinic acid (niacin) to NADP in mammals [7]

Journal of the American Chemical Society

Volumn 121, Issue 20, 1999, Pages 4904-4905

  Merkler, David J ^a   Glufke, Uta ^b   Ritenour Rodgers, Kimberly J ^a   Baumgart, Laura E ^a   DeBlassio, Jodi L ^a   Merkler, Kathleen A ^a   Vederas, John C ^b  

^a DUQUESNE UNIVERSITY   (United States)

^b UNIVERSITY OF ALBERTA   (Canada)

Author keywords

[No Author keywords available]

Indexed keywords

ALPHA AMIDATING ENZYME; COPPER; NICOTINAMIDE; NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE; NICOTINIC ACID; NICOTINURIC ACID; ZINC;

ANIMAL CELL; ANIMAL TISSUE; CARBOXY TERMINAL SEQUENCE; CHEMICAL REACTION KINETICS; ENZYME ANALYSIS; ENZYME METABOLISM; HYDROXYLATION; LETTER; NONHUMAN; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PROTEIN PROCESSING; RAT; STRUCTURE ANALYSIS; X RAY ANALYSIS;

EID: 0033606237     PISSN: 00027863     EISSN: None     Source Type: Journal    
DOI: 10.1021/ja990517e     Document Type: Letter

References (35)

1. Bradbury, A. F.; Finnie, M. D. A.; Smyth, D. G. Nature (London) 1982, 298, 686-688.
2. For reviews, see: (a) Kulathila, R.; Merkler, K. A.; Merkler, D. J. Nat. Prod. Rep. 1999, 16, 145-154.
3. (b) Eipper, B. A.; Stoffers, D. A.; Mains, R. E. Annu. Rev. Neurosci. 1992, 15, 57-85.
4. (a) Zabriskie, T. M.; Klinge, M.; Szymanski, C. M.; Cheng, H.; Vederas, J. C. Arch. Insect Biochem. Physiol. 1994, 26, 27-48.
5. (b) Kolhekar, A. S.; Roberts, M. S.; Jiang, N.; Johnson, R. C.; Mains, R. E.; Eipper, B. A.; Taghert, P. H. J. Neurosci. 1997, 17, 1363-1376.
6. (c) Grimmelikhuijzen, C. J. P.; Leviev, I.; Carstensen, K. Int. Rev. Cytol. 1996, 167, 37-89.
7. Prigge, S. T.; Kolhekar, A. S.; Eipper, B. A.; Mains, R. E.; Amzel, L. M. Science 1998, 278, 1300-1305.
8. PHM has homology to dopamine β-monooxygenase: Francisco, W. A.; Merkler, D. J.; Blackburn, N. J.; Klinman, J. P. Biochemistry 1998, 37, 8244-8252.
9. (a) Merkler, D. J.; Merkler, K. A.; Stern, W.; Fleming, F. F. Arch. Biochem. Biophys. 1996, 330, 430-434.
10. (b) Wilcox, B. J.; Ritenour-Rodgers, J.; Asser, A. S.; Baumgart, L. E.; Baumgart, M. A.; Boger, D. L.; DeBlassio, J. L.; deLong, M. A.; Glufke, U.; Henz, M. E.; King, L., III; Kulathila, R.; Merkler, K. A.; Patterson, J. E.; Robleski, J. J.; Vederas, J. C.; Merkler, D. J. Biochemistry 1999, 38, 3235-3245.
11. Specificity for the glycine skeleton is high but some D-amino acids can be substituted: Andrews, M. D.; O'Callaghan, K. A.; Vederas, J. C. Tetrahedron 1997, 53, 8295-8306.
12. (a) Lerner, R. A.; Siuzdak, G.; Prospero-Garcia, O.; Henriksen, S. J.; Boger, D. L.; Cravatt, B. F. Proc. Natl. Acad. Sci. U.S.A. 1994, 91, 9505-9508.
13. (b) Cravatt, B. F.; Prospero-Garcia, O.; Siuzdak, G.; Gilula, N. B.; Henriksen, S. J.; Boger, D. L.; Lerner, R. A. Science 1995, 268, 1506-1509.
14. (c) Boger, D. L.; Henriksen, S. J.; Cravatt, B. F. Curr. Pharm. Des. 1998, 4, 303-314.
15. (a) Bartlett, K.; Gompertz, D. Biochem. Med. 1974, 10, 15-23.
16. (b) Gregersen, N.; Kølvraa, S.; Mortensen, P. B. Biochem. Med. Metab. Biol. 1986, 35, 210-218.
17. (a) Neuvonen, P. J.; Roivas, L.; Laine, K.; Sundholm, O. Br. J. Clin. Pharmacol. 1991, 32, 473-476.
18. (b) Stern, R.; Freeman, D.; Spence, J. D. Metabolism 1992, 41, 879-881.
19. (c) Iwaki, M.; Ogiso, T.; Hayashi, H.; Tanino, T. Benet, L. Z. Drug Metab. Dispos. 1996, 24, 773-779.
20. For reviews of NAD(P) biosynthesis, see: (a) Ijichi, H.; Ichiyama, A.; Hayaishi, O. J. Biol. Chem. 1966, 241, 3701-3707.
21. (b) Moat, A. G.; Foster, J. W. Pyridine Nucleotide Coenzymes, Part B. In Coenzymes and Cofactors; Dolphin, D., Poulson, R., Avramovic, O., Eds.; Wiley: New York, 1987; Vol II, pp 1-24.
22. (c) DiPalma, J. R. In Vitamins; Friedrich, W., Ed.; Walter de Gruyter: Berlin, 1988; pp 473-542.
23. Miller, D. A.; Sayad, K. U.; Kulathila, R.; Beaudry, G. A.; Merkler, D. J.; Bertelsen, A. H. Arch. Biochem. Biophys. 1992, 298, 380-388.
24. Katopodis, A. G.; May, S. W. Biochemistry 1990, 29, 4541-4548.
25. Nicotinuric acid, N-nicotinoyl-α-hydroxyglycine, and nicotinamide were resolved at 50 °C on a Keystone Scientific ODS Hypersil column (100 × 4.6 mm). Isocratic elution was achieved using a mobile phase of 200 mM sodium acetate pH 6.6, and analytes were detected by UV absorbance at 246 nm.
26. Rohrlich, M. Arch. Pharm. (Weinheim, Ger.) 1951, 284, 6-7.
27. 2O), pD 5.6, total volume 1.6 mL, is incubated at 37 °C for 4 h. PAM is then removed using an Amicon Centricon-30 ultrafiltration device. An aliquot (0.7 mL) of the reaction mixture is analyzed by HMQC NMR using an Inova 600 Varian instrument.
28. Mounier, C. E.; Shi, J.; Sirimanne, S. R.; Chen, B.-H.; Moore, A. B.; Gill-Woznichak, M. M.; Ping, D.; May, S. W. J. Biol. Chem. 1997, 272, 5016-5023.
29. Although dietary tryptophan can provide up to two-thirds of the human requirement for niacin, the efficiency of conversion is very low. In contrast, nicotinamide (3) is very efficiently converted to NAD(P). See ref 11c, page 490.
30. 2. The livers were stored at -70 °C until analysis, see ref 10c.
31. Wong, C.-H.; Whitesides, G. M. In Enzymes in Synthetic Organic Chemistry; Pergamon-Elsevier: Tarrytown, NY, 1994; pp 139-194.
32. (a) Riss, T. L.; Zorich, N. L.; Williams, M. D.; Richardson, A. J. Liq. Chromatogr. 1980, 3, 133-158.
33. (b) Brown, E. G.; Newton, R. P.; Shaw, N. M. Anal. Biochem. 1982, 123, 378-388.
34. Rising, K. A.; Schramm, V. L. J. Am. Chem. Soc. 1997, 119, 27-37.
35. 2H).