S-Adenosylmethionine decarboxylase

Essays in Biochemistry

Volumn 46, Issue 1, 2009, Pages 25-45

  Pegg, Anthony E ^a  

^a PENN STATE COLLEGE OF MEDICINE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

MAMMALIA;

ADENOSYLMETHIONINE DECARBOXYLASE; POLYAMINE;

AMINO ACID SEQUENCE; ANIMAL; BACTERIUM; BIOCHEMISTRY; BIOLOGICAL MODEL; CHEMICAL MODEL; CONFORMATION; ENZYME ACTIVE SITE; HUMAN; METABOLISM; METHODOLOGY; MOLECULAR GENETICS; PROTEIN BINDING; REVIEW; SEQUENCE HOMOLOGY;

ADENOSYLMETHIONINE DECARBOXYLASE; AMINO ACID SEQUENCE; ANIMALS; BACTERIA; BIOCHEMISTRY; CATALYTIC DOMAIN; HUMANS; MODELS, BIOLOGICAL; MODELS, CHEMICAL; MOLECULAR CONFORMATION; MOLECULAR SEQUENCE DATA; POLYAMINES; PROTEIN BINDING; SEQUENCE HOMOLOGY, AMINO ACID;

EID: 77449159833     PISSN: 00711365     EISSN: None     Source Type: Journal    
DOI: 10.1042/BSE0460003     Document Type: Article

References (45)

1. Wallace, H.M., Fraser, A.V. and Hughes, A. (2003) A perspective of polyamine metabolism. Biochem. J. 376, 1-14
2. Ikeguchi, Y., Bewley, M. and Pegg, A.E. (2006) Aminopropyltransferases: function, structure and genetics. J. Biochem. 139, 1-9
3. Tabor, H., Rosenthal, S.M. and Tabor, C.W. (1958) The biosynthesis of spermidine and spermine from putrescine and methionine. J. Biol. Chem. 233, 907-914
4. Tait, G.H. (1976) A new pathway for the biosynthesis of spermidine. Biochem. Soc. Trans. 4, 610-612
5. Lee, J., Sperandio, V., Frantz, D.E., Longgood, J., Camilli, A., Phillips, M.A. and Michael, A.J. (2009) An alternative polyamine biosynthetic pathway is widespread in bacteria and essential for biofilm formation in Vibrio cholerae. J. Biol. Chem. 284, 9899-9907
6. Hibasami, H., Hoffman, J.L. and Pegg, A.E. (1980) Decarboxylated S-adenosylmethionine in mammalian cells. J. Biol. Chem. 255, 6675-6678
7. Pegg, A.E., Wechter, R.S., Clark, R.S., Wiest, L. and Erwin, B.G. (1986) Acetylation of decarboxylated S-adenosylmethionine by mammalian cells. Biochemistry 25, 379-384
8. Wagner, J., Hirth, Y., Piriou, F., Zakett, D., Claverie, N. and Danzin, C. (1985) N-Acetyl decarboxylated S-adenosylmethionine, a new metabolite of decarboxylated S-adenosylmethionine: isolation and characterization. Biochem. Biophys. Res. Commun. 133, 546-553
9. Wu, H., Min, J., Zeng, H., McCloskey, D.E., Ikeguchi, Y., Loppnau, P., Michael, A.J., Pegg, A.E. and Plotnikov, A.N. (2008) Crystal structure of human spermine synthase: implications of substrate binding and catalytic mechanism. J. Biol. Chem. 283, 16135-16146
10. Vinci, C.R. and Clarke, S.G. (2007) Recognition of age-damaged (R,S)-adenosyl-L-methionine by two methyltransferases in the yeast Saccharomyces cerevisiae. J. Biol. Chem. 282, 8604-8612
11. Dejima, H., Kobayashi, M., Takasaki, H., Takeda, N., Shirahata, A. and Samejima, K. (2003) Synthetic decarboxylated S-adenosyl-L-methionine as a substrate for aminopropyl transferases. Biol. Pharm. Bull. 26, 1005-1008
12. Lu, Z.J. and Markham, G.D. (2007) Metal ion activation of S-adenosylmethionine decarboxylase reflects cation charge density. Biochemistry 46, 8172-8180
13. Pegg, A.E. and Williams-Ashman, H.G. (1968) Stimulation of the decarboxylation of S-adenosylmethionine by putrescine in mammalian tissues. Biochem. Biophys. Res. Commun. 30, 76-82
14. Xiong, H., Stanley, B.A., Tekwani, B.L. and Pegg, A.E. (1997) Processing of mammalian and plant S-adenosylmethionine decarboxylase proenzymes. J. Biol. Chem. 272, 28342-28348
15. Bennett, E.M., Ekstrom, J.L., Pegg, A.E. and Ealick, S.E. (2002) Monomeric S-adenosylmethionine decarboxylase from potato provides an alternative to putrescine stimulation. Biochemistry 41, 14509-14517
16. Willert, E.K., Fitzpatrick, R. and Phillips, M.A. (2007) Allosteric regulation of an essential trypanosome polyamine biosynthetic enzyme by a catalytically dead homolog. Proc. Natl. Acad. Sci. U.S.A. 104, 8275-8280
17. Wells, G.A., Birkholtz, L.M., Joubert, F., Walter, R.D. and Louw, A.I. (2005) Novel properties of malarial S-adenosylmethionine decarboxylase as revealed by structural modelling. J. Mol. Graph. Model. 24, 307-318
18. Tolbert, W.D., Zhang, Y., Bennett, E.M., Cotter, S.E., Ekstrom, J.L., Pegg, A.E. and Ealick, S.E. (2003) Mechanism of human S-adenosylmethionine decarboxylase proenzyme processing as revealed by the structure of the S68A mutant. Biochemistry 42, 2386-2395
19. Ekstrom, J.L., Tolbert, W.D., Xiong, H., Pegg, A.E. and Ealick, S.E. (2001) Structure of a human S-adenosylmethionine decarboxylase self-processing ester intermediate and mechanism of putrescine stimulation of processing as revealed by the H243A mutant. Biochemistry 40, 9495- 9504
20. Tolbert, W.D., Ekstrom, J.L., Mathews, I.I., Secrist, J.A. I., Kapoor, P., Pegg, A.E. and Ealick, S.E. (2001) The structural basis for substrate specificity and inhibition of human S-adenosylmethionine decarboxylase. Biochemistry 40, 9484-9494
21. McCloskey, D.E., Bale, S., Secrist, J.A., Tiwari, A., Moss, T.H., Valiyaveettil, J., Brooks, W.H., Guida, W.C., Pegg, A.E. and Ealick, S.E. (2009) New insights into the design of inhibitors of human S-adenosylmethionine decarboxylase: studies of adenine C8 substitution in structural analogues of S-adenosylmethionine. J. Med. Chem. 52, 1388-1407
22. Toms, A.V., Kinsland, C., McCloskey, D.E., Pegg, A.E. and Ealick, S.E. (2004) Evolutionary links as revealed by the structure of Thermotoga maritima S-adenosylmethionine decarboxylase. J. Biol. Chem. 279, 33837-33846
23. Hackert, M.L. and Pegg, A.E. (1997) Pyruvoyl-dependent enzymes. In Comprehensive Biological Catalysis (Sinnott, M.L., ed.), pp. 201-216, Academic Press, London
24. Xiong, H., Stanley, B.A. and Pegg, A.E. (1999) Role of cysteine-82 in the catalytic mechanism of human S-adenosylmethionine decarboxylase. Biochemistry 38, 2462-2470
25. Xiong, H. and Pegg, A.E. (1999) Mechanistic studies of the processing of human S-adenosylmethionine decarboxylase proenzyme. Isolation of an ester intermediate. J. Biol. Chem. 274, 35059-35066
26. Recsei, P.A., Huynh, Q.K. and Snell, E.E. (1983) Conversion of prohistidine decarboxylase to histidine decarboxylase: peptide chain cleavage by nonhydrolytic serinolysis. Proc. Natl. Acad. Sci. U.S.A. 80, 973-977
27. Paulus, H. (2002) Protein splicing and related forms of protein autoprocessing. Annu. Rev. Biochem. 69, 447-496
28. Hillary, R.A. and Pegg, A.E. (2003) Decarboxylases involved in polyamine biosynthesis and their inactivation by nitric oxide. Biochim. Biophys. Acta 1647, 161-166
29. Kameji, T. and Pegg, A.E. (1987) Effect of putrescine on the synthesis of S-adenosylmethionine decarboxylase. Biochem. J. 243, 285-288
30. Pegg, A.E. and Williams-Ashman, H.G. (1969) On the role of S-adenosyl-L-methionine in the biosynthesis of spermidine by the rat prostate. J. Biol. Chem. 244, 682-693
31. Stanley, B.A. (1995) Mammalian S-adenosylmethionine decarboxylase regulation and processing. In Polyamines: Regulation and Molecular Interaction (Casero, Jr, R.A., ed.), pp. 27-75, R.G. Landes Company, Austin
32. Pegg, A.E., Xiong, H., Feith, D. and Shantz, L.M. (1998) S-Adenosylmethionine decarboxylase: structure, function and regulation by polyamines. Biochem. Soc. Trans. 26, 580-586
33. Bale, S., Lopez, M.M., Makhatadze, G.I., Fang, Q., Pegg, A.E. and Ealick, S.E. (2008) Structural basis for putrescine activation of human S-adenosylmethionine decarboxylase. Biochemistry 47, 13404- 13417
34. Stanley, B.A., Shantz, L.M. and Pegg, A.E. (1994) Expression of mammalian S-adenosylmethionine decarboxylase in E. coli. Determination of sites for putrescine activation of activity and processing. J. Biol. Chem. 269, 7901-7907
35. Pegg, A.E. and McCann, P.P. (1992) S-Adenosylmethionine decarboxylase as an enzyme target for therapy. Pharmacol. Ther. 56, 359-377
36. Barker, Jr, R.H., Liu, H., Hirth, B., Celatka, C.A., Fitzpatrick, R., Xiang, Y., Willert, E.K., Phillips, M.A., Kaiser, M., Bacchi, C.J. et al. (2009) Novel S-adenosylmethionine decarboxylase inhibitors for the treatment of human African trypanosomiasis. Antimicrob. Agents Chemother. 53, 2052- 2058
37. Williams-Ashman, H.G. and Schenone, A. (1972) Methylglyoxal bis(guanylhydrazone) as a potent inhibitor of mammalian and yeast S-adenosylmethionine decarboxylases. Biochem. Biophys. Res. Commun. 46, 288-295
38. Regenass, U., Caravatti, G., Mett, H., Stanek, J., Schneider, P., Müller, M., Matter, A., Vertino, P. and Porter, C.W. (1992) New S-adenosylmethionine decarboxylase inhibitors with potent antitumor activity. Cancer Res. 52, 4712-4718
39. Casara, P., Marchal, P., Wagner, J. and Danzin, C. (1989) 5'-{[(Z)-4-Amino-2-butenyl]methylamino}-5'-deoxyadenosine: a potent enzyme-activated irreversible inhibitor of S-adenosyl-L-methionine decarboxylase from Escherichia coli. J. Am. Chem. Soc. 111, 9111-9113
40. Shantz, L.M., Stanley, B.A., Secrist, J.A. and Pegg, A.E. (1992) Purification of human S-adenosylmethionine decarboxylase expressed in Escherichia coli and use of this protein to investigate the mechanism of inhibition by the irreversible inhibitors, 5'-deoxy-5'-[(3-hydrazino propyl)methylamino]adenosine and 5'{[(Z)-4-amino-2-butenyl]methylamino-5'- deoxyadenosine. Biochemistry 31, 6848-6855
41. Raney, A., Law, G.L., Mize, G.J. and Morris, D.R. (2002) Regulated translation termination at the upstream open reading frame in S-adenosylmethionine decarboxylase mRNA. J. Biol. Chem. 277, 5988-5994
42. Hanfrey, C., Elliott, K.A., Franceschetti, M., Mayer, M. J., Illingworth, C. and Michael, A.J. (2005) A dual upstream open reading frame-based autoregulatory circuit controlling polyamine-responsive translation. J. Biol. Chem. 280, 39229-39237
43. Morris, D.R. and Geballe, A.P. (2001) Upstream open reading frames as regulators of mRNA translation. Mol. Cell. Biol. 20, 8635-8642
44. Kahana, C. (2007) Ubiquitin dependent and independent protein degradation in the regulation of cellular polyamines. Amino Acids 33, 225-230
45. Yerlikaya, A. and Stanley, B.A. (2004) S-Adenosylmethionine decarboxylase degradation by the 26S proteasome is accelerated by substrate-mediated transamination. J. Biol. Chem. 279, 12469- 12478