Characterization of the peptide substrate specificity of glutathionylspermidine synthetase from Crithidia fasciculata

Molecular and Biochemical Parasitology

Volumn 84, Issue 1, 1997, Pages 25-32

  De Craecker, Sofie ^a   Verbruggen, Christophe ^a   Rajan, Padinchare K ^a   Smith, Keith ^b   Haemers, Achiel ^a   Fairlamb, Alan H ^b  

^a UNIVERSITY OF ANTWERP   (Belgium)

^b LONDON SCHOOL OF HYGIENE AND TROPICAL MEDICINE   (United Kingdom)

Author keywords

Crithidia fasciculata; glutathione binding site; glutathionylspermidine synthetase; kinetic analysis; substrate specificity; trypanothione

Indexed keywords

GLUTATHIONE DERIVATIVE; SPERMINE SYNTHASE; TRYPANOTHIONE;

ALKYLATION; ARTICLE; BINDING SITE; CHEMICAL MODIFICATION; CRITHIDIA FASCICULATA; ENZYME ACTIVITY; ENZYME KINETICS; ENZYME SPECIFICITY; NONHUMAN; PRIORITY JOURNAL;

AMIDE SYNTHASES; ANIMALS; CRITHIDIA FASCICULATA; GLUTATHIONE; LIGASES; PROTOZOAN PROTEINS; SPERMIDINE; SUBSTRATE SPECIFICITY;

EID: 0031054199     PISSN: 01666851     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0166-6851(96)02778-8     Document Type: Article

References (22)

1. Fairlamb, A.H., Blackburn, P., Ulrich, P., Chait, B.T. and Cerami, A. (1985) Trypanothione: a novel bis(glutathionyl)spermidine cofactor for glutathione reductase in trypanosomatids. Science 227, 1485-1487.
2. Fairlamb, A.H. and Cerami, A. (1992) Metabolism and functions of trypanothione in the Kinetoplastida. Annu. Rev. Microbiol. 46, 695-729.
3. Fairlamb, A.H., Henderson, G.B. and Cerami, A. (1986) The biosynthesis of trypanothione and N-glutathionylspermidine in Crithidia fasciculata. Mol. Biochem. Parasitol. 21, 247-257.
4. Henderson, G.B., Yamaguchi, M., Novoa, L., Fairlamb, A.H. and Cerami, A. (1990) Biosynthesis of the trypanosomatid metabolite trypanothione: purification and characterization of trypanothione synthetase from Crithidia fasciculata. Biochemistry 29, 3924-3929.
5. Smith, K., Nadeau, K., Walsh, C.T. and Fairlamb, A.H. (1992) Purification of glutathionylspermidine and trypanothione synthetases from Crithidia fasciculata. Protein Sci. 1, 874-883.
6. 9-bis(glutathionyl)aminopropylcadaverine (homotrypanothione) in Trypanosoma cruzi. Eur. J. Biochem. 226, 1019-1027.
7. Docampo, R. (1995) Antioxidant mechanisms. In: Biochemistry and Molecular Biology of Parasites (Marr, J.J. and Müller M., eds.), pp. 147-160. Academic Press. London.
8. Fairlamb, A.H., Henderson, G.B., Bacchi, C.J. and Cerami, A. (1987) In vivo effects of difluoromethylornithine on trypanothione and polyamine levels in bloodstream forms of Trypanosoma brucei. Mol. Biochem. Parasitol. 24, 185-191.
9. Bellofatto, V., Fairlamb, A.H., Henderson, G.B. and Cross, G.A.M. (1987) Biochemical changes associated with α-difluoromethylornithine uptake and resistance in Trypanosoma brucei. Mol. Biochem. Parasitol. 25, 227-238.
10. Cunningham, M.L. and Fairlamb, A.H. (1995) Trypanothione reductase from Leishmania donovani - Purification, characterisation and inhibition by trivalent antimonials. Eur. J. Biochem. 230, 460-468.
11. Fairlamb, A.H., Henderson, G.B. and Cerami, A. (1989) Trypanothione is the primary target for arsenical drugs against African trypanosomes. Proc. Natl. Acad. Sci. USA 86, 2607-2611.
12. Cunningham, M.L., Zvelebil, M.J.J.M. and Fairlamb, A.H. (1994) Mechanism of inhibition of trypanothione reductase and glutathione reductase by trivalent organic arsenicals. Fur. J. Biochem. 221, 285-295.
13. Kierszenbaum, F., Wirth, J.J., McCann, P.P. and Sjoerdsma, A. (1987) Arginine decarboxylase inhibitors reduce the capacity of Trypanosoma cruzi to infect and multiply in mammalian host cells. Proc. Natl. Acad. Sci. USA 84, 4278-4282.
14. Smith, K., Borges, A., Ariyanayagam, M.R. and Fairlamb, A.H. (1995) Glutathionylspermidine metabolism in Escherichia coli. Biochem. J. 312, 465-469.
15. Tabor, H. and Tabor, C.W. (1975) Isolation, characterization, and turnover of glutathionylspermidine from Escherichia coli. J. Biol. Chem. 250, 2648-2654.
16. Tabor, H. and Tabor, C.W. (1971) Glutathionylspermidine synthetase (Escherichia coli). Methods Enzymol. 17B, 815-817.
17. Bollinger, J.M. Jr., Kwon, D.S., Huisman, G.W., Kolter, R. and Walsh, C.T. (1995) Glutathionylspermidine metabolism in Escherichia coli. Purification, cloning, over-production, and characterization of a bifunctional glutathionylspermidine synthetase/amidase. J. Biol. Chem. 270, 14031-14041.
18. Böhlen, P., Stein, S., Dairman, W. and Udenfriend, S. (1973) Fluorometric assay of proteins in the nanogram range. Arch. Biochem. Biophys. 155, 213-220.
19. Dixon, M. (1953) The determination of enzyme inhibitor constants. Biochem. J. 55, 170-171.
20. Cornish-Bowden, A. (1974) A simple graphical method for determining the inhibition constants of mixed, uncompetitive and non-competitive inhibitors. Biochem. J. 137, 143-144.
21. El-Waer, A.F., Smith, K., McKie, J.H., Benson, T., Fairlamb, A.H. and Douglas, K.T. (1993) The glutamyl binding site of trypanothione reductase from Crithidia fasciculata: enzymatic properties of gamma-glutamyl-modified substrates analogues. Biochim. Biophys. Acta 1203, 93-98.
22. Verbruggen, C., De Craecker, S., Rajan, P., Jiao, X.-Y., Borloo, M., Smith, K., Fairlamb, A.H. and Haemers, A. (1996) Phosphonic and phosphinic acid tripeptides as inhibitors of glutathionylspermidine synthetase. Bioorg. Med. Chem. Lett. 6, 253-258.