A glutathione-specific aldose reductase of Leishmania donovani and its potential implications for methylglyoxal detoxification pathway

Gene

Volumn 429, Issue 1-2, 2009, Pages 1-9

  Rath, Jyoti ^a   Gowri, V S ^b   Chauhan, Swati C ^a   Padmanabhan, Prasad K ^a   Srinivasan, N ^b   Madhubala, Rentala ^a  

^a JAWAHARLAL NEHRU UNIVERSITY   (India)

^b INDIAN INSTITUTE OF SCIENCE   (India)

Author keywords

Aldose reductase; Glyoxalase; Leishmania donovani; Methylglyoxal detoxification; Structural analysis

Indexed keywords

ALDEHYDE REDUCTASE; GLUTATHIONE; METHYLGLYOXAL;

AMINO ACID COMPOSITION; AMINO TERMINAL SEQUENCE; ARTICLE; CARBOXY TERMINAL SEQUENCE; CONTROLLED STUDY; DETOXIFICATION; DNA SEQUENCE; ESCHERICHIA COLI; ISOELECTRIC POINT; LEISHMANIA DONOVANI; NONHUMAN; NUCLEOTIDE SEQUENCE; OPEN READING FRAME; PRIORITY JOURNAL; PROTEIN EXPRESSION;

ALDEHYDE REDUCTASE; AMINO ACID SEQUENCE; ANIMALS; BIOCATALYSIS; BLOTTING, SOUTHERN; ESCHERICHIA COLI; GENOME, PROTOZOAN; GLUTATHIONE; HUMANS; KINETICS; LEISHMANIA DONOVANI; METABOLIC DETOXICATION, DRUG; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; PHYLOGENY; PYRUVALDEHYDE; SEQUENCE ALIGNMENT; SUBSTRATE SPECIFICITY;

ESCHERICHIA COLI; KINETOPLASTIDA; LEISHMANIA DONOVANI; MAMMALIA; PROTOZOA;

EID: 56949084159     PISSN: 03781119     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.gene.2008.09.037     Document Type: Article

References (39)

1. Ariza A., et al. Specificity of the trypanothione-dependent Leishmania major glyoxalase I: structure and biochemical comparison with the human enzyme. Mol. Microbiol. 59 (2006) 1239-1248
2. Berendsen H.J.C., Postma J.P.M., van Gunsteren W.F., and Hermans J. Interaction models for water in relation to protein hydration. Intermolecular Forces (1981), D. Reidel Publishing Company Dordrecht, Dordrecht 331-342
3. Berendsen H.J.C., van der Spoel D., and van Drunen R. GROMACS: a message-passing parallel molecular dynamics implementation. Comp. Phys. Comm. 91 (1995) 43-56
4. Bradford M.M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72 (1976) 248-254
5. Cagen L.M., and Pisano J.J. The glutathione conjugate of prostaglandin A1 is a better substrate than prostaglandin E for partially purified avian prostaglandin E 9-ketoreductase. Biochem. Biophys. Acta 573 (1979) 547-551
6. Dixit B.L., et al. Kinetic and structural characterization of the glutathione-binding site of aldose reductase. J. Biol. Chem. 275 (2000) 21587-21595
7. Doorn J.A., Srivastava S.K., and Petersen D.R. Aldose reductase catalyzes reduction of the lipid peroxidation product 4-oxonon-2-enal. Chem. Res. Toxicol. 16 (2003) 1418-1423
8. Ghoshal K., Banerjee A.B., and Ray S. Methylglyoxal-catabolizing enzymes of Leishmania donovani promastigotes. Mol. Biochem. Parasitol. 35 (1989) 21-29
9. Greig N., Wyllie S., Vickers T.J., and Fairlamb A.H. Trypanothione-dependent glyoxalase I in Trypanosoma cruzi. Biochem. J. 400 (2006) 217-223
10. Gomes R.A., Sousa S.M., Miranda H.V., Ferreira A.E.N., Cordeiro C.A.A., and Freire A.P. Protein glycation in Saccharomyces cerevisiae. Argpyrimidine formation and methylglyoxal catabolism. FEBS J. 272 (2005) 4521-4531
11. Inoue Y., and Kimmura A. Methylglyoxal and regulation of its metabolism in microorganisms. Adv. Microb. Physiol. 37 (1995) 177-227
12. Irsch T., and Krauth-Siegel R.L. Glyoxalase II of African trypanosomes is trypanothione-dependent. J. Biol. Chem. 279 (2004) 22209-22217
13. Jorgensen W.L., and Tirado-Rives J. The OPLS force field for proteins. Energy minimizations for crystals of cyclic peptides and crambin. J. Am. Chem. Soc. 110 (1988) 1657-1666
14. Kalapos M.P. Methylglyoxal in living organisms. Chemistry, biochemistry, toxicology and biological implications. Toxicol. lett. 110 (1999) 145-175
15. Kilunga K.B., et al. Structural and mutational analysis of Trypanosoma brucei prostaglandin H2 reductase provides insight into the catalytic mechanism of aldo-ketoreductases. J. Biol. Chem. 280 (2005) 26371-26382
16. Krauth-Siegel R.L., Bauer H., and Schirmer R.H. Dithiol proteins as guardians of the intracellular redox milieu in parasites: old and new drug targets in trypanosomes and malaria-causing plasmodia. Angew. Chem. Int. Ed. Engl. 44 (2005) 690-715
17. Kumar S., Tamura K., and Nei M. MEGA3: Integrated software for molecular evolutionary genetics analysis and sequence alignment. Brief. Bioinform. 5 (2004) 150-163
18. Lindahl E., Hess B., and van der Spoel D. GROMACS 3.0: a package for molecular simulation and trajectory analysis. J. Mol. Mod. 7 (2001) 306-317
19. Lo W.C.T., Westwood M.E., McLellan A.C., Selwood T., and Thornalley P.J. Binding and modification of proteins by methylglyoxal under physiological conditions: a kinetic and mechanistic study with N alpha-acetylarginine, N alpha-acetylcysteine, and N alpha-acetyllysine, and bovine serum albumin. J. Biol. Chem. 269 (1994) 32299-32305
20. Muller S., Liebau E., Walter R.D., and Krauth-Siegel R.L. Thiol-based redox metabolism of protozoan parasites. Trends Parasitol. 19 (2003) 320-328
21. Papoulis A., Al-Abed Y., and Bucala R. Identification of N2-(1-carboxyethyl) guanine (CEG) as a guanine advanced glycosylation end product. Biochemistry 34 (1995) 648-655
22. Poirot O., Suhre K., Abergel C., O'Toole E., and Notredame C. 3DCoffee@igs: a web server for combining sequences and structures into a multiple sequence alignment. Nucleic Acids Res. 32 Web Server issue (2004) W37-W40
23. Ponces Freire A., Ferreira A., Gomes R., and Cordeiro C. Anti-glycation defences in yeast. Biochem. Soc. Trans. 31 (2003) 1409-1412
24. Padmanabhan P.K., et al. Glyoxalase I from Leishmania donovani: a potential target for anti-parasite drug. Biochem. Biophys. Res. Commun. 337 4 (2005) 1237-1248
25. Pulvertaft R.J., and Hoyle G.F. Stages in the life-cycle of Leishmania donovani. Trans. R. Soc. Trop. Med. Hyg. 54 (1960) 191-196
26. Ramana K.V., Dixit B.L., Srivastava S., Balendiran G.K., Srivastava S.K., and Bhatnagar A. Selective recognition of glutathiolated aldehydes by aldose reductase. Biochemistry 39 (2000) 12172-12180
27. Sali A., and Blundell T.L. Comparative protein modelling by satisfaction of spatial restraints. J. Mol. Biol. 234 3 (1993 Dec 5) 779-815
28. Singh R., et al. Structure of a glutathione conjugate bound to the active site of aldose reductase. Proteins 64 (2006) 101-110
29. Srinivasan N., and Blundell T.L. An evaluation of the performance of an automated procedure for comparative modeling of protein tertiary structure. Protein Eng. Design Selection 6 (1993) 501-512
30. Thornalley P.J. The glyoxalase system: new developments towards functional characterization of a metabolic pathway fundamental to biological life. Biochem. J. 269 (1990) 1-11
31. Thornalley P.J. Pharmacology of methylglyoxal: formation, modification of proteins and nucleic acids, and enzymatic detoxification-a role in pathogenesis and antiproliferative chemotherapy. Gen. Pharmacol. 27 (1996) 565-573
32. Thornalley P.J., Langborg A., and Minhas H.S. Formation of glyoxal, methylglyoxal and 3-deoxyglucosone in the glycation of proteins by glucose. Biochem. J. 344 (1999) 109-116
33. 32P-postlabelling method for the analysis of 2′-deoxyguanosine-3′-monophosphate and DNA adducts of methylglyoxal. Carcinogenesis 15 (1994) 1887-1894
34. Vander Jagt, D.L., Hunsaker, L.A., 2003. Methylglyoxal metabolism and diabetic complications: roles of aldose reductase, glyoxalase-I, betaine aldehyde dehydrogenase and 2-oxoaldehyde dehydrogenase. Chem. Biol. Interact. 143-144, 341-351.
35. Vander Jagt, D.L., Hassebrook, R.K., Hunsaker, L.A., Brown, W.M., Royer, R.E., 2001. Metabolism of the 2-oxoaldehyde methylglyoxal by aldose reductase and by glyoxalase-I: roles for glutathione in both enzymes and implications for diabetic complications. Chem. Biol. Interact. 130-132, 549-562.
36. Vickers T.J., Greig N., and Fairlamb A.H. A trypanothione-dependent glyoxalase I with a prokaryotic ancestry in Leishmania major. Proc. Natl. Acad. Sci. U. S. A. 101 (2004) 13186-13191
37. Weiner S.J., et al. A new force field for molecular mechanical simulation of nucleic acids and proteins. J. Amer. Chem. Soc. 106 (1984) 765-784
38. Yadav S.K., Singla-Pareek S.L., Reddy M.K., and Sopory S.K. Transgenic tobacco plants overexpressing glyoxalase enzymes resist an increase in methylglyoxal and maintain higher reduced glutathione levels under salinity stress. FEBS Lett. 579 (2005) 6265-6271
39. Yadav S.K., Singla-Pareek S.L., Ray M., Reddy M.K., and Sopory S.K. Methylglyoxal levels in plants under salinity stress are dependent on glyoxalase I and glutathione. Biochem. Biophys. Res. Commun. 337 (2005) 61-67