Characterization of human paraoxonase 1 variants suggest that His residues at 115 and 134 positions are not always needed for the lactonase/arylesterase activities of the enzyme

Protein Science

Volumn 22, Issue 12, 2013, Pages 1799-1807

  Bajaj, Priyanka ^a   Tripathy, Rajan K ^a   Aggarwal, Geetika ^a   Pande, Abhay H ^a  

^a NATIONAL INSTITUTE OF PHARMACEUTICAL EDUCATION AND RESEARCH NIPER   (India)

Author keywords

Acyl homoserine lactone; Organophosphate; Recombinant human PON1; Site directed mutagenesis

Indexed keywords

ACETYLCHOLINESTERASE; AMINO ACID; ARYLDIALKYLPHOSPHATASE 1; ARYLESTERASE; EDETIC ACID; GLUCONOLACTONASE; HISTIDINE; MESSENGER RNA; N ACYLHOMOSERINE LACTONE; ORGANOPHOSPHATE; PARAOXON; PHOSPHOTRIESTERASE; RECOMBINANT PROTEIN;

AMINO ACID SUBSTITUTION; ARTICLE; CATALYSIS; CHOLINESTERASE INHIBITION; DNA SEQUENCE; ENZYME ACTIVITY; ENZYME ANALYSIS; ENZYME ASSAY; ENZYME PURIFICATION; ENZYME SUBSTRATE; ESCHERICHIA COLI; HUMAN; HYDROLYSIS; NONHUMAN; NUCLEOTIDE SEQUENCE; ORGANOPHOSPHATE POISONING; PRIORITY JOURNAL; SITE DIRECTED MUTAGENESIS; WESTERN BLOTTING;

ACYL HOMOSERINE LACTONE; ORGANOPHOSPHATE; RECOMBINANT HUMAN PON1; SITE DIRECTED MUTAGENESIS;

AMINO ACID SUBSTITUTION; ARYLDIALKYLPHOSPHATASE; CARBOXYLIC ESTER HYDROLASES; CATALYTIC DOMAIN; GENETIC VARIATION; HISTIDINE; HUMANS; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MUTAGENESIS, SITE-DIRECTED; ORGANOPHOSPHATES; PHOSPHORIC TRIESTER HYDROLASES; RECOMBINANT PROTEINS;

EID: 84892904852     PISSN: 09618368     EISSN: 1469896X     Source Type: Journal    
DOI: 10.1002/pro.2380     Document Type: Article

References (40)

1. La Du BN, Aviram M, Billecke S, Navab M, Primo- Parmo S, Sorenson RC, Standiford TJ (1999) On the physiological role(s) of the paraoxonases. Chem Biol Interact 119-120:379-388.
2. La Du BN, Eckerson HW (1984) The polymorphic paraoxonase/arylesterase isozymes of human serum. Fed Proc 43:2338-2341.
3. Eckerson HW, Wyte CM, La Du BN (1983) The human serum paraoxonase/arylesterase polymorphism. Am J Hum Genet 35:1126-1138.
4. Furlong CE, Richter RJ, Li WF, Brophy VH., Carlson C, Rieder M, Nickerson D, Costa LG, Ranchalis J, Lusis AJ (2008) The functional consequences of polymorphisms in the human PON1 gene. The Paraoxonases: Their role in disease development and xenobiotic metabolism. The Netherlands: Springer.
5. Costa LG, Cole TB, Jarvik GP, Furlong CE (2003) Functional genomics of the paraoxonase (PON1) polymorphisms: Effects on pesticide sensitivity, cardiovascular disease, and drug metabolism. Annu Rev Med 54: 371-392.
6. Draganov DI, La Du BN (2004) Pharmacogenetics of paraoxonases: A brief review. Naunyn-Schmiedeberg Arch Pharmacol 369:78-88.
7. Draganov DI, Teiber JF, Speelman A, Osawa Y, Sunahara R, La Du BN (2005) Human paraoxonases (PON1, PON2, and PON3) are lactonases with overlapping and distinct substrate specificities. J Lipid Res 46: 1239-1248.
8. Khersonsky O, Tawfik DS (2005) Structure-reactivity studies of serum paraoxonase PON1 suggest that its native activity is lactonase. Biochemistry 44:6371- 6382.
9. Shih DM, Gu L, Xia YR, Navab M, Li WF, Hama S, Castellani LW, Furlong CE, Costa LG, Fogelman AM (1998) Mice lacking serum paraoxonase are susceptible to organophosphate toxicity and atherosclerosis. Nature 394:284-287.
10. Costa LG, McDonald BE, Murphy SD, Omenn GS, Richter RJ, Motulsky AG, Furlong CE (1990) Serum paraoxonase and its influence on paraoxon and chlorpyrifos-oxon toxicity in rats. Toxicol Appl Pharmacol 103:66-76.
11. Li WF, Furlong CE, Costa LG (1995) Paraoxonase protects against chlorpyrifos toxicity in mice. Toxicol Lett 76:219-226.
12. Ritcher RJ, Jarvik GP, Furlong CE (2010) Paraoxonase 1 status as a risk factor for disease or exposure. Adv Exp Med Biol 660:29-35.
13. Cole TB, Jansen K, Park S, Li WF, Furlong CE, Costa LG (2010) The toxicity of mixtures of specific organophosphate compounds is modulated by paraoxonase 1 status. Adv Exp Med Biol 660:47-60.
14. Lenz DE, Yeung D, Smith JR, Sweeney RE, Lumley LA, Cerasoli DM (2007) Stoichiometric and catalytic scavengers as protection against nerve agent toxicity: A mini review. Toxicology 233:31-39.
15. Rochu D, Chabriere E, Masson P (2007) Human paraoxonase: A promising approach for pre-treatment and therapy of organophosphorus poisoning. Toxicology 233:47-59.
16. Gupta RD, Goldsmith M, Ashani Y, Simo Y, Mullokandov G, Bar H, Ben-David M, Leader H, Margalit R, Silman I (2011) Directed evolution of hydrolases for prevention of G-type nerve agent intoxication. Nat Chem Biol 7:120-125.
17. Aharoni A, Gaidukov L, Yagur S, Toker L, Silman I, Tawfik DS (2004) Directed evolution of mammalian paraoxonases PON1 and PON3 for bacterial expression and catalytic specialization. Proc Natl Acad Sci USA 101:482-487.
18. Otto TC, Harsch CK, Yeung DT, Magliery TJ, Cerasoli DM, Lenz DE (2009) Dramatic differences in organophosphorus hydrolase activity between human and chimeric recombinant mammalian paraoxonase-1 enzymes. Biochemistry 48:10416-10422.
19. Rochu D, Renault F, Cl-ery-Barraud C, Chabrière E, Masson P (2007) Stability of highly purified human paraoxonase (PON1): Association with human phosphate binding protein (HPBP) is essential for preserving its active conformation(s). Biochim Biophys Acta 1774:874-883.
20. Amitai G, Gaidukov L, Adani R, Yishay S, Yacov G, Kushnir M, Teitlboim S, Lindenbaum M, Bel P, Khersonsky O (2006) Enhanced stereoselective hydrolysis of toxic organophosphates by directly evolved variants of mammalian serum paraoxonase. FEBS J 273: 1906-1919.
21. Ellman GL, Courtney KD (1961) A new and rapid colorimetric determination of acetylcholinesterase activity. Biochem Pharmacol 7:91-96.
22. Billecke S, Draganov D, Counsell R, Stetson P, Watson C, Hsu C, La Du BN (2000) Human serum paraoxonase (PON1) isozymes Q and R hydrolyze lactones and cyclic carbonate esters. Drug Metab Dispos 28:1335- 1342.
23. Graslund S, Nordlund P, Weigelt J, Hallberg BM, Bray J, Gileadi O, Knapp S, Oppermann U, Arrowsmith C, Hui R, Ming J, dhe-Paganon S, Park HW, Savchenko A, Yee A, Edwards A, Vincentelli R, Cambillau C, Kim R, Kim SH, Rao Z, Shi Y, Terwilliger TC, Kim CY, Hung LW, Waldo GS, Peleg Y, Albeck S, Unger T, Dym O, Prilusky J, Sussman JL, Stevens RC, Lesley SA, Wilson IA, Joachimiak A, Collart F, Dementieva I, Donnelly MI, Eschenfeldt WH, Kim Y, Stols L, Wu R, Zhou M, Burley SK, Emtage JS, Sauder JM, Thompson D, Bain K, Luz J, Gheyi T, Zhang F, Atwell S, Almo SC, Bonanno JB, Fiser A, Swaminathan S, Studier FW, Chance MR, Sali A, Acton TB, Xiao R, Zhao L, Ma LC, Hunt JF, Tong L, Cunningham K, Inouye M, Anderson S, Janjua H, Shastry R, Ho CK, Wang D, Wang H, Jiang M, Montelione GT, Stuart DI, Owens RJ, Daenke S, Schutz A, Heinemann U, Yokoyama S, Bussow K, Gunsalus KC (2008) Protein production and purification. Nat Methods 5:135-146.
24. Mirzahoseini H, Mafakheri N, Mohammadi S, Enayati N, Mortazavidehkordi N (2010) Heterologous proteins production in Escherichia coli: An investigation on the effect of codon usage and expression host optimization. Cell J 12:453-458.
25. Maertens B, Spriestersbach A, von Groll U, Roth U, Kubicek J, Gerrits M, Graf M, Liss M, Daubert D, Wagner R, Schafer F (2010) Gene optimization mechanisms: A multi-gene study reveals a high success rate of full length human proteins expressed in Escherchia coli. Protein Sci 19:1312-1326.
26. Camps J, Pujol I, Ballester F, Joven J, Simo JM (2011) Paraoxonases as potential antibiofilm agents: Their relationship with quorum-sensing signals in gramnegative bacteria. AAntimicrob Agents Chemotherntimicrob Agents Chemother 55:1325-1331.
27. Gan KN, Smolen A, Eckerson HW, La Du BN (1991) Purification of human serum paraoxonase/arylesterase. Evidence for one esterase catalyzing both activities. Drug Metab Dispos 19:100-106.
28. Jakubowski H (2000) Calcium-dependent human serum homocysteinethiolactone hydrolase: A protective mechanism against protein N-homocysteinylation. J Biol Chem 275:3957-3962.
29. La Du, BN, Adkins S, Kuo CL, Lipsig D (1993) Studies on human serum paraoxonase/arylesterase. Chem Biol Interact 87:25-34.
30. Costa LG, McDonald BE, Murphy SD, Omenn GS, Richter RJ, Motulsky AG, Furlong, CE (1990) Serum paraoxonase and its influence on paraoxon and chlorpyrifos-oxon toxicity in rats Toxicol Appl Pharmacol 103:66-76.
31. Otto TC, Kasten SA, Kovaleva E, Liu Z, Buchman G, Tolosa M, Davis D, Smith JR, Balcerzak R, Lenz DE (2010) Purification and characterization of functional human paraoxonase-1 expressed in Trichoplusiani larvae. Chem Biol Interact 187:388-392.
32. Sarka M, Harsch CK, Matic GT, Hoffman K, Norris JR, Otto TC, Lenz DE, Cerasoli DM, Magliery TJ (2012) Solubilization and humanization of paraoxonase-J Lipids 2012:610937.
33. Blum MM, Chen JC (2010) Structural characterization of the catalytic calcium binding site in diisopropylfluorophosphatase (DFPase) and comparison with related b-propeller enzymes. Chem Biol Interact 187: 373-379.
34. Sanan TT, Muthukrishnan S, Beck JM, Tao P, Hayes CJ, Otto TC, Douglas MC, David EL, Christopher MH (2010) Computational modeling of human paraoxonase 1: Preparation of protein models, binding studies, and mechanistic insight. J Phys Org Chem 23:357-369.
35. Hu X, Jiang X, Lenz DE, Cerasoli DE, Wallqvist A (2009) Insilico analyses of substrate interactions with human serum paraoxonase. Proteins 75:486-498.
36. Yeung DT, Lenz DE, Cerasoli DM (2005) Analysis of active-site amino-acid residues of human serum paraoxonase using competitive substrates. FEBS J 272: 2225-2230.
37. Khersonsky O, Tawfik DS (2006) The histidine 115- histidine 134 dyad mediates the lactonase activity of mammalian serum paraoxonases. J Biol Chem 281: 7649-7656.
38. Ben-David M, Elias M, Filippi JJ, Dunach E, Silman I, Sussman JL, Tawfik DS (2012) Catalytic versatility and backups in enzyme active sites: The case of serum paraoxonase J Mol Biol 418:181-196.
39. Ben-David M, Wieczorek G, Elias M, Silman I, Sussman JL, Tawfik DS (2013) Catalytic metal ion rearrangements underline promiscuity and evolvability of a metalloenzyme. J Mol Biol 425:1028-1038.
40. Stevens RC, Suzuki SM, Cole TB, Park SS, Richter RJ, Furlong CE (2008) Engineered recombinant human paraoxonase 1 (rHuPON1) purified from Escherichia coli protects against organophosphate poisoning. Proc Natl Acad Sci USA 105:12780-12784.