Assessment of substrate inhibition of bacterial oligopeptidase B

Biological and Pharmaceutical Bulletin

Volumn 35, Issue 11, 2012, Pages 2010-2016

  Mustafa, Malik Suliman Mohamed ^a   Nakajima, Yoshitaka ^a,b   Oyama, Hiroshi ^b   Iwata, Nobuhisa ^a   Ito, Kiyoshi ^a  

^a NAGASAKI UNIVERSITY   (Japan)

^b SETSUNAN UNIVERSITY   (Japan)

Author keywords

Oligopeptidase B; Opportunistic bacteria; Prolyl oligopeptidase family; Substrate inhibition; Substrate specificity

Indexed keywords

ARGININE; BACTERIAL ENZYME; BACTERIAL OLIGOPEPTIDASE B; LYSINE; UNCLASSIFIED DRUG;

ARTICLE; CONCENTRATION RESPONSE; ENZYME ACTIVITY; ENZYME ANALYSIS; ENZYME INHIBITION; ENZYME MECHANISM; ENZYME PURIFICATION; ENZYME SPECIFICITY; ENZYME STRUCTURE; ESCHERICHIA COLI; MOLECULAR CLONING; NONHUMAN; NUCLEOTIDE SEQUENCE; PHYSICAL CHEMISTRY; PROTEIN EXPRESSION; RHODOCOCCUS ERYTHROPOLIS; SERRATIA MARCESCENS; STENOTROPHOMONAS MALTOPHILIA;

BACTERIA; BACTERIAL PROTEINS; COUMARINS; OLIGOPEPTIDES; SERINE ENDOPEPTIDASES; SERINE PROTEINASE INHIBITORS; SUBSTRATE SPECIFICITY;

EID: 84869212787     PISSN: 09186158     EISSN: 13475215     Source Type: Journal    
DOI: 10.1248/bpb.b12-00544     Document Type: Article

References (38)

1. Barrett AJ, Rawlings ND. Families and clans of serine peptidases. Arch. Biochem. Biophys., 318, 247-250 (1995).
2. Polgár L. Prolyl oligopeptidases. Methods Enzymol., 244, 188-200 (1994).
3. Fülöp V, Böcskei Z, Polgár L. Prolyl oligopeptidase: an unusual beta-propeller domain regulates proteolysis. Cell, 94, 161-170 (1998).
4. Kanatani A, Masuda T, Shimoda T, Misoka F, Lin XS, Yoshimoto T, Tsuru D. Protease II from Escherichia coli: sequencing and expression of the enzyme gene and characterization of the expressed enzyme. J. Biochem., 110, 315-320 (1991).
5. Polgár L. A potential processing enzyme in prokaryotes: oligopeptidase B, a new type of serine peptidase. Proteins, 28, 375-379 (1997).
6. Yoshimoto T, Tabira J, Kabashima T, Inoue S, Ito K. Protease II from Moraxella lacunata: cloning, sequencing, and expression of the enzyme gene, and crystallization of the expressed enzyme. J. Biochem., 117, 654-660 (1995).
7. Morty RE, Fülöp V, Andrews NW. Substrate recognition properties of oligopeptidase B from Salmonella enterica serovar Typhimurium. J. Bacteriol., 184, 3329-3337 (2002).
8. Juhász T, Szeltner Z, Renner V, Polgár L. Role of the oxyanion binding site and subsites S1 and S2 in the catalysis of oligopeptidase B, a novel target for antimicrobial chemotherapy. Biochemistry, 41, 4096-4106 (2002).
9. Pacaud M, Richaud C. Protease II from Escherichia coli. Purification and characterization. J. Biol. Chem., 250, 7771-7779 (1975).
10. 2+ signaling in mammalian cells. J. Cell Biol., 136, 609-620 (1997).
11. Caler EV, Vaena de Avalos S, Haynes PA, Andrews NW, Burleigh BA. Oligopeptidase B-dependent signaling mediates host cell invasion by Trypanosoma cruzi. EMBO J., 17, 4975-4986 (1998).
12. Morty RE, Troeberg L, Pike RN, Jones R, Nickel P, Lonsdale-Eccles JD, Coetzer TH. A trypanosome oligopeptidase as a target for the trypanocidal agents pentamidine, diminazene and suramin. FEBS Lett., 433, 251-256 (1998).
13. Morty RE, Troeberg L, Powers JC, Ono S, Lonsdale-Eccles JD, Coetzer TH. Characterisation of the antitrypanosomal activity of peptidyl α-aminoalkyl phosphonate diphenyl esters. Biochem. Pharmacol., 60, 1497-1504 (2000).
14. Morty RE, Lonsdale-Eccles JD, Mentele R, Auerswald EA, Coetzer THT. Trypanosome-derived oligopeptidase B is released into the plasma of infected rodents, where it persists and retains full catalytic activity. Infect. Immun., 69, 2757-2761 (2001).
15. Morty RE, Pellé R, Vadász I, Uzcanga GL, Seeger W, Bubis J. Oligopeptidase B from Trypanosoma evansi. A parasite peptidase that inactivates atrial natriuretic factor in the bloodstream of infected hosts. J. Biol. Chem., 280, 10925-10937 (2005).
16. Rea D, Hazell C, Andrews NW, Morty RE, Fülöp V. Expression, purification and preliminary crystallographic analysis of oligopeptidase B from Trypanosoma brucei. Acta Crystallograph. F, 62, 808-810 (2006).
17. Ivens AC, Peacock CS, Worthey EA, Murphy L, Aggarwal G, Berriman M, Sisk E, Rajandream MA, Adlem E, Aert R, Anupama A, Apostolou Z, Attipoe P, Bason N, Bauser C, Beck A, Beverley SM, Bianchettin G, Borzym K, Bothe G, Bruschi CV, Collins M, Cadag E, Ciarloni L, Clayton C, Coulson RM, Cronin A, Cruz AK, Davies RM, De Gaudenzi J, Dobson DE, Duesterhoeft A, Fazelina G, Fosker N, Frasch AC, Fraser A, Fuchs M, Gabel C, Goble A, Goffeau A, Harris D, Hertz-Fowler C, Hilbert H, Horn D, Huang Y, Klages S, Knights A, Kube M, Larke N, Litvin L, Lord A, Louie T, Marra M, Masuy D, Matthews K, Michaeli S, Mottram JC, Müller-Auer S, Munden H, Nelson S, Norbertczak H, Oliver K, O'neil S, Pentony M, Pohl TM, Price C, Purnelle B, Quail MA, Rabbinowitsch E, Reinhardt R, Rieger M, Rinta J, Robben J, Robertson L, Ruiz JC, Rutter S, Saunders D, Schäfer M, Schein J, Schwartz DC, Seeger K, Seyler A, Sharp S, Shin H, Sivam D, Squares R, Squares S, Tosato V, Vogt C, Volckaert G, Wambutt R, Warren T, Wedler H, Woodward J, Zhou S, Zimmermann W, Smith DF, Blackwell JM, Stuart KD, Barrell B, Myler PJ. The genome of the kinetoplastid parasite, Leishmania major. Science, 309, 436-442 (2005).
18. Peacock CS, Seeger K, Harris D, Murphy L, Ruiz JC, Quail MA, Peters N, Adlem E, Tivey A, Aslett M, Kerhornou A, Ivens A, Fraser A, Rajandream MA, Carver T, Norbertczak H, Chillingworth T, Hance Z, Jagels K, Moule S, Ormond D, Rutter S, Squares R, Whitehead S, Rabbinowitsch E, Arrowsmith C, White B, Thurston S, Bringaud F, Baldauf SL, Faulconbridge A, Jeffares D, Depledge DP, Oyola SO, Hilley JD, Brito LO, Tosi LR, Barrell B, Cruz AK, Mottram JC, Smith DF, Berriman M. Comparative genomic analysis of three Leishmania species that cause diverse human disease. Nat. Genet., 39, 839-847 (2007).
19. Almeida-Campos FR, Horta MF. Proteolytic activation of leishporin: evidence that Leishmania amazonensis and Leishmania guyanensis have distinct inactive forms. Mol. Biochem. Parasitol., 111, 363-375 (2000).
20. de Andrade AS, Santoro MM, de Melo MN, Mares-Guia M. Leishmania (Leishmania) amazonensis: purification and enzymatic characterization of a soluble serine oligopeptidase from promastigotes. Exp. Parasitol., 89, 153-160 (1998).
21. de Matos Guedes HL, Carneiro MP, Gomes DC, Rossi-Bergmanmn B, Giovanni de Simone S. Oligopeptidase B from L. amazonensis: molecular cloning, gene expression analysis and molecular model. Parasitol. Res., 101, 853-863 (2007).
22. McLuskey K, Paterson NG, Bland ND, Isaacs NW, Mottram JC. Crystal structure of Leishmania major oligopeptidase B gives insight into the enzymatic properties of a trypanosomatid virulence factor. J. Biol. Chem., 285, 39249-39259 (2010).
23. McKerrow JH, Rosenthal PJ, Swenerton R, Doyle P. Development of protease inhibitors for protozoan infections. Curr. Opin. Infect. Dis., 21, 668-672 (2008).
24. Mundaya JC, McLuskeya K, Browna E, Coombsb GH, Mottram JC. Oligopeptidase B deficient mutants of Leishmania major. Mol BiochParas, 175, 49-57 (2011).
25. Swenerton RK, Zhang S, Sajid M, Medzihradszky KF, Craik CS, Kelly BL, McKerrow JH. The oligopeptidase B of Leishmania regulates parasite enolase and immune evasion. J. Biol. Chem., 286, 429-440 (2011).
26. Matheson N, Schmidt J, Travis J. Isolation and properties of an angiotensin II-cleaving peptidase from mesquite pollen. Am. J. Respir. Cell Mol. Biol., 12, 441-448 (1995).
27. Bagarozzi DA Jr, Potempa J, Travis J. Purification and characterization of an arginine-specific peptidase from ragweed (Ambrosia artemisiifolia) pollen. Am. J. Respir. Cell Mol. Biol., 18, 363-369 (1998).
28. Guo ZJ, Lamb C, Dixon RA. A serine protease from suspension-cultured soybean cells. Phytochemistry, 47, 547-553 (1998).
29. Tsuji A, Yuasa K, Matsuda Y. Identification of oligopeptidase B in higher plants. Purification and characterization of oligopeptidase B from quiescent wheat embryo, Triticum aestivum. J. Biochem., 136, 673-681 (2004).
30. Jian-Bin Y, Guo-Qiang W, Pan D, De-Xu Z, Ming-Wei W, Xue-Yuan J. High-level expression and purification of Escherichia coli oligopeptidase B. Protein Expr. Purif., 47, 645-650 (2006).
31. Mäkinen KK, Mäkinen PL, Loesche WJ, Syed SA. Purification and general properties of an oligopeptidase from Treponema denticola ATCC 35405 - A human oral spirochete. Arch. Biochem. Biophys., 316, 689-698 (1995).
32. Fenno JC, Lee SY, Bayer CH, Ning Y. The opdB locus encodes the trypsin-like peptidase activity of Treponema denticola. Infect. Immun., 69, 6193-6200 (2001).
33. Lee SY, Fenno JC. Expression of Treponema denticola oligopeptidase B in Escherichia coli. Curr. Microbiol., 48, 379-382 (2004).
34. Mikhailova AG, Khairullin RF, Demidyuk IV, Gromova TY, Kostrov SV, Rumsh LD. Oligopeptidase B from Serratia proteamaculans. II. Enzymatic characteristics: substrate analysis, influence of calcium ions, pH and temperature dependences. Biochemistry (Mosc.), 76, 480-490 (2011).
35. Usuki H, Uesugi Y, Iwabuchi M, Hatanaka T. Activation of oligo-peptidase B from Streptomyces griseus by thiol-reacting reagents is independent of the single reactive cysteine residue. Biochim. Biophys. Acta, 1794, 1673-1683 (2009).
36. Strom MS, Lory S. Cloning and expression of the pilin gene of Pseudomonas aeruginosa PAK in Escherichia coli. J. Bacteriol., 165, 367-372 (1986).
37. Coetzer TH, Goldring JP, Huson LEJ. Oligopeptidase B: A processing peptidase involved in pathogenesis. Biochimie, 90, 336-344 (2008).
38. Tsuji A, Yoshimoto T, Yuasa K, Matsuda Y. Protamine: a unique and potent inhibitor of oligopeptidase B. J. Pept. Sci., 12, 65-71 (2006).