Leucyl Aminopeptidase PepA

Handbook of Proteolytic Enzymes

Volumn 2, Issue , 2013, Pages 1484-1492

  Colloms, Sean D ^a  

^a UNIVERSITY OF GLASGOW   (United Kingdom)

Author keywords

[No Author keywords available]

Indexed keywords

EID: 84884878311     PISSN: None     EISSN: None     Source Type: Book    
DOI: 10.1016/B978-0-12-382219-2.00334-3     Document Type: Chapter

References (52)

1. Vogt V.M. Purification and properties of an aminopeptidase from Escherichia coli. J. Biol. Chem. 1970, 245:4760-4769.
2. Dick A.J., Matheson A.T., Wang J.H. A ribosomal-bound aminopeptidase in Escherichia coli B, purification and properties. Can. J. Biochem. 1970, 48:1181-1188.
3. Tsai C.S., Matheson A.T. Purification and properties of a ribosomal peptidase from Escherichia coli B. Can. J. Biochem. 1965, 43:1643-1652.
4. Miller C.G., Mackinnon K. Peptidase mutants of Salmonella typhimurium. J. Bacteriol. 1974, 120:355-363.
5. Miller C.G. Genetic mapping of Salmonella typhimurium peptidase mutations. J. Bacteriol. 1975, 122:171-176.
6. Miller C.G., Schwartz G. Peptidase-deficient mutants of Escherichia coli. J. Bacteriol. 1978, 135:603-611.
7. Stirling C.J., Colloms S.D., Collins J.F., Szatmari G., Sherratt D.J. xerB, an Escherichia coli gene required for plasmid ColE1 site-specific recombination, is identical to pepA, encoding aminopeptidase A, a protein with substantial similarity to bovine lens leucine aminopeptidase. EMBO J. 1989, 8:1623-1627.
8. Charlier D., Hassanzadeh G., Kholti A., Gigot D., Piérard A., Glansdorff N. carP, involved in pyrimidine regulation of the Escherichia coli carbamoylphosphate synthetase operon encodes a sequence-specific DNA-binding protein identical to XerB and PepA, also required for resolution of ColE1 multimers. J. Mol. Biol. 1995, 250:392-406.
9. Wood D.O., Solomon M.J., Speed R.R. Characterization of the Rickettsia prowazekii pepA gene encoding leucine aminopeptidase. J. Bacteriol. 1993, 175:159-165.
10. Woolwine S.C., Wozniak D.J. Identification of an Escherichia coli pepA homolog and its involvement in suppression of the algB phenotype in mucoid Pseudomonas aeruginosa. J. Bacteriol. 1999, 181:107-116.
11. Behari J., Stagon L., Calderwood S.B. pepA, a gene mediating pH regulation of virulence genes in Vibrio cholerae. J. Bacteriol. 2001, 183:178-188.
12. Hermes H.F., Sonke T., Peters P.J., van Balken J.A., Kamphuis J., Dijkhuizen L., Meijer E.M. Purification and characterization of an L-aminopeptidase from Pseudomonas putida ATCC 12633. Appl. Environ. Microbiol. 1993, 59:4330-4334.
13. Komeda H., Hariyama N., Asano Y. L-Stereoselective amino acid amidase with broad substrate specificity from Brevundimonas diminuta, characterization of a new member of the leucine aminopeptidase family. Appl. Microbiol. Biotechnol. 2006, 70:412-421.
14. Matheson A.T., Dick A.J., Rollin F. A ribosomal-bound aminopeptidase in Escherichia coli B, substrate specificity. Can. J. Biochem. 1970, 48:1292-1296.
15. Gu Y.Q., Holzer F.M., Walling L.L. Overexpression, purification and biochemical characterization of the wound-induced leucine aminopeptidase of tomato. Eur. J. Biochem. 1999, 263:726-735.
16. Gu Y.Q., Walling L.L. Specificity of the wound-induced leucine aminopeptidase (LAP-A) of tomato activity on dipeptide and tripeptide substrates. Eur. J. Biochem. 2000, 267:1178-1187.
17. Miller C.G., Green L. Degradation of proline peptides in peptidase-deficient strains of Salmonella typhimurium. J. Bacteriol. 1983, 153:350-356.
18. Kale A., Pijning T., Sonke T., Dijkstra B.W., Thunnissen A.M. Crystal structure of the leucine aminopeptidase from Pseudomonas putida reveals the molecular basis for its enantioselectivity and broad substrate specificity. J. Mol. Biol. 2010, 398:703-714.
19. Woolwine S.C., Sprinkle A.B., Wozniak D.J. Loss of Pseudomonas aeruginosa PhpA aminopeptidase activity results in increased algD transcription. J. Bacteriol. 2001, 183:4674-4679.
20. Little A.J., Sutherland J.D., Wilson E.J., Wood-Collins D.A.J. Directed evolution of novel biosynthetic pathways, Overexpression of leucine aminopeptidase allows an Escherichia coli proline auxotroph to grow faster on prolinamide. Bioorg. Medicinal Chem. Lett. 1994, 4:2555-2558.
21. Bhosale M., Pande S., Kumar A., Kairamkonda S., Nandi D. Characterization of two M17 family members in Escherichia coli, Peptidase A and Peptidase B. Biochem. Biophys. Res. Commun. 2010, 395:76-81.
22. Alén C., Sherratt D.J., Colloms S.D. Direct interaction of aminopeptidase A with recombination site DNA in Xer site-specific recombination. EMBO J. 1997, 16:5188-5197.
23. Colloms S.D., McCulloch R., Grant K., Neilson L., Sherratt D.J. Xer-mediated site-specific recombination in vitro. EMBO J. 1996, 15:1172-1181.
24. Burley S.K., David P.R., Sweet R.M., Taylor A., Lipscomb W.N. Structure determination and refinement of bovine lens leucine aminopeptidase and its complex with bestatin. J. Mol. Biol. 1992, 224:113-140.
25. McCulloch R., Burke M.E., Sherratt D.J. Peptidase activity of Escherichia coli aminopeptidase A is not required for its role in Xer site-specific recombination. Mol. Microbiol. 1994, 12:241-251.
26. Sträter N., Sherratt D.J., Colloms S.D. X-ray structure of aminopeptidase A from Escherichia coli and a model for the nucleoprotein complex in Xer site-specific recombination. EMBO J. 1999, 18:4513-4522.
27. Sträter N., Sun L., Kantrowitz E.R., Lipscomb W.N. A bicarbonate ion as a general base in the mechanism of peptide hydrolysis by dizinc leucine aminopeptidase. Proc. Natl. Acad. Sci. USA 1999, 96:11151-11155.
28. Charlier D., Kholti A., Huysveld N., Gigot D., Maes D., Thia-Toong T.L., Glansdorff N. Mutational analysis of Escherichia coli PepA, a multifunctional DNA-binding aminopeptidase. J. Mol. Biol. 2000, 302:411-426.
29. Reijns M., Lu Y., Leach S., Colloms S.D. Mutagenesis of PepA suggests a new model for the Xer/cer synaptic complex. Mol. Microbiol. 2005, 57:927-941.
30. Hodgman T.C., Griffiths H., Summers D.K. Nucleoprotein architecture and ColE1 dimer resolution, a hypothesis. Mol. Microbiol. 1998, 29:545-558.
31. Lutfullah G., Azhar N., Amin F., Khan Z., Azim M.K., Shouqat K., Noor S., Ali R. Structural bioinformatics of Vibrio cholerae aminopeptidase A (PepA) monomer. Protein Pept. Lett. 2009, 16:36-45.
32. Huynh K.H., Natarajan S., Choi J., Song N.H., Kim J.G., Lee B.M., Ahn Y.J., Kang L.W. Cloning, expression, crystallization and preliminary X-ray crystallographic analysis of leucine aminopeptidase (LAP) from the pepA gene of Xanthomonas oryzae pv. Oryzae. Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. 2009, 65:952-955.
33. Suzuki H., Kamatani S., Kim E.S., Kumagai H. Aminopeptidases A, B, and N and dipeptidase D are the four cysteinylglycinases of Escherichia coli K-12. J. Bacteriol. 2001, 183:1489-1490.
34. Yen C., Green L., Miller C.G. Degradation of intracellular protein in Salmonella typhimurium peptidase mutants. J. Mol. Biol. 1980, 143:21-33.
35. Miller C.G., Green L. Degradation of abnormal proteins in peptidase-deficient mutants of Salmonella typhimurium. J. Bacteriol. 1981, 147:925-930.
36. Braun V., Günthner K., Hantke K., Zimmermann L. Intracellular activation of albomycin in Escherichia coli and Salmonella typhimurium. J. Bacteriol. 1983, 156:308-315.
37. Gibson M.M., Price M., Higgins C.F. Genetic characterization and molecular cloning of the tripeptide permease (tpp) genes of Salmonella typhimurium. J. Bacteriol. 1984, 160:122-130.
38. Kazakov T., Vondenhoff G.H., Datsenko K.A., Novikova M., Metlitskaya A., Wanner B.L., Severinov K. Escherichia coli peptidase A, B, or N can process translation inhibitor microcin C. J. Bacteriol. 2008, 190:2607-2610.
39. Circello B.T., Miller C.G., Lee J.H., van der Donk W.A., Metcalf W.W. The antibiotic dehydrophos is converted to a toxic pyruvate analog by peptide bond cleavage in Salmonella enterica. Antimicrob. Agents Chemother. 2011, 55:3357-3362.
40. Minh P.N., Devroede N., Massant J., Maes D., Charlier D. Insights into the architecture and stoichiometry of Escherichia coli PepA-DNA complexes involved in transcriptional control and site-specific DNA recombination by atomic force microscopy. Nucleic Acids Res. 2009, 37:1463-1476.
41. Charlier D., Gigot D., Huysveld N., Roovers M., Piérard A., Glansdorff N. Pyrimidine regulation of the Escherichia coli and Salmonella typhimurium carAB operons, CarP and integration host factor (IHF) modulate the methylation status of a GATC site present in the control region. J. Mol. Biol. 1995, 250:383-391.
42. Kholti A., Charlier D., Gigot D., Huysveld N., Roovers M., Glansdorff N. pyrH-encoded UMP-kinase directly participates in pyrimidine-specific modulation of promoter activity in Escherichia coli. J. Mol. Biol. 1998, 280:571-582.
43. Watt S.A., Wilke A., Patschkowski T., Niehaus K. Comprehensive analysis of the extracellular proteins from Xanthomonas campestris pv. campestris B100. Proteomics 2005, 5:153-167.
44. Chung W.J., Shu H.Y., Lu C.Y., Wu C.Y., Tseng Y.H., Tsai S.F., Lin C.H. Qualitative and comparative proteomic analysis of Xanthomonas campestris pv. campestris 17. Proteomics 2007, 7:2047-2058.
45. Mathew Z., Knox T.M., Miller C.G. Salmonella enterica serovar Typhimurium peptidase B is a leucyl aminopeptidase with specificity for acidic amino acids. J. Bacteriol. 2000, 182:3383-3393.
46. Shibata K., Tsuchida N., Watanabe T. Cloning and sequence analysis of the aminopeptidase My gene from Mycoplasma salivarium. FEMS Microbiol. Lett. 1995, 130:19-24.
47. Rawlings N.D., Barrett A.J. Evolutionary families of metallopeptidases. Methods Enzymol. 1995, 248:183-228.
48. Taylor A. Aminopeptidases, structure and function. FASEB J. 1993, 7:290-298.
49. Lowther W.T., Matthews B.W. Metalloaminopeptidases, common functional themes in disparate structural surroundings. Chem. Rev. 2002, 102:4581-4608.
50. Gonzales T., Robert-Baudouy J. Bacterial aminopeptidases, properties and functions. FEMS Microbiol. Rev. 1996, 18:319-344.
51. Miller C.G. Protein degradation and proteolytic modification. Escherichia coli and Salmonella typhimurium, Cellular and Molecular Biology 1996, Vol. 2:938-954. ASM Press, Washington DC. 2nd ed.
52. Matsui M., Fowler J.H., Walling L.L. Leucine aminopeptidases, diversity in structure and function. Biol. Chem. 2006, 387:1535-1544.