The Biochemical and molecular characterization of recombinant Bacillus subtilis tripeptidase (PepT) as a zinc-dependent metalloenzyme

Molecules and Cells

Volumn 10, Issue 4, 2000, Pages 423-431

  Cha, Myung Hoon ^a   Yong, Whan Mi ^a   Lee, Sang Min ^a   Lee, Young Seek ^a   Chung, Il Yup ^a  

^a Hanyang University   (South Korea)

Author keywords

Aminopeptidase; Metalloenzyme; Tripeptidase; Zinc Ion

Indexed keywords

AMINOPEPTIDASE; CATION; COBALT; METALLOPROTEIN; PEPT TRIPEPTIDASE; RECOMBINANT PROTEIN; ZINC;

AMINO ACID SEQUENCE; ARTICLE; BACILLUS SUBTILIS; BACTERIAL GENE; CHEMISTRY; DNA SEQUENCE; ENZYMOLOGY; GENE DELETION; GENETICS; ISOLATION AND PURIFICATION; PROTEIN DENATURATION;

AMINO ACID SEQUENCE; AMINOPEPTIDASES; BACILLUS SUBTILIS; CATIONS; COBALT; GENES, BACTERIAL; METALLOPROTEINS; PROTEIN DENATURATION; RECOMBINANT PROTEINS; SEQUENCE ANALYSIS, DNA; SEQUENCE DELETION; ZINC;

EID: 0034738919     PISSN: 10168478     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article

References (39)

1. Allen, M. P., Yamada, A. H., and Carpenter, F. H. (1983) Kinetic parameters of metal-substituted leucine aminopeptidase from bovine lens. Biochemistry 22, 3778-3783.
2. Arfin, S. M., Kendall, R. L., Hall, L., Weaver, L. H., Stewart, A. E., Matthews, B. W., and Bradshaw, R. A. (1995) Eukaryotic methionyl aminopeptidases: two classes of cobalt-dependent enzymes. Proc. Natl. Acad. Sci. USA 92, 7714-7718.
3. Bayliss, M. E. and Prescott, J. M. (1986) Modified activity of Aeromonas aminopeptidase: metal ion substitutions and role of substrates. Biochemistry 25, 8113-8117.
4. Bazan, J. F., Weaver, L. H., Roderick, S. L., Huber, R., and Matthews, B. W. (1994) Sequence and structure comparison suggest that methionine aminopeptidase, prolidase, aminopeptidase P, and creatinase share a common fold. Proc. Natl. Acad. Sci. USA 91, 2473-2477.
5. Ben-Bassat, A., Bauer, K., Chang, S.-Y., Myambo, K., Boosman, A., and Chang, S. (1987) Processing of the initiation methionine from proteins: properties of the Escherichia coli methionine aminopeptidase and its gene structure. J. Bacteriol. 169, 751-757.
6. Bosman, B. W., Tan, P. S. T., and Konings, W. N. (1990) Purification and characterization of a tripeptidase from Lactococcus lactis subsp. cremoris Wg2. Appl. Environ. Microbiol. 56, 1839-1843.
7. Burley, S. K., David, P. R., Sweet, R. M., Taylor, A., and Lipscomb, W. N. (1992) Structure determination and refinement of bovine lens leucine aminopeptidase and its complex with bestatin. J. Mol. Biol. 224, 113-140.
8. Chang, Y. H., Teichert, U., and Smith, J.A. (1990) Purification and characterization of a methionine aminopeptidase from Sacchromyces cerevisiae. J. Biol. Chem. 265, 19892-19897.
9. Fleischmann, R. D., Adams, M. D., White, O., Clayton, R. A., Kirkness, E. F., Kerlavage, A. R., Bult, C. J., Tomb, J.-F., Dougherty, B. A., Merrick, J. M., McKenney, K., Sutton, G., FitzHugh, W., Fields, C., Gocayne, J. D., Scott, J., Shirley, R., Liu, L.-I., Glodek, A., Kelley, J. M., Weidman, J F., Phillips, C. A., Spriggs, T., Hedblom, E., Cotton, M. D., Utterback, T. R., Hanna, M. C., Nguyen, D. T., Saudek, D. M., Brandon, R. C., Fine, L. D., Fritchman, J. L., Fuhrmann, J. L., Geoghagen, N. S. M., Gnehm, C. L., McDonald, L. A., Small, K. V., Fraser, C. M., Smith, H. O., and Venter, J. C. (1995) Wholegenome random sequencing and assembly of Haemophilus influenzas Rd. Science 269, 496-512.
10. Foglino, M., Gharbi, S., and Lazdunski, A. (1986) Nucleotide sequence of the pepN gene encoding aminopeptidase N of Escherichia coli. Gene 49, 303-309.
11. Ghosh, M., Grunden, A. M., Dunn, D. M., Weiss, R. and Adams, M. W. W. (1998) Characterization of native and recombinant forms of an unusual cobalt-dependent proline dipeptidase (prolidase) from the hyperthermophilic archaeor. Pyrococcus furiosus. J. Bacteriol. 180, 4781-4789.
12. Gonzales, T. and Robert-Baudouy, J. (1996) Bacterial aminopeptidases: properties and functions. FEMS Microbiol. Rev. 18, 319-344.
13. Guenet, C., Lepage, P., and Harris, B. A. (1992) Isolation of the leucine aminopeptidase gene from Aeromonas proteolytica. Evidence for an enzyme precursor. J. Biol. Chem. 267, 8390-8395.
14. Hermsdorf, C. L. (1978) Tripeptide-specific aminopeptidase from Escherichia coli AJ005. Biochemistry 17, 3370-3376.
15. Hooper, N. M. (1994) Families of zinc metalloproteases. FEBS Lett. 354, 1-6.
16. Jiang, W. and Bond, J. S. (1992) Families of metalloendopeptidases and their relationships. FEBS Lett. 312, 110-114.
17. Jongeneel, C. V., Bouvier, J., and Bairoch, A. (1989) A unique signature identifies a family of zinc-dependent metallopeptidases. FEBS Lett. 242, 211-214.
18. Kendall, R. L. and Bradshaw, R. A. (1992) Isolation and characterization of the methionine aminopeptidase from porcine liver responsible for the co-translational processing of proteins. J. Biol. Chem. 267, 20667-20673.
19. Klein, I. R., Klein, U., Schad, M., and Plapp, R. (1993) Cloning, DNA sequence analysis and partial characterization of pepN, a lysyl aminopeptidase from Lactobacillus delbrueckii ssp. lactis DSM7290. Eur. J. Biochem. 217, 105-114.
20. Lombardo, M.-J., Miller, C. G., and Rudd, K. E. (1993) Physical mapping of the Escherichia coli pepT and potABCD genes. J. Bacteriol. 175, 7745-7746.
21. McCaman, M. T. and Gabe, J. D. (1986) The nucleotide sequence of the pepN gene and its over-expression in Escherichia coli. Gene 48, 145-153.
22. Mierau, I., Haandrikman, A. J., Velterop, O., Tan, P. S. T., Leenhouts, K. L., Konings, W. N., Venema, G., and Kok, J. (1994) Tripeptidase gene (pepT) of Lactococcus lactis: molecular cloning and nucleotide sequencing of pepT and construction of a chromosomal deletion mutant. J. Bacteriol. 176, 2854-2861.
23. Miller, C. G. and MacKinnon, K. (1974) Peptidase mutants of Salmonella typhimurium. J. Bacteriol. 120, 355-363.
24. Miller, C. G. and Schwartz, G. (1978) Peptidase-deficient mutants of Escherichia coli. J. Bacteriol. 135, 603-611.
25. Miller, C. G., Miller, J. L., and Bagga, D. A. (1991) Cloning and nucleotide sequence of the anaerobically regulated pepT gene of Salmonella typhimurium. J. Bacteriol. 173, 3554-3558.
26. Park, Y. S., Cha, M. H., Yong, W.-M., Kim, H. J., Chung, I. Y., and Lee, Y. S. (1999) The purification and characterization of Bacillus subtilis tripeptidase (PepT). J. Biochem. Mol. Biol. 32, 239-246.
27. Roderick, S. L. and Matthews, B. W. (1993) Structure of the cobalt-dependent methionine aminopeptidase from Escherichia coli: a new type of proteolytic enzyme. Biochemistry 32, 3907-3912.
28. Schrogel, O., Krispin, O., and Allmansberger, R. (1996) Expression of a pepT homologue from Bacillus subtilis. FEMS Microbiol. Lett. 145, 341-348.
29. Simitsopoulou, M., Vafopoulou, A., Choli-Papadopoulou, T., and Alichanidis, E. (1997) Purification and partial characterization of a tripeptidase from Pediococcus pentosaceus K9.2. Appl. Environ. Microbiol. 63, 4872-4876.
30. Squire, C. R., Talebian, M., Menon, J. G., Dekruyff, S., Lee, T. D., Shively, J. E., and Rothman, B. S. (1991) Leucine aminopeptidase-like activity in Aplysia hemolymph rapidly degrades biologically active alpha-bag cell peptide fragments. J. Biol. Chem. 266, 22355-22363.
31. Stirling, C. J., Colloms, S. D., Collins, J. F., Szatmari, G., and Sherratt, D. J. (1989) xerB, an Escherichia coli gene required for plasmid Co1E1 site-specific recombination, is identical to pepA, encoding aminopeptidase A, a protein with substantial similarity to bovine lens leucine aminopeptidase. EMBO J. 8, 1623-1627.
32. Strater, N. and Lipscomb, W. N. (1995) Two-metal ion mechanism of bovine lens leucine aminopeptidase: active site solvent structure and binding mode of L-leucinal, a gemdiolate transition state analogue, by X-ray crystallography. Biochemistry 34, 14792-14800.
33. Strauch, K. L. and Miller, C. G. (1983) Isolation and characterization Salmonella typhimurium mutants lacking a tripeptidase (Peptidase T). J. Bacteriol. 154, 763-771.
34. Tan, P. S. T., van Alen-Boerrigter, I. J., Poolman, B., Siezen, R. J., de Vos, W. M., and Konings, W. N. (1992) Characterization of the Lactococcus lactis pepN gene encoding an aminopeptidase homologous to mammalian aminopeptidase N. FEBS Lett. 306, 9-16.
35. Taylor, A. (1993) Aminopeptidases: towards a mechanism of action. Trends Biochem. Sci. 18, 167-171.
36. 2+ as a cofactor: A case of mistaken identity? Protein Sci. 7, 2684-2687.
37. Wilcox, D. E. (1996) Binuclear metallohydrolases. Chem. Rev. 96, 2435-2458.
38. Yen, C., Green, L., and Miller, C. G. (1980) Degradation of intracellular protein in Salmonella typhimurium peptidase mutants. J. Mol. Biol. 143, 21-33.
39. Yoon, J. W. and Kwon, Y. M. (1993) Partial purification and properties of Aminopeptidases in Cotyledons of Cancavalia lineata L. Mol. Cells 3, 83-88.