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. 1993 Oct 1;295(Pt 1):57–60. doi: 10.1042/bj2950057

Thimet oligopeptidase: similarity to 'soluble angiotensin II-binding protein' and some corrections to the published amino acid sequence of the rat testis enzyme.

N McKie 1, P M Dando 1, N D Rawlings 1, A J Barrett 1
PMCID: PMC1134819  PMID: 8216239

Abstract

The deduced amino acid sequence of pig liver soluble angiotensin II-binding protein [Sugiura, Hagiwara and Hirose (1992) J. Biol. Chem. 267, 18067-18072] is similar over most of its length to that reported for rat testis thimet oligopeptidase (EC 3.4.24.15) by Pierotti, Dong, Glucksman, Orlowski and Roberts [(1990) (Biochemistry 29, 10323-10329]. We have found that homogeneous rat testis thimet oligopeptidase binds angiotensin II with the same distinctive characteristics as the pig liver protein. Analysis of the nucleotide sequences reported for the two proteins pointed to the likelihood that sequencing errors had caused two segments of the amino acid sequence of the rat protein to be translated out of frame, and re-sequencing of selected parts of the clone (kindly provided by the previous authors) confirmed this. The revised deduced amino acid sequence of rat thimet oligopeptidase contains 687 residues, representing a protein of 78,308 Da, and is more closely related to those of the pig liver protein and other known homologues of thimet oligopeptidase than that described previously.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Acker G. R., Molineaux C., Orlowski M. Synaptosomal membrane-bound form of endopeptidase-24.15 generates Leu-enkephalin from dynorphin1-8, alpha- and beta-neoendorphin, and Met-enkephalin from Met-enkephalin-Arg6-Gly7-Leu8. J Neurochem. 1987 Jan;48(1):284–292. doi: 10.1111/j.1471-4159.1987.tb13160.x. [DOI] [PubMed] [Google Scholar]
  2. Barrett A. J., Brown M. A. Chicken liver Pz-peptidase, a thiol-dependent metallo-endopeptidase. Biochem J. 1990 Nov 1;271(3):701–706. doi: 10.1042/bj2710701. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Camargo A. C., Caldo H., Emson P. C. Degradation of neurotensin by rabbit brain endo-oligopeptidase A and endo-oligopeptidase B (proline-endopeptidase). Biochem Biophys Res Commun. 1983 Nov 15;116(3):1151–1159. doi: 10.1016/s0006-291x(83)80263-0. [DOI] [PubMed] [Google Scholar]
  4. Chu T. G., Orlowski M. Soluble metalloendopeptidase from rat brain: action on enkephalin-containing peptides and other bioactive peptides. Endocrinology. 1985 Apr;116(4):1418–1425. doi: 10.1210/endo-116-4-1418. [DOI] [PubMed] [Google Scholar]
  5. Cicilini M. A., Ribeiro M. J., de Oliveira E. B., Mortara R. A., de Camargo A. C. Endooligopeptidase A activity in rabbit heart: generation of enkephalin from enkephalin containing peptides. Peptides. 1988 Sep-Oct;9(5):945–955. doi: 10.1016/0196-9781(88)90072-1. [DOI] [PubMed] [Google Scholar]
  6. Conlin C. A., Miller C. G. Cloning and nucleotide sequence of opdA, the gene encoding oligopeptidase A in Salmonella typhimurium. J Bacteriol. 1992 Mar;174(5):1631–1640. doi: 10.1128/jb.174.5.1631-1640.1992. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. Conlin C. A., Trun N. J., Silhavy T. J., Miller C. G. Escherichia coli prlC encodes an endopeptidase and is homologous to the Salmonella typhimurium opdA gene. J Bacteriol. 1992 Sep;174(18):5881–5887. doi: 10.1128/jb.174.18.5881-5887.1992. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. Dando P. M., Brown M. A., Barrett A. J. Human thimet oligopeptidase. Biochem J. 1993 Sep 1;294(Pt 2):451–457. doi: 10.1042/bj2940451. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. De Camargo A. C., Da Fonseca M. J., Caldo H., De Morais Carvalho K. Influence of the carboxyl terminus of luteinizing hormone-releasing hormone and bradykinin on hydrolysis by brain endo-oligopeptidases. J Biol Chem. 1982 Aug 25;257(16):9265–9267. [PubMed] [Google Scholar]
  10. Giasson L., Specht C. A., Milgrim C., Novotny C. P., Ullrich R. C. Cloning and comparison of A alpha mating-type alleles of the Basidiomycete Schizophyllum commune. Mol Gen Genet. 1989 Jul;218(1):72–77. doi: 10.1007/BF00330567. [DOI] [PubMed] [Google Scholar]
  11. Hagiwara H., Sugiura N., Wakita K., Hirose S. Purification and characterization of angiotensin-binding protein from porcine liver cytosolic fraction. Eur J Biochem. 1989 Nov 6;185(2):405–410. doi: 10.1111/j.1432-1033.1989.tb15129.x. [DOI] [PubMed] [Google Scholar]
  12. Hamilton S., Miller C. G. Cloning and nucleotide sequence of the Salmonella typhimurium dcp gene encoding dipeptidyl carboxypeptidase. J Bacteriol. 1992 Mar;174(5):1626–1630. doi: 10.1128/jb.174.5.1626-1630.1992. [DOI] [PMC free article] [PubMed] [Google Scholar]
  13. Isaya G., Kalousek F., Rosenberg L. E. Sequence analysis of rat mitochondrial intermediate peptidase: similarity to zinc metallopeptidases and to a putative yeast homologue. Proc Natl Acad Sci U S A. 1992 Sep 1;89(17):8317–8321. doi: 10.1073/pnas.89.17.8317. [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. Kawabata S., Nakagawa K., Muta T., Iwanaga S., Davie E. W. Rabbit liver microsomal endopeptidase with substrate specificity for processing proproteins is structurally related to rat testes metalloendopeptidase 24.15. J Biol Chem. 1993 Jun 15;268(17):12498–12503. [PubMed] [Google Scholar]
  15. Kiron M. A., Soffer R. L. Purification and properties of a soluble angiotensin II-binding protein from rabbit liver. J Biol Chem. 1989 Mar 5;264(7):4138–4142. [PubMed] [Google Scholar]
  16. McDermott J. R., Gibson A. M., Turner J. D. Involvement of endopeptidase 24.15 in the inactivation of bradykinin by rat brain slices. Biochem Biophys Res Commun. 1987 Jul 15;146(1):154–158. doi: 10.1016/0006-291x(87)90704-2. [DOI] [PubMed] [Google Scholar]
  17. Messing J. New M13 vectors for cloning. Methods Enzymol. 1983;101:20–78. doi: 10.1016/0076-6879(83)01005-8. [DOI] [PubMed] [Google Scholar]
  18. Oliver S. G., van der Aart Q. J., Agostoni-Carbone M. L., Aigle M., Alberghina L., Alexandraki D., Antoine G., Anwar R., Ballesta J. P., Benit P. The complete DNA sequence of yeast chromosome III. Nature. 1992 May 7;357(6373):38–46. doi: 10.1038/357038a0. [DOI] [PubMed] [Google Scholar]
  19. Orlowski M., Michaud C., Chu T. G. A soluble metalloendopeptidase from rat brain. Purification of the enzyme and determination of specificity with synthetic and natural peptides. Eur J Biochem. 1983 Sep 1;135(1):81–88. doi: 10.1111/j.1432-1033.1983.tb07620.x. [DOI] [PubMed] [Google Scholar]
  20. Pierotti A., Dong K. W., Glucksman M. J., Orlowski M., Roberts J. L. Molecular cloning and primary structure of rat testes metalloendopeptidase EC 3.4.24.15. Biochemistry. 1990 Nov 13;29(45):10323–10329. doi: 10.1021/bi00497a006. [DOI] [PubMed] [Google Scholar]
  21. Rawlings N. D., Barrett A. J. Evolutionary families of peptidases. Biochem J. 1993 Feb 15;290(Pt 1):205–218. doi: 10.1042/bj2900205. [DOI] [PMC free article] [PubMed] [Google Scholar]
  22. Sanger F., Nicklen S., Coulson A. R. DNA sequencing with chain-terminating inhibitors. Proc Natl Acad Sci U S A. 1977 Dec;74(12):5463–5467. doi: 10.1073/pnas.74.12.5463. [DOI] [PMC free article] [PubMed] [Google Scholar]
  23. Sen I., Jim K. F., Soffer R. L. Solubilization and characterization of an angiotensin II binding protein from liver. Eur J Biochem. 1983 Oct 17;136(1):41–49. doi: 10.1111/j.1432-1033.1983.tb07702.x. [DOI] [PubMed] [Google Scholar]
  24. Staden R. Finding protein coding regions in genomic sequences. Methods Enzymol. 1990;183:163–180. doi: 10.1016/0076-6879(90)83012-x. [DOI] [PubMed] [Google Scholar]
  25. Sugiura N., Hagiwara H., Hirose S. Molecular cloning of porcine soluble angiotensin-binding protein. J Biol Chem. 1992 Sep 5;267(25):18067–18072. [PubMed] [Google Scholar]
  26. Tisljar U., Knight C. G., Barrett A. J. An alternative quenched fluorescence substrate for Pz-peptidase. Anal Biochem. 1990 Apr;186(1):112–115. doi: 10.1016/0003-2697(90)90582-t. [DOI] [PubMed] [Google Scholar]

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