Bovine pepsinogens and pepsins. The sequence around a reactive aspartyl residue (original) (raw)

Abstract

The specific inhibitor, _N_-diazoacetylnorleucine methyl ester reacts stoicheiometrically with bovine pepsin resulting in a simultaneous loss of all enzymic activity. A peptide containing a modified aspartyl group was isolated from bovine pepsin labelled with 14C-labelled inhibitor. The aspartic acid residue is presumed to be part of the active centre and is in the same heptapeptide sequence as in porcine pepsin: Ile-Val-Asp-Thr-Gly-Thr-Ser.

673

Selected References

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

  1. Bayliss R. S., Knowles J. R., Wybrandt G. B. An aspartic acid residue at the active site of pepsin. The isolation and sequence of the heptapeptide. Biochem J. 1969 Jun;113(2):377–386. doi: 10.1042/bj1130377. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Blombäck B., Blombäck M., Edman P., Hessel B. Human fibrinopeptides. Isolation, characterization and structure. Biochim Biophys Acta. 1966 Feb 28;115(2):371–396. doi: 10.1016/0304-4165(66)90437-5. [DOI] [PubMed] [Google Scholar]
  3. Chow R. B., Kassel B. Bovine pepsinogen and pepsin. I. Isolation, purification, and some properties of the pepsinogen. J Biol Chem. 1968 Apr 25;243(8):1718–1724. [PubMed] [Google Scholar]
  4. Cornish-Bowden A. J., Knowles J. R. The pH-dependence of pepsin-catalysed reactions. Biochem J. 1969 Jun;113(2):353–362. doi: 10.1042/bj1130353. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Delpierre G. R., Fruton J. S. Inactivation of pepsin by diphenyldiazomethane. Proc Natl Acad Sci U S A. 1965 Oct;54(4):1161–1167. doi: 10.1073/pnas.54.4.1161. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. Delpierre G. R., Fruton J. S. Specific inactivation of pepsin by a diazo ketone. Proc Natl Acad Sci U S A. 1966 Dec;56(6):1817–1822. doi: 10.1073/pnas.56.6.1817. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. Edman P., Begg G. A protein sequenator. Eur J Biochem. 1967 Mar;1(1):80–91. doi: 10.1007/978-3-662-25813-2_14. [DOI] [PubMed] [Google Scholar]
  8. Erlanger B. F., Vratsanos S. M., Wassermann N., Cooper A. G. Stereochemical investigation of the active center of pepsin using a new inactivator. Biochem Biophys Res Commun. 1967 Jul 21;28(2):203–208. doi: 10.1016/0006-291x(67)90430-5. [DOI] [PubMed] [Google Scholar]
  9. Fry K. T., Kim O. K., Kettering C. F., Spona J., Hamilton G. A. A reactive aspartyl residue of pepsin. Biochem Biophys Res Commun. 1968 Mar 12;30(5):489–495. doi: 10.1016/0006-291x(68)90078-8. [DOI] [PubMed] [Google Scholar]
  10. Ginodman L. M., Valueva T. A., Kozlov L. V., Shkarenkova L. S. Dokazatel'stvo blokirovaniia diazikarbonil'nym ingibitorom karboksil'noi gruppy aktivnogo tsentra pepsina. Biokhimiia. 1969 Jan-Feb;34(1):211–213. [PubMed] [Google Scholar]
  11. HEILMANN J., BARROLLIER J., WATZKE E. Beitrag zur Aminosäurebestimmung auf Papierchromatogrammen. Hoppe Seylers Z Physiol Chem. 1957;309(4-6):219–220. [PubMed] [Google Scholar]
  12. Kay J., Ryle A. P. An active site peptide from pepsin C. Biochem J. 1971 Jun;123(1):75–82. doi: 10.1042/bj1230075. [DOI] [PMC free article] [PubMed] [Google Scholar]
  13. Knowles J. R., Wybrandt G. B. The sequence around an active-site aspartyl residue in pepsin. FEBS Lett. 1968 Sep;1(4):211–212. doi: 10.1016/0014-5793(68)80063-8. [DOI] [PubMed] [Google Scholar]
  14. Lang H. M., Kassell B. Bovine pepsinogens and pepsins. 3. Composition and specificity of the pepsins. Biochemistry. 1971 Jun 8;10(12):2296–2301. doi: 10.1021/bi00788a018. [DOI] [PubMed] [Google Scholar]
  15. Lundblad R. L., Stein W. H. On the reaction of diazoacetyl compounds with pepsin. J Biol Chem. 1969 Jan 10;244(1):154–160. [PubMed] [Google Scholar]
  16. Meitner P. A., Kassell B. Bovine pepsinogens and pepsins. A series of zymogens and enzymes that differ in organic phosphate content. Biochem J. 1971 Jan;121(2):249–256. doi: 10.1042/bj1210249. [DOI] [PMC free article] [PubMed] [Google Scholar]
  17. Ong E. B., Perlmann G. E. Specific inactivation of pepsin by benzyloxycarbonyl-L-phenylalanyldiazomethane. Nature. 1967 Sep 30;215(5109):1492–1494. doi: 10.1038/2151492b0. [DOI] [PubMed] [Google Scholar]
  18. RAO K. R., BIRNBAUM S. M., KINGSLEY R. B., GREENSTEIN J. P. Enzymatic susceptibility of corresponding chloroacetyl- and glycyl-L-amino acids. J Biol Chem. 1952 Oct;198(2):507–524. [PubMed] [Google Scholar]
  19. Rajagopalan T. G., Stein W. H., Moore S. The inactivation of pepsin by diazoacetylnorleucine methyl ester. J Biol Chem. 1966 Sep 25;241(18):4295–4297. [PubMed] [Google Scholar]
  20. Sodek J., Hofmann T. Amino acid sequence around the active site aspartic acid in penicillopepsin. Can J Biochem. 1970 Sep;48(9):1014–1016. doi: 10.1139/o70-158. [DOI] [PubMed] [Google Scholar]
  21. Stepanov V. M., Vaganova T. I. Identification of the carboxyl group of pepsin reacting with diazoacetamide derivatives. Biochem Biophys Res Commun. 1968 Jun 10;31(5):825–830. doi: 10.1016/0006-291x(68)90637-2. [DOI] [PubMed] [Google Scholar]