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