Proteolysis in eucaryotic cells: aminopeptidases and dipeptidyl aminopeptidases of yeast revisited - PubMed (original) (raw)
Proteolysis in eucaryotic cells: aminopeptidases and dipeptidyl aminopeptidases of yeast revisited
T Achstetter et al. Arch Biochem Biophys. 1983.
Abstract
Using nine different L-aminoacyl-4-nitroanilides and four different dipeptidyl-4-nitroanilides, aminopeptidases and dipeptidyl aminopeptidases active at pH 7.5 and (or) pH 5.5 in logarithmically growing and stationary-phase cells of Saccharomyces cerevisiae were searched for. Ion-exchange chromatography was used to separate the proteins of the soluble cell extract. Besides the three already-characterized aminopeptidases--aminopeptidase I (P. Matile, A. Wiemken, and W. Guyer (1971) Planta (Berlin) 96, 43-53; J. Frey and K. H. Röhm (1978) Biochim. Biophys. Acta 527, 31-41), aminopeptidase II (J. Frey and K. H. Röhm (1978) Biochim. Biophys. Acta 527, 31-41; J. Knüver (1982) Thesis, Fachbereich Chemie, Marburg, FRG), and aminopeptidase Co (T. Achstetter, C. Ehmann, and D. H. Wolf (1982) Biochem. Biophys. Res. Commun. 109, 341-347)--12 additional aminopeptidase activities are found in soluble cell extracts eluting from the ion-exchange column. These activities differ from the characterized aminopeptidases in one or more of the parameters such as charge, size, substrate specificity, inhibition pattern, pH optimum for activity and regulation. Also, a particulate aminopeptidase, called aminopeptidase P, is found in the nonsoluble fraction of disintegrated cells. Besides the described particulate X-prolyl-dipeptidyl aminopeptidase (M. P. Suarez Rendueles, J. Schwencke, N. Garcia-Alvarez and S. Gascon (1981) FEBS Lett. 131, 296-300), three additional dipeptidyl aminopeptidase activities of different substrate specificities are found in the soluble extract.
Similar articles
- Dipeptidyl-aminopeptidases and aminopeptidases in Dictyostelium discoideum.
Chan SA, Toursarkissian K, Sweeney JP, Jones TH. Chan SA, et al. Biochem Biophys Res Commun. 1985 Mar 29;127(3):962-8. doi: 10.1016/s0006-291x(85)80038-3. Biochem Biophys Res Commun. 1985. PMID: 3885944 - Proline specific endo- and exopeptidases.
Walter R, Simmons WH, Yoshimoto T. Walter R, et al. Mol Cell Biochem. 1980 Apr 18;30(2):111-27. doi: 10.1007/BF00227927. Mol Cell Biochem. 1980. PMID: 6991912 Review. - Generation of non-bitter casein hydrolysates by using combinations of a proteinase and aminopeptidases.
O'Cuinn G, FitzGerald R, Bouchier P, McDonnell M. O'Cuinn G, et al. Biochem Soc Trans. 1999 Aug;27(4):730-4. doi: 10.1042/bst0270730. Biochem Soc Trans. 1999. PMID: 10917673 Review. No abstract available.
Cited by
- Quantitative proteomic comparison of stationary/G0 phase cells and tetrads in budding yeast.
Kumar R, Srivastava S. Kumar R, et al. Sci Rep. 2016 Aug 25;6:32031. doi: 10.1038/srep32031. Sci Rep. 2016. PMID: 27558777 Free PMC article. - Structure and activity of CPNGRC: a modified CD13/APN peptidic homing motif.
Plesniak LA, Salzameda B, Hinderberger H, Regan E, Kahn J, Mills SA, Teriete P, Yao Y, Jennings P, Marassi F, Adams JA. Plesniak LA, et al. Chem Biol Drug Des. 2010 Jun;75(6):551-62. doi: 10.1111/j.1747-0285.2010.00974.x. Epub 2010 Mar 30. Chem Biol Drug Des. 2010. PMID: 20374250 Free PMC article. - Aminopeptidase C of Aspergillus niger is a novel phenylalanine aminopeptidase.
Basten DE, Dekker PJ, Schaap PJ. Basten DE, et al. Appl Environ Microbiol. 2003 Feb;69(2):1246-50. doi: 10.1128/AEM.69.2.1246-1250.2003. Appl Environ Microbiol. 2003. PMID: 12571053 Free PMC article. - Stationary phase in the yeast Saccharomyces cerevisiae.
Werner-Washburne M, Braun E, Johnston GC, Singer RA. Werner-Washburne M, et al. Microbiol Rev. 1993 Jun;57(2):383-401. doi: 10.1128/mr.57.2.383-401.1993. Microbiol Rev. 1993. PMID: 8393130 Free PMC article. Review. - Hormone processing and membrane-bound proteinases in yeast.
Achstetter T, Wolf DH. Achstetter T, et al. EMBO J. 1985 Jan;4(1):173-7. doi: 10.1002/j.1460-2075.1985.tb02333.x. EMBO J. 1985. PMID: 3894003 Free PMC article.