Substrate phosphorylation can inhibit proteolysis by trypsin-like enzymes - PubMed (original) (raw)
Substrate phosphorylation can inhibit proteolysis by trypsin-like enzymes
M Benore-Parsons et al. Arch Biochem Biophys. 1989.
Abstract
The effect of substrate phosphorylation on the susceptibility to proteolytic cleavage by trypsin-like enzymes was investigated using the model heptapeptide Leu-Arg-Arg-Ala-Ser-Leu-Gly, a peptide representing the endogenous phosphorylation site of pyruvate kinase. Phosphorylation of Ser 5 altered the kinetics of proteolysis by two proteases, trypsin and rat plasma kallikrein, both of which cleaved between Arg 3 and Ala 4. In the case of trypsin, phosphorylation decreased the rate of cleavage 47-fold. In the case of rat plasma kallikrein, phosphorylation decreased proteolysis 13-fold. Phosphorylation resulted in an apparent redirection of the preferential site from Arg 3 to Arg 2. Because sequences analogous to this model peptide are commonly found in exposed domains of globular proteins, and since these regions are susceptible to both phosphorylation and protease attack, the results indicate that substrate phosphorylation may selectively influence protein processing and turnover.
Similar articles
- Phosphorylation of ribosomal protein S6 and a peptide analogue of S6 by a protease-activated kinase isolated from rat liver.
Gabrielli B, Wettenhall RE, Kemp BE, Quinn M, Bizonova L. Gabrielli B, et al. FEBS Lett. 1984 Oct 1;175(2):219-26. doi: 10.1016/0014-5793(84)80740-1. FEBS Lett. 1984. PMID: 6479343 - Tetrapeptide substrates for the discrimination among kallikreins and other trypsin-like serine proteinases.
Prado ES, Araújo-Viel MS, Juliano MA, Juliano L, Stella RC, Sampaio CA. Prado ES, et al. Biol Chem Hoppe Seyler. 1986 Mar;367(3):199-205. doi: 10.1515/bchm3.1986.367.1.199. Biol Chem Hoppe Seyler. 1986. PMID: 3518738 - Effects of secondary interactions on the kinetics of peptide and peptide ester hydrolysis by tissue kallikrein and trypsin.
Fiedler F. Fiedler F. Eur J Biochem. 1987 Mar 2;163(2):303-12. doi: 10.1111/j.1432-1033.1987.tb10801.x. Eur J Biochem. 1987. PMID: 3643848 - Mapping the active sites of bovine thrombin, factor IXa, factor Xa, factor XIa, factor XIIa, plasma kallikrein, and trypsin with amino acid and peptide thioesters: development of new sensitive substrates.
McRae BJ, Kurachi K, Heimark RL, Fujikawa K, Davie EW, Powers JC. McRae BJ, et al. Biochemistry. 1981 Dec 8;20(25):7196-206. doi: 10.1021/bi00528a022. Biochemistry. 1981. PMID: 6976185 - Anterior pituitary glandular kallikrein: trypsin activation and estrogen regulation.
Powers CA. Powers CA. Mol Cell Endocrinol. 1986 Jul;46(2):163-74. doi: 10.1016/0303-7207(86)90095-x. Mol Cell Endocrinol. 1986. PMID: 3522314
Cited by
- Epstein-Barr virus protein EBNA-LP engages YY1 through leucine-rich motifs to promote naïve B cell transformation.
Cable JM, Reinoso-Vizcaino NM, White RE, Luftig MA. Cable JM, et al. PLoS Pathog. 2024 Jul 31;20(7):e1011950. doi: 10.1371/journal.ppat.1011950. eCollection 2024 Jul. PLoS Pathog. 2024. PMID: 39083560 Free PMC article. - Peptidomics Analysis of Milk Protein-Derived Peptides Released over Time in the Preterm Infant Stomach.
Beverly RL, Underwood MA, Dallas DC. Beverly RL, et al. J Proteome Res. 2019 Mar 1;18(3):912-922. doi: 10.1021/acs.jproteome.8b00604. Epub 2019 Jan 24. J Proteome Res. 2019. PMID: 30638015 Free PMC article. - Antibacterial Peptides in Dermatology-Strategies for Evaluation of Allergic Potential.
Deptuła M, Wardowska A, Dzierżyńska M, Rodziewicz-Motowidło S, Pikuła M. Deptuła M, et al. Molecules. 2018 Feb 14;23(2):414. doi: 10.3390/molecules23020414. Molecules. 2018. PMID: 29443886 Free PMC article. Review. - Proteomic discovery of host kinase signaling in bacterial infections.
Richter E, Mostertz J, Hochgräfe F. Richter E, et al. Proteomics Clin Appl. 2016 Oct;10(9-10):994-1010. doi: 10.1002/prca.201600035. Epub 2016 Sep 9. Proteomics Clin Appl. 2016. PMID: 27440122 Free PMC article. Review. - A vitellogenin polyserine cleavage site: highly disordered conformation protected from proteolysis by phosphorylation.
Havukainen H, Underhaug J, Wolschin F, Amdam G, Halskau Ø. Havukainen H, et al. J Exp Biol. 2012 Jun 1;215(Pt 11):1837-46. doi: 10.1242/jeb.065623. J Exp Biol. 2012. PMID: 22573762 Free PMC article.
MeSH terms
Substances
LinkOut - more resources
Full Text Sources
Other Literature Sources