1,224
Views
7
CrossRef citations to date
0
Altmetric
Research Article

Kinetic and computational analysis of the reversible inhibition of porcine pancreatic elastase: a structural and mechanistic approach

, , , &
Pages 131-139 | Received 24 Mar 2016, Accepted 01 Jul 2016, Published online: 04 Aug 2016

References

  • Bieth JG. Elastases: catalytic and biological properties. New York: Academic Press; 1986:217–320
  • Werb Z, Banda MJ, McKerrow JH, Sandhaus RA. Elastases and elastin degradation. J Invest Dermatol 1982;79:154–9
  • van de Lest CH, Versteeg EM, Veerkamp JH, van Kuppevelt TH. Digestion of proteoglycans in porcine pancreatic elastase-induced emphysema in rats. Eur Respir J 1995;8:238–45
  • Shotton DM, Hartley BS. Amino-acid sequence of porcine pancreatic elastase and its homologies with other serine proteinases. Nature 1970;225:802–6
  • Li de la Sierra I, Papamichael EM, Sakarellos C, et al. Interaction of the peptide CF3-Leu-Ala-NH-C6H4-CF3 (TFLA) with porcine pancreatic elastase. X-ray studies at 1.8A. J Mol Recognit 1990;3:36–44
  • Bieth JG, Dirrig S, Jung ML, et al Investigation of the active center of rat pancreatic elastase. Biochim Biophys Acta 1989;994:64–74
  • Theodorou LG, Lymperopoulos K, Bieth JG, Papamichael EM. Insight into the catalysis of hydrolysis of four newly synthesized substrates by papain: a proton inventory study. Biochemistry 2001;40:3996–4004
  • Volk A, Mispelter J, Dimicoli JL, et al. Heteronuclear directed site-selective NOESY spectroscopy by polarization transfer or multiple quantum filtering. Mag Resonance Chem 1988;26:78–84
  • McCrudden MTC, Ryan LA, Turkington P, Timson DJ. The contribution of key hydrophobic residues in ecotin to enzyme-inhibitor complex stability. J Enzyme Inhib Med Chem 2009;24:1207–10
  • Foukis A, Stergiou PY, Theodorou LG, et al. Purification, kinetic characterization and properties of a novel thermo-tolerant extracellular protease from Kluyveromyces marxianus IFO 0288 with potential biotechnological interest. Bioresour Technol 2012;123:214–20
  • Papamichael EM, Stergiou PY, Foukis A, et al. Effective kinetic methods and tools in investigating the mechanism of action of specific hydrolases. In: Ekinci D, ed. Medicinal chemistry and drug design. Rijeka, Croatia: INTECH open science; 2012:235–74
  • Lente G, Fábián I, Poë AJ. A common misconception about the Eyring equation. New J Chem 2005;29:759–60
  • Cleland WW, Northrop DB. Energetics of substrate binding, catalysis, and product release. Methods Enzymol 1999;308:3–27
  • Lyne PD, Lamb ML, Saeh JC. Accurate prediction of the relative potencies of members of a series of kinase inhibitors using molecular docking and MM-GBSA scoring. J Med Chem 2006;49:4805–8
  • Das D, Koh Y, Tojo Y, et al. Prediction of potency of protease inhibitors using free energy simulations with polarizable quantum mechanics-based ligand charges and a hybrid water model. J Chem Inf Model 2009;49:2851–62
  • Bieth JG. Some kinetic consequences of the tight binding of protein-proteinase-inhibitors to proteolytic enzymes and their application to the determination of dissociation constants. In: Fritz H, Tschesche H, Greene LJ, Truscheit E, eds. Bayer-symposium V proteinase inhibitors. New York: Springer-Verlag; 1974:463–9
  • Faller B, Bieth JG. Kinetics of the interaction of chymotrypsin with eglin c. Biochem J 1991;280:27–32
  • Theodorou LG, Bieth JG, Papamichael EM. The catalytic mode of cysteine proteinases of papain (C1) family. Bioresour Technol 2007;98:1931–9
  • Conrad JS, Dawso SR, Hubbard ER, et al. Inhibitor binding to the binuclear active site of tyrosinase: temperature, pH, and solvent deuterium isotope effects. Biochemistry 1994;33:5739–44
  • Papamichael EM, Theodorou LG. Experimental and theoretical approaches in investigating enzymatic mechanisms: applications on the thermo-stable extracellular protease-A-17N-1 from Bacillus sp., with possible biotechnological interest. In: Rao LV, Pandey A, Larroche C, et al., eds. Current topics on bioprocesses in food industry. Vol III. New Delhi, India: Asiatech Publishers INC; 2010:130–9
  • Schowen KB, Schowen RL. Solvent isotope effects of enzyme systems. Meth Enzymol 1982;87:551–606
  • Venkatasubban KS, Schowen RL. The Proton Inventory technique. CRC Crit Rev Biochem 1984;17:1–44
  • Kresge AJ, More O, Powell MF. Solvent isotopes effects, fractionation factors and mechanisms of proton-transfer reactions. In: Buncel E, Lee CC, eds. Isotopes in organic chemistry. Amsterdam: Elsevier; 1987:177–273
  • Stein RL, Strimpler AM, Hori H, Powers JC. Catalysis by human leukocyte elastase: proton inventory as a mechanistic probe. Biochemistry 1987;26:1305–1314
  • Quinn DM, Sutton LD. Theoretical basis and mechanistic utility of solvent isotope effects. In: Cook PF, ed. Enzyme mechanism from isotope effects. Boston, MA: CRC Press; 1991:74–126
  • Papamichael EM, Theodorou LG, Bieth JG. Insight into catalytic mechanism of papain-like cysteine proteinases: the case of D158. Appl Biochem Biotechnol 2004;118:171–5
  • Fersht A. Structure and mechanism in protein science: a guide to enzyme catalysis and protein folding. New York: WH Freeman and Company; 1999:173–181, 348–55
  • Bezeau M, Endrenyi L. Design of experiments for the precise estimation of dose-response parameters: the Hill equation. J Theor Biol 1986;123:415–30
  • Porter CM, Miller BC. Cooperativity in monomeric enzymes with single ligand-binding sites. Bioorg Chem 2012;43:44–50
  • Schowen RL. Mechanistic deductions from solvent isotope effects. In: Streitwieser A, Taft RW, eds. Progress in physical organic chemistry. New York: Wiley Intersciences; 1972:275–329
  • Syrén PO. The solution of nitrogen inversion in amidases. FEBS J 2013;280:3069–83
  • Scheiner S. Analysis of catalytic mechanism of serine proteases. Viability of the ring-flip hypothesis. J Phys Chem B 2008;112:6837–46

Reprints and Corporate Permissions

Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?

To request a reprint or corporate permissions for this article, please click on the relevant link below:

Academic Permissions

Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?

Obtain permissions instantly via Rightslink by clicking on the button below:

If you are unable to obtain permissions via Rightslink, please complete and submit this Permissions form. For more information, please visit our Permissions help page.