ENZO: A web tool for derivation and evaluation of kinetic models of enzyme catalyzed reactions

PLoS ONE

Volumn 6, Issue 7, 2011, Pages

  Bevc, Staš ^a,b   Konc, Janez ^a   Stojan, Jure ^c   Hodošček, Milan ^a   Penca, Matej ^a   Praprotnik, Matej ^a   Janežič, Dušanka ^a,b  

^a NATIONAL INSTITUTE OF CHEMISTRY   (Slovenia)

^b UNIVERSITY OF PRIMORSKA   (Slovenia)

^c UNIVERSITY OF LJUBLJANA   (Slovenia)

Author keywords

[No Author keywords available]

Indexed keywords

ALGORITHM; ARTICLE; CATALYSIS; COMPUTER INTERFACE; COMPUTER MODEL; COMPUTER PROGRAM; DERIVATIZATION; ENZYME ANALYSIS; ENZYME KINETICS; ENZYME MECHANISM; INTERNET; MATHEMATICAL ANALYSIS; MATHEMATICAL COMPUTING; REGRESSION ANALYSIS; ANIMAL; BIOCATALYSIS; BIOLOGICAL MODEL; DRUG EFFECT; ENZYME ACTIVATION; ENZYME ACTIVE SITE; ENZYME SPECIFICITY; KINETICS; METABOLISM; STANDARD; TITRIMETRY; TORPEDO;

ACETYLCHOLINESTERASE; BUTYRYLTHIOCHOLINE; CATHEPSIN B; ENZYME;

ACETYLCHOLINESTERASE; ALGORITHMS; ANIMALS; BIOCATALYSIS; BUTYRYLTHIOCHOLINE; CATALYTIC DOMAIN; CATHEPSIN B; ENZYME ACTIVATION; ENZYMES; INTERNET; KINETICS; MODELS, BIOLOGICAL; REFERENCE STANDARDS; SUBSTRATE SPECIFICITY; TITRIMETRY; TORPEDO;

EID: 79960465396     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0022265     Document Type: Article

References (17)

1. Michaelis L, Menten ML, (1913) Kinetik der Invertinwirkung. Biochem Z 49: 333-369.
2. Rosenberry TL, (1975) Acetylcholinesterase. Adv Enzymol 43: 103-218.
3. Lineweaver H, Burk D, (1934) The determination of enzyme dissociation constants. J Am Chem Soc 56: 658-666.
4. Duggleby RG, (1995) Analysis of enzyme progress curves by non-linear regression. Methods Enzymol 249: 61-90.
5. Kuzmic P, (2009) DynaFit-a software package for enzymology. Methods Enzymol 467: 247-280.
6. Johnson KA, (2009) Fitting enzyme kinetic data with KinTek Global Kinetic Explorer. Methods Enzymol 467: 601-626.
7. Yamaoka K, Nakagawa T, (1983) A nonlinear least squares program based on differential equations, MULTI (RUNGE), for microcomputers. J Pharmacobiodyn 6: 595-606.
8. Stojan J, (1997) Analysis of progress curves in an acetylcholinesterase reaction: a numerical integration treatment. J Chem Inf Comput Sci 37: 1025-1027.
9. Harel M, Quinn DM, Nair HK, Silman I, Sussman JL, (1996) The X-ray structure of a transition state analog complex reveals the molecular origins of the catalytic power and substrate specificity of acetylcholinesterase. J Am Chem Soc 118: 2340-2346.
10. Ellman GL, Courtney KD, Andres V Jr, Feather-Stone RM, (1961) A new and rapid colorimetric determination of acetylcholinesterase activity. Biochem Pharmacol 7: 88-95.
11. Rozman J, Stojan J, Kuhelj R, Turk V, Turk B, (1999) Autocatalytic processing of recombinant human procathepsin B is a bimolecular process. FEBS Lett 459: 358-362.
12. Pungercar JR, Caglic D, Sajid M, Dolinar M, Vasiljeva O, Pozgan U, Turk D, Bogyo M, Turk V, Turk B, (2009) Autocatalytic processing of procathepsin B is triggered by proenzyme activity. FEBS Lett 276: 660-668.
13. Pace CN, Vajdos F, Lee L, Grimsley G, Grey T, (1995) How to measure and predict the molar absorption coefficient of a protein. Prot Sci 4: 2411-2423.
14. Colletier JP, Fournier D, Greenblatt HM, Stojan J, Sussman JL, Zaccai G, Silman I, Weik M, (2006) Structural insights into substrate traffic and inhibition in acetylcholinesterase. EMBO J 25: 2746-2756.
15. Stojan J, Brochier L, Alies C, Colletier JP, Fournier D, (2004) Inhibition of Drosophila melanogaster acetylcholinesterase by high concentrations of substrate. Eur J Biochem 271: 1364-1371.
16. Masson P, Nachon F, Bartels CF, Froment MT, Ribes F, Mathews C, Lockridge O, (2003) High activity of human butyrylcholinesterase at low pH in the presence of excess butyrylthiocholine. Eur J Biochem 270: 315-324.
17. Pavlič MR, (1973) On the nature of the acceleration of the methanesulfonylation of acetylcholinesterase by tetraethylammonium. Biochim Biophys Acta 327: 393-397.