ENZO: A Web Tool for Derivation and Evaluation of Kinetic Models of Enzyme Catalyzed Reactions

We describe a web tool ENZO (Enzyme Kinetics), a graphical interface for building kinetic models of enzyme catalyzed reactions. ENZO automatically generates the corresponding differential equations from a stipulated enzyme reaction scheme. These differential equations are processed by a numerical solver and a regression algorithm which fits the coefficients of differential equations to experimentally observed time course curves. ENZO allows rapid evaluation of rival reaction schemes and can be used for routine tests in enzyme kinetics. It is freely available as a web tool, at http://enzo.cmm.ki.si.

[1]  R. Duggleby,et al.  Analysis of enzyme progress curves by nonlinear regression. , 1995, Methods in enzymology.

[2]  O. Vasiljeva,et al.  Autocatalytic processing of procathepsin B is triggered by proenzyme activity , 2009, The FEBS journal.

[3]  D. Burk,et al.  The Determination of Enzyme Dissociation Constants , 1934 .

[4]  K Yamaoka,et al.  A nonlinear least squares program based on differential equations, MULTI (RUNGE), for microcomputers. , 1983, Journal of pharmacobio-dynamics.

[5]  K. Courtney,et al.  A new and rapid colorimetric determination of acetylcholinesterase activity. , 1961, Biochemical pharmacology.

[6]  Kenneth A Johnson,et al.  Fitting enzyme kinetic data with KinTek Global Kinetic Explorer. , 2009, Methods in enzymology.

[7]  Jure Stojan,et al.  Analysis of Progress Curves in an Acetylcholinesterase Reaction: A Numerical Integration Treatment , 1997, J. Chem. Inf. Comput. Sci..

[8]  J. Sussman,et al.  The X-ray structure of a transition state analog complex reveals the molecular origins of the catalytic power and substrate specificity of acetylcholinesterase. , 1996 .

[9]  P. Kuzmič,et al.  DynaFit--a software package for enzymology. , 2009, Methods in enzymology.

[10]  M. Froment,et al.  High activity of human butyrylcholinesterase at low pH in the presence of excess butyrylthiocholine. , 2003, European journal of biochemistry.

[11]  C. Pace,et al.  How to measure and predict the molar absorption coefficient of a protein , 1995, Protein science : a publication of the Protein Society.

[12]  J. Colletier,et al.  Inhibition of Drosophila melanogaster acetylcholinesterase by high concentrations of substrate. , 2004, European journal of biochemistry.

[13]  V. Turk,et al.  Autocatalytic processing of recombinant human procathepsin B is a bimolecular process , 1999, FEBS letters.

[14]  Jure Stojan,et al.  Structural insights into substrate traffic and inhibition in acetylcholinesterase , 2006, The EMBO journal.

[15]  이기용 백미의 acetylcholinesterase 저해 활성 성분 , 2001 .