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Computer‐assisted simulations of phosphofructokinase‐1 kinetics using simplified velocity equations
Author(s) -
Roy Harry,
Diwan Joyce,
D. Segel Leigh,
Segel Irwin H.
Publication year - 2001
Publication title -
biochemistry and molecular biology education
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.34
H-Index - 39
eISSN - 1539-3429
pISSN - 1470-8175
DOI - 10.1111/j.1539-3429.2001.tb00055.x
Subject(s) - phosphofructokinase , allosteric regulation , substrate (aquarium) , kinetics , kinetic energy , chemistry , symmetry (geometry) , thermodynamics , enzyme , computer science , physics , mathematical physics , biochemistry , mathematics , glycolysis , classical mechanics , biology , geometry , ecology
Equations useful for simulating the kinetic behavior of phosphofructokinase are presented. The equations, which are based on the concerted transition (symmetry) model for allosteric enzymes, account for substrate inhibition by MgATP, cooperative binding by F‐6‐P, activation by F‐2, 6‐P 2 , and deinhibition by AMP. Velocity calculations can be performed using either a spreadsheet program (e.g., MS Excel) or a web‐based program (e.g., Authorware). Both approaches are illustrated. © 2001 IUBMB. Published by Elsevier Science Ltd. All rights reserved.