The average enzyme principle. Issue 17 (23rd July 2013)

• Record Type: Journal Article
• Authors: Reznik, Ed; Chaudhary, Osman; Segrè, Daniel
• Is Part Of: FEBS letters. Volume 587:Issue 17(2013)
• Page Start: 2891
• Page End: 2894
• Publication Date: 2013-07-23
• Subjects: Enzyme regulation -- Michaelis–Menten -- Metabolic network -- Enzyme kinetics -- Systems biology; Biochemistry -- Periodicals; Biophysics -- Periodicals; Molecular biology -- Periodicals; Biochimie -- Périodiques; Biochemistry; Biophysics; Molecular biology; Periodicals; 572.05
• DOI: 10.1016/j.febslet.2013.07.032
• Languages: English
• ISSNs: 0014-5793

Abstract

Abstract : The Michaelis–Menten equation for an irreversible enzymatic reaction depends linearly on the enzyme concentration. Even if the enzyme concentration changes in time, this linearity implies that the amount of substrate depleted during a given time interval depends only on the average enzyme concentration. Here, we use a time re‐scaling approach to generalize this result to a broad category of multi‐reaction systems, whose constituent enzymes have the same dependence on time, e.g . they belong to the same regulon. This "average enzyme principle" provides a natural methodology for jointly studying metabolism and its regulation. Abstract : In Michaelis–Menten kinetics with time‐dependent enzyme, metabolite concentrations are determined by the average enzyme over a given time interval. This "average enzyme principle" holds also for co‐regulated multi‐reaction pathways. This approach offers new avenues for integrating metabolism and regulation.