Literature DB >> 1954231

Experimental designs for estimating the parameters of the Michaelis-Menten equation from progress curves of enzyme-catalyzed reactions.

R G Duggleby1, R B Clarke.   

Abstract

When the progress curve for an enzyme catalysed reaction follows the integrated Michaelis-Menten equation, the maximum velocity and Michaelis constant can be determined from a single such curve. In this paper, an experimental design for collecting the data is proposed which is close to optimum in the sense that it produces the smallest standard error in the estimate of the Michaelis constant. This design involves choosing an initial substrate concentration which is approx. two or three times the value of the Michaelis constant.

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Year:  1991        PMID: 1954231     DOI: 10.1016/0167-4838(91)90007-m

Source DB:  PubMed          Journal:  Biochim Biophys Acta        ISSN: 0006-3002


  2 in total

1.  Beyond the Michaelis-Menten equation: Accurate and efficient estimation of enzyme kinetic parameters.

Authors:  Boseung Choi; Grzegorz A Rempala; Jae Kyoung Kim
Journal:  Sci Rep       Date:  2017-12-05       Impact factor: 4.379

2.  The Removal of Time-Concentration Data Points from Progress Curves Improves the Determination of Km: The Example of Paraoxonase 1.

Authors:  Boštjan Petrič; Marko Goličnik; Aljoša Bavec
Journal:  Molecules       Date:  2022-02-15       Impact factor: 4.411

  2 in total

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