...Celebrating the 100th Anniversary of Michaelis-Menten Kinetics

6th Beilstein ESCEC Symposium 2013

16 – 20 September 2013

Hotel Jagdschloss Niederwald, Rüdesheim, Germany

Scientific Program: Carsten Kettner and Martin G. Hicks


Proceedings of this Beilstein ESCEC Symposium.


In a small research laboratory at one of Berlin’s municipal hospitals (“Am Urban”) two researchers’ very careful work laid the foundation for enzyme kinetics as a systematic field which formed the basis of modern enzymology:

In 1913, Leonor Michaelis and his coworker Maud L. Menten published a paper on the concept of an affinity constant, by studying the relationship between the rate of formation of products in dependence of the concentrations of an enzyme (invertase) and its substrate at constant and controlled pH (Michaelis, M. and Menten M.L., 1913 [1]). The best-known outcome of this work was the Michaelis–Menten equation, together with the Michaelis constant. This term was coined by George Briggs and J. B. S. Haldane in 1925 (Briggs, G.E. and Haldane, J.B.S., 1925[2]), whose work on enzyme kinetics led to the steady-state approximation assuming a negligible rate of the change of the enzyme-substrate complex compared to the rates of changes in the concentrations of both the substrate and the product. Since then enzymes have been routinely characterized by applying Michaelis and Menten’s approach and evaluation of enzymatic activities. Over the last hundred years this has allowed mechanistic models to be developed and has led to the discovery of a tremendous number of new metabolic pathways in cells and tissues.

Today, the multi-disciplinary approach of modern enzymology, combining a variety of modern experimental and analytical techniques, leads to the generation of huge amounts of data on enzyme structures and activities that are published in journals and databases. However, the outcome of accessing these comprehensive data resources often fails to meet expectations since the functional enzyme data have often been collected under quite disparate experimental conditions and the details of the assay conditions used are often incompletely described. 

[1] Michaelis, L. and Menten, M.L. (1913) Die Kinetik der Invertinwirkung. Biochem. Z. 49:333-369. Engl. Translation: Goody, R.S. and Johnson, K.A. (2011) The Kinetics of Invertase Action. Biochemistry 50:8264-8269.

[2] Briggs, G.E. and Haldane, J.B.S. (1925) A note on the kinetics of enzyme action. Biochem. J. 19:338-339.

Because these issues cause significant problems in the interpretation and reproduction of published data, the STRENDA (Standards for Reporting Enzymology Data) Commission was set up almost ten years ago to address the improvement of the reporting quality of functional enzyme data in order to support the community with the efficient application of enzyme kinetics in the in vivo, in vitro and in silico investigation of biological systems.

The STRENDA Guidelines are the result of extensive consulting sessions with the scientific community and are recommended today by more than 30 biochemistry journals.

The analysis of Michaelis-Menten kinetics 100 years ago shares a number of other prominent anniversaries, such as the discovery of the DNA structure by Watson and Crick (1953) [3], the concept of allosteric interactions introduced by Monod, Changeux and Jacob (1963) [4] and the start of metabolic control analysis by Kacser and Burns (1973) [5].

This 6th Symposium on Experimental Standard Conditions of Enzyme Characterizations provides the platform not only to commemorate these scientific landmarks but also to bring together experts from all fields of modern enzymology and metabolic network investigation to present and discuss new results, approaches and methodologies in enzymology.

[3] Watson J.D. and Crick F.H.C. (1953) A Structure for Deoxyribose Nucleic Acid. Nature 171(4356):737–738.

[4] Monod, J., Changeux, J.-P., Jacob, F. (1963) Allosteric proteins and cellular control systems. J. Mol. Biol. 6:306–329.

[5] Kacser, H. and Burns, J.A. (1973) The control of flux. Symposia of the Society for Experimental Biology 27:65–104.

Aspects covered by this symposium

  • Biochemistry and molecular biology coming of age: 100 years of Michaelis-Menten kinetics, 60 years of the structure of DNA, and 40 years of Metabolic Control Analysis
  • Systems biology and systems medicine: the new kids on the block
  • Sequence, structure, kinetics, control and Regulation
  • Physiological meaning of enzyme kinetics
  • Network kinetics versus enzyme kinetics
  • Enzymes in metabolic collaboration
  • Pitfalls in data reproduction
  • The end to the tower of Babel: making biochemists peak a lingua franca

Scientific Program

100 Years of Michaelis-Menten Kinetics
Athel Cornish-Bowden, CNRS-BIP, Marseille, France

Understanding Mechanisms of Enzyme Cooperativity: Importance of not being at Equilibrium
María Luz Cárdenas, CNRS-BIP, Marseille, France

Mapping the Biochemistry of the Whole
Hans V. Westerhoff, Free University of Amsterdam, The Netherlands

How not to Do Kinetics: Examples from the GTPase Field
Roger Goody, MPI for Molecular Physiology, Dortmund, Germany

Variety is the Price of Life. Diversity in the Mechanisms of Fosfomycin Resistance Proteins in Pathogenic Microorganisms
Richard N. Armstrong, Vanderbilt University, Nashville, TN, USA

Challenges in Reporting of Date in (applied) Biocatalysis
Munishwar N. Gupta, Indian Institute of Technology, Delhi, India

Enzyme Classification, Annotation and Metabolism
Dietmar Schomburg, TU Braunschweig, Germany

From Mechanism to Medicine - Controlling Sulfuryl-transfer in vivo
Thomas S. Leyh, Albert Einstein College of Medicine, Bronx, NY, USA

Enzymes in Protein Interaction Networks
Peter Uetz, Virginia Commonwealth University, Richmond, VA, USA

A Global Context for Prediction of Functional Trends in Enzyme Superfamilies
Patricia Babbit, University of California, San Francisco, CA, USA

Specificity and Promiscuity in a Superfamily of Phosphatases
Karen N. Allen, University of Boston, MA, USA

Enzyme Kinetics in Systems Biology with NMR Spectroscopy
Johann M. Rohwer, University of Stellenbosch, South Africa

Evolution of the Tryptophan Synthase Complex
Reinhard Sterner, University of Regensburg, Germany

Structure, Function and Evolution of Blood Group Glycosyl-transferases
Monica Palcic, Carlsberg Laboratory, Copenhagen, Denmark

Structure and Function of Translesion DNA Polymerases and Interactions with Damaged DNA
F. Peter Guengerich, Vanderbilt University, Nashville, TN, USA

The Role of Fe, Co and Ni in the Bacterial Life on CO and CO2
Holger Dobbek, Humbold University, Berlin, Germany

PhnJ - A Novel Radical SAM Enzyme from the C-P Lyase Complex
Frank M. Raushel, Texas A&M University, College Station, TX, USA

Reactions of Cg10062, a cis-3-Chloroacrylic Acid Dehalogenase Homologue, with Acetylene and Allene Substrates: Implications for Mechanism and Function
Christian P. Whitman, The University of Texas at Austin, TX, USA

Intracellular pH, a Metabolic Signal?
Gertien J. Smits, University of Amsterdam, The Netherlands

A Generic Rate Equation for Catalysed, Tempalte-directed Polymerisation and its Use in Computation Systems Biology
Jan-Hendrik S. Hofmeyr, University of Stellenbosch, South Africa

Modelling of Complex Enzyme Kinetics: the MultifunctionalTrypanothione Synthethase of Trypanosoma brucei
Barbara M. Bakker, University Medical Center Groningen, The Netherlands

The Catalytic Reaction Mechanisms of Drosophilid Alcohol Dehydrogenases
Jan-Olof Winberg, University of Tromsö, Norway

Regio- and Stereoselective ω-transaminas/MAO-N Cascade Processes for the Synthesis of Chiral Amines
Elaine O'Reilly, The University of Manchester, UK

Oral Poster Presentations

Ulrike Wittig / Heidelberg Institute for THeoretical Studies (HITS), Germany

Karen van Eunen / University of Groningen, The Netherlands

Sandra Schlee / University of Regensburg, Germany

Hartmut Schlüter / University Medical Center Hamburg-Eppendorf, Germany

Alejandro E. Leroux / University of Heidelberg, Germany

Isaac Olusanjo Adewale / Obafemi Awolowo University, Ile-Ife, Nigeria

Ludwig Krabben / Free University Berlin, Germany