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FEBS Journal

Cover image for Vol. 281 Issue 2

Special Issue: Enzyme Catalysis and Allostery: A Century of Advances in Molecular Understanding

January 2014

Volume 281, Issue 2

Pages i–iii, 433–645

  1. Front Cover

    1. Top of page
    2. Front Cover
    3. Editorial Information
    4. Special Issue
    5. Author index
    6. Table of Contents
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      Front Cover (page i)

      Article first published online: 16 JAN 2014 | DOI: 10.1111/febs.12630

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      Enzyme Catalysis and Allostery: A Century of Advances in Molecular Understanding

      Detecting enzyme fluctuations in single molecules (by J. R. Moffitt and C. Bustamante, pp. 498–517). The discovery of feedback inhibition (by J. Gerhart, pp. 612–620). Recent citations to classic allostery papers (by A. Cornish-Bowden, pp. 435–463). Energetics of the binding of oxygen to haemoglobin (by M. Brunori, pp. 633–643).

  2. Editorial Information

    1. Top of page
    2. Front Cover
    3. Editorial Information
    4. Special Issue
    5. Author index
    6. Table of Contents
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      Editorial Information (pages ii–iii)

      Article first published online: 16 JAN 2014 | DOI: 10.1111/febs.12630_1

  3. Special Issue

    1. Top of page
    2. Front Cover
    3. Editorial Information
    4. Special Issue
    5. Author index
    6. Table of Contents
    1. You have free access to this content
      Introduction: Enzyme catalysis and allostery: a century of advances in molecular understanding (pages 433–434)

      Athel Cornish-Bowden

      Article first published online: 9 JAN 2014 | DOI: 10.1111/febs.12695

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      The year 2013 marks the 100th anniversary of Michaelis and Menten's paper (published in the forerunner of this journal), and the 50th anniversary of the introduction of allosteric regulation, both papers that continue to have a major impact on biochemistry in the 21st century. In this Special Issue a series of 15 reviews describe the historical context of the classic papers, and current research developed from them.

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      Commemorating the 1913 Michaelis–Menten paper Die Kinetik der Invertinwirkung: three perspectives (pages 435–463)

      Ute Deichmann, Stefan Schuster, Jean-Pierre Mazat and Athel Cornish-Bowden

      Article first published online: 13 DEC 2013 | DOI: 10.1111/febs.12598

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      The standard approach to enzyme kinetics that we know today derives from a classic paper on invertase that Leonor Michaelis, who has a building named in his honour at Humboldt University, and Maud Menten published 100 years ago. Victor Henri was their major predecessor, and made important steps towards the work that we associate with them.

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      Validity of the Michaelis–Menten equation – steady-state or reactant stationary assumption: that is the question (pages 464–472)

      Santiago Schnell

      Article first published online: 18 NOV 2013 | DOI: 10.1111/febs.12564

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      The Michaelis–Menten equation is generally used to estimate kinetic parameters when the steady-state assumption is valid. This review shows that the Michaelis-Menten equation can only lead to accurate estimation of kinetic parameters when it is used under experimental conditions meeting the reactant stationary assumption. Surprisingly the standard experimental practice is unnecessarily restrictive for the validity of the reactant stationary assumption.

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      Time-scale separation – Michaelis and Menten's old idea, still bearing fruit (pages 473–488)

      Jeremy Gunawardena

      Article first published online: 17 OCT 2013 | DOI: 10.1111/febs.12532

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      We review the use of time-scale separation as a method for simplifying the analytical description of complicated molecular systems, an idea introduced in enzyme kinetics by Michaelis and Menten. We outline a “linear framework” which unifies many classical formulas in biochemistry, molecular and systems biology and provides new approaches to analysing non-equilibrium gene regulation and multi-enzyme systems.

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      The power of integrating kinetic isotope effects into the formalism of the Michaelis–Menten equation (pages 489–497)

      Judith P. Klinman

      Article first published online: 2 SEP 2013 | DOI: 10.1111/febs.12477

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      The integration of kinetic isotope effects into the formalism of the Michaelis-Menten equation began in the 1970s and has continued to this day. The impact of isotopic substitution on the primary steady state kinetic parameters (kcat and kcat/Km) goes far beyond a simple ‘doubling’ of the available experimental data, providing a richness of insight into enzyme kinetic and chemical mechanisms.

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      Extracting signal from noise: kinetic mechanisms from a Michaelis–Menten-like expression for enzymatic fluctuations (pages 498–517)

      Jeffrey R. Moffitt and Carlos Bustamante

      Article first published online: 25 OCT 2013 | DOI: 10.1111/febs.12545

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      Enzyme-catalyzed reactions are naturally stochastic, and statistical measures of these fluctuations can place constraints on potential kinetic mechanisms. Here we review several recent results in the field of statistical kinetics with a focus on the randomness parameter. This remarkable statistical measure of fluctuations can limit the complexity and the topology of potential kinetic mechanisms as well as aspects of substrate binding.

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      Single-molecule enzymology à la Michaelis–Menten (pages 518–530)

      Ramon Grima, Nils G. Walter and Santiago Schnell

      Article first published online: 2 JAN 2014 | DOI: 10.1111/febs.12663

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      In this review we discuss both experimental and theoretical techniques which enable single molecule analysis of enzyme catalysed reactions. We pay special attention to the major developments in the field of stochastic enzyme kinetics. We also discuss the differences between stochastic and deterministic rate equations, and how these depend on enzyme molecule numbers and substrate inflow into the reaction compartment.

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      Clusters of reaction rates and concentrations in protein networks such as the phosphotransferase system (pages 531–548)

      Hanna M. Härdin, Antonios Zagaris, Allan R. Willms and Hans V. Westerhoff

      Article first published online: 23 DEC 2013 | DOI: 10.1111/febs.12664

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      We present a phenomenon pertaining to the phosphotransferase reaction network. Following a fast transient, reaction rates cluster in well-separated groups corresponding to distinct subnetworks. During that phase, concentrations of compounds within a subnetwork are approximately at steady state, while those connecting subnetworks to each other vary substantially. We also demonstrate that other, similar protein networks exhibit this same behavior.

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      New types of experimental data shape the use of enzyme kinetics for dynamic network modeling (pages 549–571)

      Katja Tummler, Timo Lubitz, Max Schelker and Edda Klipp

      Article first published online: 4 NOV 2013 | DOI: 10.1111/febs.12525

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      Michaelis and Menten's famous publication on the reaction kinetics of the enzyme invertase introduced the first mathematical description of the dynamics of biological reactions. This review gives an overview on the development of this elegant rate law over the past hundred years, and puts it into context of novel techniques in systems biology, network modeling and large scale experimental studies.

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      Challenges for an enzymatic reaction kinetics database (pages 572–582)

      Ulrike Wittig, Maja Rey, Renate Kania, Meik Bittkowski, Lei Shi, Martin Golebiewski, Andreas Weidemann, Wolfgang Müller and Isabel Rojas

      Article first published online: 25 OCT 2013 | DOI: 10.1111/febs.12562

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      Curating and structuring data for use in databases is time consuming due to the classical publication structure, lack of standard terminology and a precision gap between database entries and scientific English prose. Using the SABIO-RK database as example we describe this curation challenge, as well as tools that aim at helping authors and curators to bridge this gap.

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      Fifty-five years of enzyme classification: advances and difficulties (pages 583–592)

      Andrew G. McDonald and Keith F. Tipton

      Article first published online: 17 OCT 2013 | DOI: 10.1111/febs.12530

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      The list of ‘enzymes classified according to the reactions they catalyse’ has been developed significantly since its first publication by Dixon & Webb in 1958. The number of enzymes has greatly increased and the ExplorEnz online version has enhanced content, search and output facilities. These and some problems associated with the EC classification system are described in this review.

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      How not to do kinetics: examples involving GTPases and guanine nucleotide exchange factors (pages 593–600)

      Roger S. Goody

      Article first published online: 23 OCT 2013 | DOI: 10.1111/febs.12551

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      Errors in the interpretation of kinetic data on GTPases and guanine nucleotide exchange factors have led to false mechanistic conclusions in a number of cases. The examples presented here have led to incorrect conclusions about the mechanism of exchange factors, on small molecules acting as their own exchange factors and on other events concerning Rab GTPases.

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      Michaelis–Menten at 100 and allosterism at 50: driving molecular motors in a hailstorm with noisy ATPase engines and allosteric transmission (pages 601–611)

      Debashish Chowdhury

      Article first published online: 25 NOV 2013 | DOI: 10.1111/febs.12596

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      A molecular motor generates force by ATP hydrolysis at its “engine”. Its “transmission system” is based on allosteric mechanism. Here we celebrate the centenary of the landmark paper of Michaelis and Menten, and the golden jubilee of the classic paper of Monod et al. by highlighting their relevance in explaining the mechanisms of the engine and the transmission system, respectively.

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      From feedback inhibition to allostery: the enduring example of aspartate transcarbamoylase (pages 612–620)

      John Gerhart

      Article first published online: 5 SEP 2013 | DOI: 10.1111/febs.12483

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      I review pre-1965 research on aspartate transcarbamoylase, which as Yates and Pardee discovered in 1956 possesses special properties establishing feedback inhibition by end products in the pyrimidine biosynthetic pathway. Analysis of these properties, including sigmoidal substrate saturation and inhibition or activation by nucleotides binding at other sites, aided the 1965 conceptualization of the allosteric transition by Monod, Wyman, and Changeux.

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      Understanding allosteric and cooperative interactions in enzymes (pages 621–632)

      Athel Cornish-Bowden

      Article first published online: 2 SEP 2013 | DOI: 10.1111/febs.12469

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      The paper by Monod, Changeux and Jacob that introduced biochemists to the idea of allosteric feedback inhibition is now 50 years old, and the papers on classic models for enzyme cooperativity that followed it are almost as old. All of these papers continue to be heavily and increasingly cited today.

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      Variations on the theme: allosteric control in hemoglobin (pages 633–643)

      Maurizio Brunori

      Article first published online: 28 NOV 2013 | DOI: 10.1111/febs.12586

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      Selection among pre-existing conformational states of a protein is the basic concept of allostery. Dramatic variations in allosteric control observed for different hemoglobins, respond to peculiar physiological requirements. The efficacy of this elegant theory in accounting for functional cooperativity and the conformational selection mechanism conforming to the basic concept of Darwinian evolution may account for the popularity of the model.

  4. Author index

    1. Top of page
    2. Front Cover
    3. Editorial Information
    4. Special Issue
    5. Author index
    6. Table of Contents
    1. You have free access to this content
      Author index (page 644)

      Article first published online: 16 JAN 2014 | DOI: 10.1111/febs.12631

  5. Table of Contents

    1. Top of page
    2. Front Cover
    3. Editorial Information
    4. Special Issue
    5. Author index
    6. Table of Contents
    1. You have free access to this content
      Table of Contents (page 645)

      Article first published online: 16 JAN 2014 | DOI: 10.1111/febs.12632

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