© 2014

Carbonic Anhydrase: Mechanism, Regulation, Links to Disease, and Industrial Applications

  • Susan C. Frost
  • Robert McKenna


  • Up to date reference for researchers and students in the carbonic anhydrase family

  • Contributions from internationally recognized investigators at the forefront of the carbonic anhydrase field

  • Mix of topics to reach audiences with interests across phylums


Part of the Subcellular Biochemistry book series (SCBI, volume 75)

Table of contents

  1. Front Matter
    Pages i-ix
  2. Introduction

    1. Front Matter
      Pages 1-1
    2. Robert McKenna, Susan C. Frost
      Pages 3-5
  3. Carbonic Anhydrases: Ancient but Relevant

    1. Front Matter
      Pages 7-7
    2. Christopher D. Boone, Melissa Pinard, Rob McKenna, David Silverman
      Pages 31-52
    3. R. Siva Sai Kumar, James G. Ferry
      Pages 77-87
    4. Matthew S. Kimber
      Pages 89-103
    5. Holger M. Becker, Michael Klier, Joachim W. Deitmer
      Pages 105-134
    6. Ashok Aspatwar, Martti E. E. Tolvanen, Csaba Ortutay, Seppo Parkkila
      Pages 135-156
    7. Martin Benej, Silvia Pastorekova, Jaromir Pastorek
      Pages 199-219
    8. Narges K. Tafreshi, Mark C. Lloyd, Marilyn M. Bui, Robert J. Gillies, David L. Morse
      Pages 221-254
    9. Robert McKenna, Claudiu T. Supuran
      Pages 291-323
    10. Sally-Ann Poulsen, Rohan A. Davis
      Pages 325-347
    11. Andrea Scozzafava, Claudiu T. Supuran
      Pages 349-359

About this book



The study of carbonic anhydrase has spanned multiple generations of scientists.  Carbonic anhydrase was first discovered in 1932 by Meldrum and Roughton.  Inhibition by sulfanilamide was shown in 1940 by Mann and Keilin.  Even Hans Krebs contributed to early studies with a paper in 1948 showing the relationship of 25 different sulfonamides to CA inhibition. It was he who pointed out the importance of both the charged and uncharged character of these compounds for physiological experiments.

            The field of study that focuses on carbonic anhydrase (CA) has exploded in recent years with the identification of new families and isoforms.  The CAs are metalloenzymes which are comprised of 5 structurally different families: the alpha, beta, gamma, and delta, and epsilon classes.  The alpha class is found primarily in animals with several isoforms  associated with human disease.  The beta CAs are expressed primarily in plants and are the most divergent.  The gamma CAs are the most ancient. These are structurally related to the beta CAs, but have a mechanism more similar to the alpha CAs.   The delta CAs are found in marine algae and diflagellates.  The epsilon class is found in prokaryotes in which it is part of the carboxysome shell perhaps supplying RuBisCO with CO2 for carbon fixation.  

            With the excitement surrounding the discovery of disease-related CAs, scientists have redoubled their efforts to better understand structure-function relationships, to design high affinity, isotype-specific inhibitors, and to delineate signaling systems that play regulatory roles over expression and activity.  We have designed the book to cover basic information of mechanism, structure, and function of the CA families.  The authors included in this book bring to light the newest data with regard to the role of CA in physiology and pathology, across phylums, and in unique environmental niches.


carbonic anhydrase industrial applications mechanism pathology structure

Editors and affiliations

  • Susan C. Frost
    • 1
  • Robert McKenna
    • 2
  1. 1.Department of Biochemistry and Molecular BiologyUniversity of FloridaGainesvilleUSA
  2. 2.Department of Biochemistry and Molecular BiologyUniversity of FloridaGainesvilleUSA

Bibliographic information

  • Book Title Carbonic Anhydrase: Mechanism, Regulation, Links to Disease, and Industrial Applications
  • Editors Susan C. Frost
    Robert McKenna
  • Series Title Subcellular Biochemistry
  • Series Abbreviated Title Subcellular Biochemistry
  • DOI
  • Copyright Information Springer Science+Business Media Dordrecht 2014
  • Publisher Name Springer, Dordrecht
  • eBook Packages Biomedical and Life Sciences Biomedical and Life Sciences (R0)
  • Hardcover ISBN 978-94-007-7358-5
  • Softcover ISBN 978-94-024-0250-6
  • eBook ISBN 978-94-007-7359-2
  • Series ISSN 0306-0225
  • Edition Number 1
  • Number of Pages IX, 430
  • Number of Illustrations 38 b/w illustrations, 37 illustrations in colour
  • Topics Gene Function
    Protein Science
    Biomedicine, general
  • Buy this book on publisher's site
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