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Structure of Transglutaminases: Unique Features Serve Diverse Functions

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Transglutaminases

Abstract

Understanding the diverse functions and pathologies of transglutaminases requires detailed analysis and interpretation of their structures. This chapter is an attempt to describe in detail how these enzymes are folded into functional domains, what type of catalytic and scaffolding functions have been gained as the result of their evolution, how their regulation is achieved through unique Ca2+ and purine nucleotide binding sites, redox changes and specific proteolytic actions, and by influencing the equilibrium of open-close configurations. The importance of structural motifs in pathologies is underlined by the celiac epitopes of transglutaminase 2, responsible for autoimmune reactions.

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Authors and Affiliations

  1. Department of Biochemistry and Molecular Biology, University of Debrecen, Debrecen, Hungary

    Máté Á. Demény & László Fésüs

  2. Department of Pediatrics, University of Debrecen, Debrecen, Hungary

    Ilma Korponay-Szabó

Authors
  1. Máté Á. Demény
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  2. Ilma Korponay-Szabó
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  3. László Fésüs
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Corresponding author

Correspondence to László Fésüs .

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Editors and Affiliations

  1. Grad Sch of Pharmaceutical Sciences, Nagoya University, Nagoya, Aichi, Japan

    Kiyotaka Hitomi

  2. Micro-Signaling Regulation Technol. Unit, RIKEN Center for Life Sci. Technologies, Wako, Saitama, Japan

    Soichi Kojima

  3. Dept. Biochemistry and Molecular Biology, University of Debrecen, Debrecen, Hungary

    Laszlo Fesus

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Demény, M.Á., Korponay-Szabó, I., Fésüs, L. (2015). Structure of Transglutaminases: Unique Features Serve Diverse Functions. In: Hitomi, K., Kojima, S., Fesus, L. (eds) Transglutaminases. Springer, Tokyo. https://doi.org/10.1007/978-4-431-55825-5_1

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