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Volume 63, Issue 6


An enzyme family reunion — similarities, differences and eccentricities in actions on α-glucans

Eun-Seong Seo
  • Enzyme and Protein Chemistry, Department of Systems Biology, Technical University of Denmark, Søltofts Plads, Bldg. 224, DK-2800, Kgs. Lyngby, Denmark
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/ Camilla Christiansen
  • Enzyme and Protein Chemistry, Department of Systems Biology, Technical University of Denmark, Søltofts Plads, Bldg. 224, DK-2800, Kgs. Lyngby, Denmark
  • Plant Biology Laboratory, Faculty of Life Sciences, University of Copenhagen, DK-1871, Frederiksberg, Denmark
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/ Maher Abou Hachem
  • Enzyme and Protein Chemistry, Department of Systems Biology, Technical University of Denmark, Søltofts Plads, Bldg. 224, DK-2800, Kgs. Lyngby, Denmark
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/ Morten Nielsen
  • Enzyme and Protein Chemistry, Department of Systems Biology, Technical University of Denmark, Søltofts Plads, Bldg. 224, DK-2800, Kgs. Lyngby, Denmark
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/ Kenji Fukuda
  • Enzyme and Protein Chemistry, Department of Systems Biology, Technical University of Denmark, Søltofts Plads, Bldg. 224, DK-2800, Kgs. Lyngby, Denmark
  • Carlsberg Laboratory, Gamle Carlsberg Vej 10, DK-2500, Valby, Denmark
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/ Sophie Bozonnet
  • Enzyme and Protein Chemistry, Department of Systems Biology, Technical University of Denmark, Søltofts Plads, Bldg. 224, DK-2800, Kgs. Lyngby, Denmark
  • Carlsberg Laboratory, Gamle Carlsberg Vej 10, DK-2500, Valby, Denmark
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/ Andreas Blennow / Nushin Aghajari
  • Laboratorie de BioCristallographie, Institut de Biologie et Chimie des Protéines, UMR 5086-CNRS/Université de Lyon, IFR128 “BioSciences Gerland Lyon-Sud”, F-69367, Lyon, France
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/ Richard Haser
  • Laboratorie de BioCristallographie, Institut de Biologie et Chimie des Protéines, UMR 5086-CNRS/Université de Lyon, IFR128 “BioSciences Gerland Lyon-Sud”, F-69367, Lyon, France
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/ Birte Svensson
  • Enzyme and Protein Chemistry, Department of Systems Biology, Technical University of Denmark, Søltofts Plads, Bldg. 224, DK-2800, Kgs. Lyngby, Denmark
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Published Online: 2008-12-04 | DOI: https://doi.org/10.2478/s11756-008-0164-2


α-Glucans in general, including starch, glycogen and their derived oligosaccharides are processed by a host of more or less closely related enzymes that represent wide diversity in structure, mechanism, specificity and biological role. Sophisticated three-dimensional structures continue to emerge hand-in-hand with the gaining of novel insight in modes of action. We are witnessing the “test of time” blending with remaining questions and new relationships for these enzymes. Information from both within and outside of ALAMY_3 Symposium will provide examples on what the family contains and outline some future directions. In 2007 a quantum leap crowned the structural biology by the glucansucrase crystal structure. This initiates the disclosure of the mystery on the organisation of the multidomain structure and the “robotics mechanism” of this group of enzymes. The central issue on architecture and domain interplay in multidomain enzymes is also relevant in connection with the recent focus on carbohydrate-binding domains as well as on surface binding sites and their long underrated potential. Other questions include, how different or similar are glycoside hydrolase families 13 and 31 and is the lid finally lifted off the disguise of the starch lyase, also belonging to family 31? Is family 57 holding back secret specificities? Will the different families be sporting new “eccentric” functions, are there new families out there, and why are crystal structures of “simple” enzymes still missing? Indeed new understanding and discovery of biological roles continuously emphasize value of the collections of enzyme models, sequences, and evolutionary trees which will also be enabling advancement in design for useful and novel applications.

Keywords: glycoside hydrolase families 13, 31, 57, 70, and 77; crystal structures; substrate specificities; surface binding sites; degree of multiple attack; starch granules; calcium ions; starch-binding domains; barley α-amylase

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About the article

Published Online: 2008-12-04

Published in Print: 2008-12-01

Citation Information: Biologia, Volume 63, Issue 6, Pages 967–979, ISSN (Online) 1336-9563, ISSN (Print) 0006-3088, DOI: https://doi.org/10.2478/s11756-008-0164-2.

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© 2008 Slovak Academy of Sciences. This work is licensed under the Creative Commons Attribution-NonCommercial-NoDerivatives 3.0 License. BY-NC-ND 3.0

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