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Starch- and glycogen-debranching and branching enzymes: Prediction of structural features of the catalytic (β/α)8-barrel domain and evolutionary relationship to other amylolytic enzymes

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Abstract

Sequence alignment and structure prediction are used to locate catalytic α-amylase-type (β/α)8-barrel domains and the positions of their β-strands and α-helices in isoamylase, pullulanase, neopullulanase, α-amylase-pullulanase, dextran glucosidase, branching enzyme, and glycogen branching enzymes—all enzymes involved in hydrolysis or synthesis of α-1,6-glucosidic linkages in starch and related polysaccharides. This has allowed identification of the transferase active site of the glycogen debranching enzyme and the locations of β ⇑ α loops making up the active sites of all enzymes studied. Activity and specificity of the enzymes are discussed in terms of conserved amino acid residues and loop variations. An evolutionary distance tree of 47 amylolytic and related enzymes is built on 37 residues representing the four best conserved β-strands of the barrel. It exhibits clusters of enzymes close in specificity, with the branching and glycogen debranching enzymes being the most distantly related.

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  1. Michael R. Sierks

    Present address: Department of Chemical and Biochemical Engineering, University of Maryland Baltimore County, 21228, Baltimore, Maryland

Authors and Affiliations

  1. Department of Chemistry, Carlsberg Laboratory, Gamle Carlsberg Vej 10, DK-2500, Copenhagen Valby, Denmark

    Hans M. Jespersen, Michael R. Sierks & Birte Svensson

  2. Department of Chemistry, University of Manitoba, R3T 2N2, Winnipeg, Manitoba, Canada

    E. Ann MacGregor

  3. Centre de Recherches sur les Macromolécules Végétales, C. N. R. S., B.P., 53X-38041, Grenoble cedex, France

    Bernard Henrissat

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  1. Hans M. Jespersen
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  2. E. Ann MacGregor
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Jespersen, H.M., Ann MacGregor, E., Henrissat, B. et al. Starch- and glycogen-debranching and branching enzymes: Prediction of structural features of the catalytic (β/α)8-barrel domain and evolutionary relationship to other amylolytic enzymes. J Protein Chem 12, 791–805 (1993). https://doi.org/10.1007/BF01024938

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