The carbohydrate-binding module family 20-diversity, structure, and function

Camilla Christiansen, Maher Abou Hachem, S. Janecek, A. Vikso-Nielsen, A. Blennow, Birte Svensson

    Research output: Contribution to journalJournal articleResearchpeer-review

    Abstract

    Starch-active enzymes often possess starch-binding domains (SBDs) mediating attachment to starch granules and other high molecular weight substrates. SBDs are divided into nine carbohydrate-binding module (CBM) families, and CBM20 is the earliest-assigned and best characterized family. High diversity characterizes CBM20s, which occur in starch-active glycoside hydrolase families 13, 14, 15, and 77, and enzymes involved in starch or glycogen metabolism, exemplified by the starch-phosphorylating enzyme glucan, water dikinase 3 from Arabidopsis thaliana and the mammalian glycogen phosphatases, laforins. The clear evolutionary relatedness of CBM20s to CBM21s, CBM48s and CBM53s suggests a common clan hosting most of the known SBDs. This review surveys the diversity within the CBM20 family, and makes an evolutionary comparison with CBM21s, CBM48s and CBM53s, discussing intrafamily and interfamily relationships. Data on binding to and enzymatic activity towards soluble ligands and starch granules are summarized for wild-type, mutant and chimeric fusion proteins involving CBM20s. Noticeably, whereas CBM20s in amylolytic enzymes confer moderate binding affinities, with dissociation constants in the low micromolar range for the starch mimic beta-cyclodextrin, recent findings indicate that CBM20s in regulatory enzymes have weaker, low millimolar affinities, presumably facilitating dynamic regulation. Structures of CBM20s, including the first example of a full-length glucoamylase featuring both the catalytic domain and the SBD, are summarized, and distinct architectural and functional features of the two SBDs and roles of pivotal amino acids in binding are described. Finally, some applications of SBDs as affinity or immobilization tags and, recently, in biofuel and in planta bioengineering are presented.
    Original languageEnglish
    JournalF E B S Journal
    Volume276
    Issue number18
    Pages (from-to)5006-5029
    ISSN1742-464X
    DOIs
    Publication statusPublished - 2009

    Keywords

    • starch-binding domain
    • alpha-glucan
    • water dikinase
    • molecular recognition
    • starch metabolism
    • amylolytic enzymes
    • glucan

    Cite this

    Christiansen, Camilla ; Abou Hachem, Maher ; Janecek, S. ; Vikso-Nielsen, A. ; Blennow, A. ; Svensson, Birte. / The carbohydrate-binding module family 20-diversity, structure, and function. In: F E B S Journal. 2009 ; Vol. 276, No. 18. pp. 5006-5029.
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    abstract = "Starch-active enzymes often possess starch-binding domains (SBDs) mediating attachment to starch granules and other high molecular weight substrates. SBDs are divided into nine carbohydrate-binding module (CBM) families, and CBM20 is the earliest-assigned and best characterized family. High diversity characterizes CBM20s, which occur in starch-active glycoside hydrolase families 13, 14, 15, and 77, and enzymes involved in starch or glycogen metabolism, exemplified by the starch-phosphorylating enzyme glucan, water dikinase 3 from Arabidopsis thaliana and the mammalian glycogen phosphatases, laforins. The clear evolutionary relatedness of CBM20s to CBM21s, CBM48s and CBM53s suggests a common clan hosting most of the known SBDs. This review surveys the diversity within the CBM20 family, and makes an evolutionary comparison with CBM21s, CBM48s and CBM53s, discussing intrafamily and interfamily relationships. Data on binding to and enzymatic activity towards soluble ligands and starch granules are summarized for wild-type, mutant and chimeric fusion proteins involving CBM20s. Noticeably, whereas CBM20s in amylolytic enzymes confer moderate binding affinities, with dissociation constants in the low micromolar range for the starch mimic beta-cyclodextrin, recent findings indicate that CBM20s in regulatory enzymes have weaker, low millimolar affinities, presumably facilitating dynamic regulation. Structures of CBM20s, including the first example of a full-length glucoamylase featuring both the catalytic domain and the SBD, are summarized, and distinct architectural and functional features of the two SBDs and roles of pivotal amino acids in binding are described. Finally, some applications of SBDs as affinity or immobilization tags and, recently, in biofuel and in planta bioengineering are presented.",
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    author = "Camilla Christiansen and {Abou Hachem}, Maher and S. Janecek and A. Vikso-Nielsen and A. Blennow and Birte Svensson",
    year = "2009",
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    The carbohydrate-binding module family 20-diversity, structure, and function. / Christiansen, Camilla; Abou Hachem, Maher; Janecek, S.; Vikso-Nielsen, A.; Blennow, A.; Svensson, Birte.

    In: F E B S Journal, Vol. 276, No. 18, 2009, p. 5006-5029.

    Research output: Contribution to journalJournal articleResearchpeer-review

    TY - JOUR

    T1 - The carbohydrate-binding module family 20-diversity, structure, and function

    AU - Christiansen, Camilla

    AU - Abou Hachem, Maher

    AU - Janecek, S.

    AU - Vikso-Nielsen, A.

    AU - Blennow, A.

    AU - Svensson, Birte

    PY - 2009

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    AB - Starch-active enzymes often possess starch-binding domains (SBDs) mediating attachment to starch granules and other high molecular weight substrates. SBDs are divided into nine carbohydrate-binding module (CBM) families, and CBM20 is the earliest-assigned and best characterized family. High diversity characterizes CBM20s, which occur in starch-active glycoside hydrolase families 13, 14, 15, and 77, and enzymes involved in starch or glycogen metabolism, exemplified by the starch-phosphorylating enzyme glucan, water dikinase 3 from Arabidopsis thaliana and the mammalian glycogen phosphatases, laforins. The clear evolutionary relatedness of CBM20s to CBM21s, CBM48s and CBM53s suggests a common clan hosting most of the known SBDs. This review surveys the diversity within the CBM20 family, and makes an evolutionary comparison with CBM21s, CBM48s and CBM53s, discussing intrafamily and interfamily relationships. Data on binding to and enzymatic activity towards soluble ligands and starch granules are summarized for wild-type, mutant and chimeric fusion proteins involving CBM20s. Noticeably, whereas CBM20s in amylolytic enzymes confer moderate binding affinities, with dissociation constants in the low micromolar range for the starch mimic beta-cyclodextrin, recent findings indicate that CBM20s in regulatory enzymes have weaker, low millimolar affinities, presumably facilitating dynamic regulation. Structures of CBM20s, including the first example of a full-length glucoamylase featuring both the catalytic domain and the SBD, are summarized, and distinct architectural and functional features of the two SBDs and roles of pivotal amino acids in binding are described. Finally, some applications of SBDs as affinity or immobilization tags and, recently, in biofuel and in planta bioengineering are presented.

    KW - starch-binding domain

    KW - alpha-glucan

    KW - water dikinase

    KW - molecular recognition

    KW - starch metabolism

    KW - amylolytic enzymes

    KW - glucan

    U2 - 10.1111/j.1742-4658.2009.07221.x

    DO - 10.1111/j.1742-4658.2009.07221.x

    M3 - Journal article

    VL - 276

    SP - 5006

    EP - 5029

    JO - F E B S Journal

    JF - F E B S Journal

    SN - 1742-464X

    IS - 18

    ER -