A β1-6/β1-3 galactosidase from B ifidobacterium animalis subsp. lactis Bl-04 gives insight into sub-specificities of β-galactoside catabolism within B ifidobacterium

Alexander Holm Viborg, Folmer Fredslund, Takane Katayama, Stinne Kirketerp Nielsen, Birte Svensson, Motomitsu Kitaoka, Leila Lo Leggio, Maher Abou Hachem

    Research output: Contribution to journalJournal articleResearchpeer-review

    Abstract

    The Bifidobacterium genus harbours several health promoting members of the gut microbiota. Bifidobacteria display metabolic specialization by preferentially utilizing dietary or host-derived β-galactosides. This study investigates the biochemistry and structure of a glycoside hydrolase family 42 (GH42) β-galactosidase from the probiotic Bifidobacterium animalis subsp. lactis Bl-04 (BlGal42A). BlGal42A displays a preference for undecorated β1-6 and β1-3 linked galactosides and populates a phylogenetic cluster with close bifidobacterial homologues implicated in the utilization of N-acetyl substituted β1-3 galactosides from human milk and mucin. A long loop containing an invariant tryptophan in GH42, proposed to bind substrate at subsite + 1, is identified here as specificity signature within this clade of bifidobacterial enzymes. Galactose binding at the subsite − 1 of the active site induced conformational changes resulting in an extra polar interaction and the ordering of a flexible loop that narrows the active site. The amino acid sequence of this loop provides an additional specificity signature within this GH42 clade. The phylogenetic relatedness of enzymes targeting β1-6 and β1-3 galactosides likely reflects structural differences between these substrates and β1-4 galactosides, containing an axial galactosidic bond. These data advance our molecular understanding of the evolution of sub-specificities that support metabolic specialization in the gut niche.
    Original languageEnglish
    JournalMolecular Microbiology
    Volume94
    Issue number5
    Pages (from-to)1024–1040
    Number of pages17
    ISSN0950-382X
    DOIs
    Publication statusPublished - 2014

    Cite this

    @article{7e25b8720ae242cf8bc0e1803e779f93,
    title = "A β1-6/β1-3 galactosidase from B ifidobacterium animalis subsp. lactis Bl-04 gives insight into sub-specificities of β-galactoside catabolism within B ifidobacterium",
    abstract = "The Bifidobacterium genus harbours several health promoting members of the gut microbiota. Bifidobacteria display metabolic specialization by preferentially utilizing dietary or host-derived β-galactosides. This study investigates the biochemistry and structure of a glycoside hydrolase family 42 (GH42) β-galactosidase from the probiotic Bifidobacterium animalis subsp. lactis Bl-04 (BlGal42A). BlGal42A displays a preference for undecorated β1-6 and β1-3 linked galactosides and populates a phylogenetic cluster with close bifidobacterial homologues implicated in the utilization of N-acetyl substituted β1-3 galactosides from human milk and mucin. A long loop containing an invariant tryptophan in GH42, proposed to bind substrate at subsite + 1, is identified here as specificity signature within this clade of bifidobacterial enzymes. Galactose binding at the subsite − 1 of the active site induced conformational changes resulting in an extra polar interaction and the ordering of a flexible loop that narrows the active site. The amino acid sequence of this loop provides an additional specificity signature within this GH42 clade. The phylogenetic relatedness of enzymes targeting β1-6 and β1-3 galactosides likely reflects structural differences between these substrates and β1-4 galactosides, containing an axial galactosidic bond. These data advance our molecular understanding of the evolution of sub-specificities that support metabolic specialization in the gut niche.",
    author = "Viborg, {Alexander Holm} and Folmer Fredslund and Takane Katayama and Nielsen, {Stinne Kirketerp} and Birte Svensson and Motomitsu Kitaoka and Leggio, {Leila Lo} and {Abou Hachem}, Maher",
    year = "2014",
    doi = "10.1111/mmi.12815",
    language = "English",
    volume = "94",
    pages = "1024–1040",
    journal = "Molecular Microbiology",
    issn = "0950-382X",
    publisher = "Wiley-Blackwell",
    number = "5",

    }

    A β1-6/β1-3 galactosidase from B ifidobacterium animalis subsp. lactis Bl-04 gives insight into sub-specificities of β-galactoside catabolism within B ifidobacterium. / Viborg, Alexander Holm; Fredslund, Folmer; Katayama, Takane; Nielsen, Stinne Kirketerp; Svensson, Birte; Kitaoka, Motomitsu; Leggio, Leila Lo; Abou Hachem, Maher .

    In: Molecular Microbiology, Vol. 94, No. 5, 2014, p. 1024–1040.

    Research output: Contribution to journalJournal articleResearchpeer-review

    TY - JOUR

    T1 - A β1-6/β1-3 galactosidase from B ifidobacterium animalis subsp. lactis Bl-04 gives insight into sub-specificities of β-galactoside catabolism within B ifidobacterium

    AU - Viborg, Alexander Holm

    AU - Fredslund, Folmer

    AU - Katayama, Takane

    AU - Nielsen, Stinne Kirketerp

    AU - Svensson, Birte

    AU - Kitaoka, Motomitsu

    AU - Leggio, Leila Lo

    AU - Abou Hachem, Maher

    PY - 2014

    Y1 - 2014

    N2 - The Bifidobacterium genus harbours several health promoting members of the gut microbiota. Bifidobacteria display metabolic specialization by preferentially utilizing dietary or host-derived β-galactosides. This study investigates the biochemistry and structure of a glycoside hydrolase family 42 (GH42) β-galactosidase from the probiotic Bifidobacterium animalis subsp. lactis Bl-04 (BlGal42A). BlGal42A displays a preference for undecorated β1-6 and β1-3 linked galactosides and populates a phylogenetic cluster with close bifidobacterial homologues implicated in the utilization of N-acetyl substituted β1-3 galactosides from human milk and mucin. A long loop containing an invariant tryptophan in GH42, proposed to bind substrate at subsite + 1, is identified here as specificity signature within this clade of bifidobacterial enzymes. Galactose binding at the subsite − 1 of the active site induced conformational changes resulting in an extra polar interaction and the ordering of a flexible loop that narrows the active site. The amino acid sequence of this loop provides an additional specificity signature within this GH42 clade. The phylogenetic relatedness of enzymes targeting β1-6 and β1-3 galactosides likely reflects structural differences between these substrates and β1-4 galactosides, containing an axial galactosidic bond. These data advance our molecular understanding of the evolution of sub-specificities that support metabolic specialization in the gut niche.

    AB - The Bifidobacterium genus harbours several health promoting members of the gut microbiota. Bifidobacteria display metabolic specialization by preferentially utilizing dietary or host-derived β-galactosides. This study investigates the biochemistry and structure of a glycoside hydrolase family 42 (GH42) β-galactosidase from the probiotic Bifidobacterium animalis subsp. lactis Bl-04 (BlGal42A). BlGal42A displays a preference for undecorated β1-6 and β1-3 linked galactosides and populates a phylogenetic cluster with close bifidobacterial homologues implicated in the utilization of N-acetyl substituted β1-3 galactosides from human milk and mucin. A long loop containing an invariant tryptophan in GH42, proposed to bind substrate at subsite + 1, is identified here as specificity signature within this clade of bifidobacterial enzymes. Galactose binding at the subsite − 1 of the active site induced conformational changes resulting in an extra polar interaction and the ordering of a flexible loop that narrows the active site. The amino acid sequence of this loop provides an additional specificity signature within this GH42 clade. The phylogenetic relatedness of enzymes targeting β1-6 and β1-3 galactosides likely reflects structural differences between these substrates and β1-4 galactosides, containing an axial galactosidic bond. These data advance our molecular understanding of the evolution of sub-specificities that support metabolic specialization in the gut niche.

    U2 - 10.1111/mmi.12815

    DO - 10.1111/mmi.12815

    M3 - Journal article

    VL - 94

    SP - 1024

    EP - 1040

    JO - Molecular Microbiology

    JF - Molecular Microbiology

    SN - 0950-382X

    IS - 5

    ER -