Identification and characterization of 2-oxoglutarate-dependent dioxygenases catalyzing selective cis-hydroxylation of proline and pipecolinic acid from actinomycetes

Ryotaro Hara, Naoko Uchiumi, Kuniki Kino

    Research output: Contribution to journalArticle

    7 Citations (Scopus)

    Abstract

    Microbial hydroxylases were screened for the capacity to effect direct hydroxylation of proline and pipecolinic acid, based on genomic information. Of the eight candidates screened, 2-oxoglutarate-dependent hydroxylase from Streptosporangium roseum NBRC 3776T and aspartyl/asparaginyl β-hydroxylase from Catenulispora acidiphila NBRC 102108T showed both proline and pipecolinic acid hydroxylation activities. In the case of l-proline hydroxylation, both enzymes catalyzed the simultaneous formation of cis-3-hydroxy-l-proline and cis-4-hydroxy-l-proline, and cis-4-hydroxy-l-proline was preferentially produced. In the case of l-pipecolinic acid hydroxylation, both enzymes catalyzed the simultaneous formation of cis-3-hydroxy-l-pipecolinic acid and cis-5-hydroxy-l-pipecolinic acid. While the former enzyme preferentially produced cis-3-hydroxy-l-pipecolinic acid, the latter enzyme preferentially produced cis-5-hydroxy-l-pipecolinic acid.

    Original languageEnglish
    Pages (from-to)55-58
    Number of pages4
    JournalJournal of Biotechnology
    Volume172
    Issue number1
    DOIs
    Publication statusPublished - 2014 Feb 20

    Fingerprint

    Dioxygenases
    Hydroxylation
    Actinobacteria
    Proline
    Hydroxyproline
    Acids
    Mixed Function Oxygenases
    Enzymes
    NSC 153174
    alpha-ketoglutaric acid
    Thermodynamic properties

    Keywords

    • Dioxygenase
    • Hydroxylase
    • Hydroxylation
    • Hydroxypipecolinic acid
    • Hydroxyproline

    ASJC Scopus subject areas

    • Biotechnology
    • Applied Microbiology and Biotechnology

    Cite this

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    abstract = "Microbial hydroxylases were screened for the capacity to effect direct hydroxylation of proline and pipecolinic acid, based on genomic information. Of the eight candidates screened, 2-oxoglutarate-dependent hydroxylase from Streptosporangium roseum NBRC 3776T and aspartyl/asparaginyl β-hydroxylase from Catenulispora acidiphila NBRC 102108T showed both proline and pipecolinic acid hydroxylation activities. In the case of l-proline hydroxylation, both enzymes catalyzed the simultaneous formation of cis-3-hydroxy-l-proline and cis-4-hydroxy-l-proline, and cis-4-hydroxy-l-proline was preferentially produced. In the case of l-pipecolinic acid hydroxylation, both enzymes catalyzed the simultaneous formation of cis-3-hydroxy-l-pipecolinic acid and cis-5-hydroxy-l-pipecolinic acid. While the former enzyme preferentially produced cis-3-hydroxy-l-pipecolinic acid, the latter enzyme preferentially produced cis-5-hydroxy-l-pipecolinic acid.",
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    author = "Ryotaro Hara and Naoko Uchiumi and Kuniki Kino",
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    AU - Uchiumi, Naoko

    AU - Kino, Kuniki

    PY - 2014/2/20

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    N2 - Microbial hydroxylases were screened for the capacity to effect direct hydroxylation of proline and pipecolinic acid, based on genomic information. Of the eight candidates screened, 2-oxoglutarate-dependent hydroxylase from Streptosporangium roseum NBRC 3776T and aspartyl/asparaginyl β-hydroxylase from Catenulispora acidiphila NBRC 102108T showed both proline and pipecolinic acid hydroxylation activities. In the case of l-proline hydroxylation, both enzymes catalyzed the simultaneous formation of cis-3-hydroxy-l-proline and cis-4-hydroxy-l-proline, and cis-4-hydroxy-l-proline was preferentially produced. In the case of l-pipecolinic acid hydroxylation, both enzymes catalyzed the simultaneous formation of cis-3-hydroxy-l-pipecolinic acid and cis-5-hydroxy-l-pipecolinic acid. While the former enzyme preferentially produced cis-3-hydroxy-l-pipecolinic acid, the latter enzyme preferentially produced cis-5-hydroxy-l-pipecolinic acid.

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    KW - Hydroxyproline

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