Functional characterization of aconitase X as a cis-3-hydroxy-L-proline dehydratase

Seiya Watanabe, Kunihiko Tajima, Satoshi Fujii, Fumiyasu Fukumori, Ryotaro Hara, Rio Fukuda, Mao Miyazaki, Kuniki Kino, Yasuo Watanabe

    Research output: Contribution to journalArticle

    3 Citations (Scopus)

    Abstract

    In the aconitase superfamily, which includes the archetypical aconitase, homoaconitase, and isopropylmalate isomerase, only aconitase X is not functionally annotated. The corresponding gene (LhpI) was often located within the bacterial gene cluster involved in L-hydroxyproline metabolism. Screening of a library of (hydroxy)proline analogues revealed that this protein catalyzes the dehydration of cis-3-hydroxy-L-proline to " 1 -pyrroline-2-carboxylate. Furthermore, electron paramagnetic resonance and site-directed mutagenic analyses suggests the presence of a mononuclear Fe(III) center, which may be coordinated with one glutamate and two cysteine residues. These properties were significantly different from those of other aconitase members, which catalyze the isomerization of α- to β-hydroxy acids, and have a [4Fe-4S] cluster-binding site composed of three cysteine residues. Bacteria with the LhpI gene could degrade cis-3-hydroxy-L-proline as the sole carbon source, and LhpI transcription was up-regulated not only by cis-3-hydroxy-L-proline, but also by several isomeric 3- and 4-hydroxyprolines.

    Original languageEnglish
    Article number38720
    JournalScientific Reports
    Volume6
    DOIs
    Publication statusPublished - 2016 Dec 8

    Fingerprint

    Aconitate Hydratase
    Hydro-Lyases
    Proline
    Hydroxyproline
    Cysteine
    Bacterial Genes
    Hydroxy Acids
    Electron Spin Resonance Spectroscopy
    Multigene Family
    Dehydration
    Genes
    Libraries
    Glutamic Acid
    Carbon
    Binding Sites
    Bacteria
    Proteins

    ASJC Scopus subject areas

    • General

    Cite this

    Watanabe, S., Tajima, K., Fujii, S., Fukumori, F., Hara, R., Fukuda, R., ... Watanabe, Y. (2016). Functional characterization of aconitase X as a cis-3-hydroxy-L-proline dehydratase. Scientific Reports, 6, [38720]. https://doi.org/10.1038/srep38720

    Functional characterization of aconitase X as a cis-3-hydroxy-L-proline dehydratase. / Watanabe, Seiya; Tajima, Kunihiko; Fujii, Satoshi; Fukumori, Fumiyasu; Hara, Ryotaro; Fukuda, Rio; Miyazaki, Mao; Kino, Kuniki; Watanabe, Yasuo.

    In: Scientific Reports, Vol. 6, 38720, 08.12.2016.

    Research output: Contribution to journalArticle

    Watanabe, S, Tajima, K, Fujii, S, Fukumori, F, Hara, R, Fukuda, R, Miyazaki, M, Kino, K & Watanabe, Y 2016, 'Functional characterization of aconitase X as a cis-3-hydroxy-L-proline dehydratase', Scientific Reports, vol. 6, 38720. https://doi.org/10.1038/srep38720
    Watanabe S, Tajima K, Fujii S, Fukumori F, Hara R, Fukuda R et al. Functional characterization of aconitase X as a cis-3-hydroxy-L-proline dehydratase. Scientific Reports. 2016 Dec 8;6. 38720. https://doi.org/10.1038/srep38720
    Watanabe, Seiya ; Tajima, Kunihiko ; Fujii, Satoshi ; Fukumori, Fumiyasu ; Hara, Ryotaro ; Fukuda, Rio ; Miyazaki, Mao ; Kino, Kuniki ; Watanabe, Yasuo. / Functional characterization of aconitase X as a cis-3-hydroxy-L-proline dehydratase. In: Scientific Reports. 2016 ; Vol. 6.
    @article{c0d8d190b4ce485ebcde3242d1513820,
    title = "Functional characterization of aconitase X as a cis-3-hydroxy-L-proline dehydratase",
    abstract = "In the aconitase superfamily, which includes the archetypical aconitase, homoaconitase, and isopropylmalate isomerase, only aconitase X is not functionally annotated. The corresponding gene (LhpI) was often located within the bacterial gene cluster involved in L-hydroxyproline metabolism. Screening of a library of (hydroxy)proline analogues revealed that this protein catalyzes the dehydration of cis-3-hydroxy-L-proline to {"} 1 -pyrroline-2-carboxylate. Furthermore, electron paramagnetic resonance and site-directed mutagenic analyses suggests the presence of a mononuclear Fe(III) center, which may be coordinated with one glutamate and two cysteine residues. These properties were significantly different from those of other aconitase members, which catalyze the isomerization of α- to β-hydroxy acids, and have a [4Fe-4S] cluster-binding site composed of three cysteine residues. Bacteria with the LhpI gene could degrade cis-3-hydroxy-L-proline as the sole carbon source, and LhpI transcription was up-regulated not only by cis-3-hydroxy-L-proline, but also by several isomeric 3- and 4-hydroxyprolines.",
    author = "Seiya Watanabe and Kunihiko Tajima and Satoshi Fujii and Fumiyasu Fukumori and Ryotaro Hara and Rio Fukuda and Mao Miyazaki and Kuniki Kino and Yasuo Watanabe",
    year = "2016",
    month = "12",
    day = "8",
    doi = "10.1038/srep38720",
    language = "English",
    volume = "6",
    journal = "Scientific Reports",
    issn = "2045-2322",
    publisher = "Nature Publishing Group",

    }

    TY - JOUR

    T1 - Functional characterization of aconitase X as a cis-3-hydroxy-L-proline dehydratase

    AU - Watanabe, Seiya

    AU - Tajima, Kunihiko

    AU - Fujii, Satoshi

    AU - Fukumori, Fumiyasu

    AU - Hara, Ryotaro

    AU - Fukuda, Rio

    AU - Miyazaki, Mao

    AU - Kino, Kuniki

    AU - Watanabe, Yasuo

    PY - 2016/12/8

    Y1 - 2016/12/8

    N2 - In the aconitase superfamily, which includes the archetypical aconitase, homoaconitase, and isopropylmalate isomerase, only aconitase X is not functionally annotated. The corresponding gene (LhpI) was often located within the bacterial gene cluster involved in L-hydroxyproline metabolism. Screening of a library of (hydroxy)proline analogues revealed that this protein catalyzes the dehydration of cis-3-hydroxy-L-proline to " 1 -pyrroline-2-carboxylate. Furthermore, electron paramagnetic resonance and site-directed mutagenic analyses suggests the presence of a mononuclear Fe(III) center, which may be coordinated with one glutamate and two cysteine residues. These properties were significantly different from those of other aconitase members, which catalyze the isomerization of α- to β-hydroxy acids, and have a [4Fe-4S] cluster-binding site composed of three cysteine residues. Bacteria with the LhpI gene could degrade cis-3-hydroxy-L-proline as the sole carbon source, and LhpI transcription was up-regulated not only by cis-3-hydroxy-L-proline, but also by several isomeric 3- and 4-hydroxyprolines.

    AB - In the aconitase superfamily, which includes the archetypical aconitase, homoaconitase, and isopropylmalate isomerase, only aconitase X is not functionally annotated. The corresponding gene (LhpI) was often located within the bacterial gene cluster involved in L-hydroxyproline metabolism. Screening of a library of (hydroxy)proline analogues revealed that this protein catalyzes the dehydration of cis-3-hydroxy-L-proline to " 1 -pyrroline-2-carboxylate. Furthermore, electron paramagnetic resonance and site-directed mutagenic analyses suggests the presence of a mononuclear Fe(III) center, which may be coordinated with one glutamate and two cysteine residues. These properties were significantly different from those of other aconitase members, which catalyze the isomerization of α- to β-hydroxy acids, and have a [4Fe-4S] cluster-binding site composed of three cysteine residues. Bacteria with the LhpI gene could degrade cis-3-hydroxy-L-proline as the sole carbon source, and LhpI transcription was up-regulated not only by cis-3-hydroxy-L-proline, but also by several isomeric 3- and 4-hydroxyprolines.

    UR - http://www.scopus.com/inward/record.url?scp=85006054943&partnerID=8YFLogxK

    UR - http://www.scopus.com/inward/citedby.url?scp=85006054943&partnerID=8YFLogxK

    U2 - 10.1038/srep38720

    DO - 10.1038/srep38720

    M3 - Article

    C2 - 27929065

    AN - SCOPUS:85006054943

    VL - 6

    JO - Scientific Reports

    JF - Scientific Reports

    SN - 2045-2322

    M1 - 38720

    ER -