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Bifunctional enzyme fusion of 3-hexulose-6-phosphate synthase and 6-phospho-3-hexuloisomerase.

Bifunctional enzyme fusion of 3-hexulose-6-phosphate synthase and 6-phospho-3-hexuloisomerase. Research Abstract Details 

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  • Bifunctional enzyme fusion of 3-hexulose-6-phosphate synthase and 6-phospho-3-hexuloisomerase. Abstract Text:

    izumi oritaIzumi Orita,naoki sakamotoNaoki Sakamoto,nobuo katoNobuo Kato,hiroya yurimotoHiroya Yurimoto,yasuyoshi sakaiYasuyoshi Sakai,izumi oritaIzumi Orita,naoki sakamotoNaoki Sakamoto,nobuo katoNobuo Kato,hiroya yurimotoHiroya Yurimoto,yasuyoshi sakaiYasuyoshi Sakai,

    The formaldehyde-fixing enzymes, 3-Hexulose-6-phosphate synthase (HPS) and 6-phospho-3-hexuloisomerase (PHI), are the key enzymes catalyzing sequential reactions in the ribulose monophosphate (RuMP) pathway. In this study, we generated two fused gene constructs of the hps and phi genes (i.e., hps-phi and phi-hps) from a methylotrophic bacterium Mycobacterium gastri MB19. The gene product of hps-phi exhibited both HPS and PHI activities at room temperature and catalyzed the sequential reactions more efficiently than a simple mixture of the individual enzymes. The gene product of phi-hps failed to display any enzyme activity. Escherichia coli strains harboring the hps-phi gene consumed formaldehyde more efficiently and exhibited better growth in a formaldehyde-containing medium than the host strain. Our results demonstrate that the engineered fusion gene has the possibility to be used to establish a formaldehyde-resistance detoxification system in various organisms.

    Bifunctional enzyme fusion of 3-hexulose-6-phosphate synthase and 6-phospho-3-hexuloisomerase. Publishing Authors By Initials

    i oritaI Orita,n sakamotoN Sakamoto,n katoN Kato,h yurimotoH Yurimoto,y sakaiY Sakai,i oritaI Orita,n sakamotoN Sakamoto,n katoN Kato,h yurimotoH Yurimoto,y sakaiY Sakai,

    For similar abstracts research abstracts see: abstracts research

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    Bifunctional enzyme fusion of 3-hexulose-6-phosphate synthase and 6-phospho-3-hexuloisomerase. Journal Published:

    PUBLICATION TYPE: Research Support, Non-U.S. Gov

    Journal: Applied microbiology and biotechnology

    VOLUME: 76

    Page Numbers: 439-45

    Journal Abbreviation: Appl. Microbiol. Biotechnol.

    ISSN: 0175-7598

    DAY: 23

    MONTH: 05

    YEAR: 2007

    Bifunctional enzyme fusion of 3-hexulose-6-phosphate synthase and 6-phospho-3-hexuloisomerase. Information

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    LANGUAGE: eng

    NlmUniqueID: 8406612

    Bifunctional enzyme fusion of 3-hexulose-6-phosphate synthase and 6-phospho-3-hexuloisomerase. Keywords Mesh Terms:

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    Grant and Affiliation Information for Bifunctional enzyme fusion of 3-hexulose-6-phosphate synthase and 6-phospho-3-hexuloisomerase.

    AFFILIATION: Division of Applied Life Sciences, Graduate School of Agriculture, Kyoto University, Kitashirakawa-Oiwake, Sakyo-ku, 606-8502 Kyoto, Japan.

    Country: Germany

    Germany Research PublicationGermany Research Publication

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    MEDLINETA: Appl Microbiol Biotechnol

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