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Sökning: WFRF:(Hoshino Yosuke)

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  • Gamiz-Arco, Gloria, et al. (författare)
  • Heme-binding enables allosteric modulation in an ancient TIM-barrel glycosidase
  • 2021
  • Ingår i: Nature Communications. - : Springer Nature. - 2041-1723. ; 12
  • Tidskriftsartikel (refereegranskat)abstract
    • Glycosidases are phylogenetically widely distributed enzymes that are crucial for the cleavage of glycosidic bonds. Here, we present the exceptional properties of a putative ancestor of bacterial and eukaryotic family-1 glycosidases. The ancestral protein shares the TIM-barrel fold with its modern descendants but displays large regions with greatly enhanced conformational flexibility. Yet, the barrel core remains comparatively rigid and the ancestral glycosidase activity is stable, with an optimum temperature within the experimental range for thermophilic family-1 glycosidases. None of the similar to 5500 reported crystallographic structures of similar to 1400 modern glycosidases show a bound porphyrin. Remarkably, the ancestral glycosidase binds heme tightly and stoichiometrically at a well-defined buried site. Heme binding rigidifies this TIM-barrel and allosterically enhances catalysis. Our work demonstrates the capability of ancestral protein reconstructions to reveal valuable but unexpected biomolecular features when sampling distant sequence space. The potential of the ancestral glycosidase as a scaffold for custom catalysis and biosensor engineering is discussed. Family 1 glycosidases (GH1) are present in the three domains of life and share classical TIM-barrel fold. Structural and biochemical analyses of a resurrected ancestral GH1 enzyme reveal heme binding, not known in its modern descendants. Heme rigidifies the TIM-barrel and allosterically enhances catalysis.
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3.
  • Hoshino, Yosuke, et al. (författare)
  • Cryogenian evolution of stigmasteroid biosynthesis
  • 2017
  • Ingår i: Science Advances. - : AMER ASSOC ADVANCEMENT SCIENCE. - 2375-2548. ; 3:9
  • Tidskriftsartikel (refereegranskat)abstract
    • Sedimentary hydrocarbon remnants of eukaryotic C-26-C-30 sterols can be used to reconstruct early algal evolution. Enhanced C-29 sterol abundances provide algal cellmembranes a density advantage in large temperature fluctuations. Here, we combined a literature review with new analyses to generate a comprehensive inventory of unambiguously syngenetic steranes in Neoproterozoic rocks. Our results show that the capacity for C-29 24ethyl- sterol biosynthesis emerged in the Cryogenian, that is, between 720 and 635 million years ago during the Neoproterozoic Snowball Earth glaciations, which were an evolutionary stimulant, not a bottleneck. This biochemical innovation heralded the rise of green algae to global dominance of marine ecosystems and highlights the environmental drivers for the evolution of sterol biosynthesis. The Cryogenian emergence of C-29 sterol biosynthesis places benchmark for verifying older sterane signatures and sets a new framework for our understanding of early algal evolution.
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  • Resultat 1-3 av 3

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