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Structures of Polyhydroxyalkanoate Synthase PhaC from <i>Aeromonas caviae</i> , Producing Biodegradable Plastics

Angewandte Chemie International Edition 2025 4 citations ? Citation count from OpenAlex, updated daily. May differ slightly from the publisher's own count. Score: 48 ? 0–100 AI score estimating relevance to the microplastics field. Papers below 30 are filtered from public browse.
Min Fey Chek, Sun‐Yong Kim, Tomoyuki Mori, Min Fey Chek, Tomoyuki Mori, Keiji Matsumoto, Keiji Matsumoto, Shunsuke Sato, Shunsuke Sato, Shunsuke Sato, Shunsuke Sato, Shunsuke Sato, Toshio Hakoshima Shunsuke Sato, Toshio Hakoshima

Summary

Researchers solved the crystal structures of polyhydroxyalkanoate synthase PhaC from Aeromonas caviae, providing molecular-level insight into how this bacterial enzyme polymerizes biodegradable PHA plastics, with implications for engineering improved bioplastic production systems.

Polyhydroxyalkanoate (PHA) is a biodegradable polyester that can serve as a promising alternative to petrochemical plastics, which present a serious source of pollution. PHA synthase (PhaC) is a key enzyme responsible for producing a wide variety of PHAs in microorganisms. Here, we present crystal structures of full-length PhaC from Aeromonas caviae, a high-performance PhaC employed for industrial use. The structure reveals an N-terminal helical domain that mediates head-to-head dimerization and stabilizes the C-terminal α/β catalytic domain to form a tunnel that connects the catalytic center embedded inside the protein to the protein surface. We showed that this tunnel is a putative egress tunnel for the product PHA chain. Our results establish a fundamental understanding of the PhaC machinery that should lead to improvement of this enzyme in industrial applications.

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