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<p>Cells achieve metabolic precision by assembling enzymes into dynamic complexes, but the regulatory mechanism of these metabolons is unclear. Here we characterize the chalcone synthase (CHS)–chalcone isomerase-like protein (CHIL) complex, a key component of flavonoid metabolons. While crystallography provides a static view, our analyses reveal that CHS undergoes rapid, reversible binding cycles with CHIL that regulate catalysis in real time. CHIL removes coenzyme A, an inhibitor of Claisen cyclization, transiently reshapes the CHS active site and guides the tetraketide intermediate towards productive cyclization, thereby suppressing derailment by-products. These findings demonstrate a previously unproven and generalizable regulatory effect in metabolons: guided active-site tuning via transient enzyme association. This concept enhances our understanding of metabolon function and opens avenues for synthetic biology and metabolic engineering.</p><p></p>

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Transient dynamics of flavonoid metabolons tune chalcone synthase specificity

  • 期刊论文

  • 出版模式：

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  • 发表日期：

    2026年6月15日

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  • Riki Imaizumi,
  • Toshiyuki Waki,
  • Yoshikazu Hattori,
  • Kohei Takeshita,
  • Miru Sumita,
  • Kazutomo Kawaguchi,
  • Hiroyuki Kumeta,
  • Kenichi Umeda,
  • Kyohei Sato,
  • Taro Yanai,
  • Hiroaki Matsuura,
  • Takeshi Yokoyama,
  • Risa Omura,
  • Kayo Nakatani,
  • Naoki Sakai,
  • Yukimura Kawagiwa,
  • Yamato Doi,
  • Aoi Yasuda,
  • Takuya Nakano,
  • Kaichi Uno,
  • Kunihiro Yoshida,
  • Misato Tsunashima,
  • Tomohide Saio,
  • Yoshikazu Tanaka,
  • Seiji Takahashi,
  • Noriyuki Kodera,
  • Kunishige Kataoka,
  • Masaki Yamamoto,
  • Satoshi Yamashita,
  • Toru Nakayama

摘要

Cells achieve metabolic precision by assembling enzymes into dynamic complexes, but the regulatory mechanism of these metabolons is unclear. Here we characterize the chalcone synthase (CHS)–chalcone isomerase-like protein (CHIL) complex, a key component of flavonoid metabolons. While crystallography provides a static view, our analyses reveal that CHS undergoes rapid, reversible binding cycles with CHIL that regulate catalysis in real time. CHIL removes coenzyme A, an inhibitor of Claisen cyclization, transiently reshapes the CHS active site and guides the tetraketide intermediate towards productive cyclization, thereby suppressing derailment by-products. These findings demonstrate a previously unproven and generalizable regulatory effect in metabolons: guided active-site tuning via transient enzyme association. This concept enhances our understanding of metabolon function and opens avenues for synthetic biology and metabolic engineering.