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<p>Serine proteases in ribosomally synthesized and post-translationally modified peptides (RiPPs) catalyze the cleavage on the precursor peptides in the biosynthesis of RiPP natural products. Here, we identified an uncharacterized serine protease WprP<sub>2</sub> from <i>Streptomyces venezuelae</i> NPDC049867, encoded next to the radical <i>S</i>-adenosyl-L-methionine (SAM) enzyme WprB<sub>2</sub> involved in the biosynthesis of cyclophane natural products. In vitro characterization of S9 protease WprP<sub>2</sub> revealed that the precursor peptide WprA<sub>2</sub> is uniformly cleaved. The cleavage activity of WprP<sub>2</sub> has not been seen in any serine proteases and expands the S9 protease in RiPP biosynthesis.</p><p></p>

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S9 protease WprP2 catalyzes uniform cleavage on the precursor peptide in RiPP biosynthesis

  • 期刊论文

  • 出版模式：

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  • 发表日期：

    2026年1月29日

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  • Jabal Rahmat Haedar,
  • Abujunaid Habib Khan,
  • Suze Ma,
  • Stefano Donadio,
  • Chin-Soon Phan

摘要

Serine proteases in ribosomally synthesized and post-translationally modified peptides (RiPPs) catalyze the cleavage on the precursor peptides in the biosynthesis of RiPP natural products. Here, we identified an uncharacterized serine protease WprP2 from Streptomyces venezuelae NPDC049867, encoded next to the radical S-adenosyl-L-methionine (SAM) enzyme WprB2 involved in the biosynthesis of cyclophane natural products. In vitro characterization of S9 protease WprP2 revealed that the precursor peptide WprA2 is uniformly cleaved. The cleavage activity of WprP2 has not been seen in any serine proteases and expands the S9 protease in RiPP biosynthesis.