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<p>Our understanding of how depolymerase sequence and structure determine substrate specificity is fragmentary due to the limited number of experimentally characterized enzymes. Here we show DepoCatalog - an experimentally validated collection of 129 recombinantly prepared <i>Klebsiella</i> phage depolymerases (90 enzymes produced in this study and 39 homologs from the literature), with specificity spanning 75 KL-types. Enzymes originated from podo-, sipho-, myo-, jumbo phages, and prophages. Using activity profiling, structural modeling, and domain dissection, we propose a five‑class framework that captures the architectural and functional diversity of these enzymes. DepoCatalog uncovers cross-reactivity and taxa‑specific enzymes. Structural comparisons indicate that specificity switching or extension is associated with modifications to the C‑terminal domain. We further hypothesize that podoviruses encoding up to two RBPs show greater receptor adaptability than jumbo phages with multiple specialized RBPs. Finally, we develop a publicly accessible, DepoCat dataset (<a href="https://depocat.uwr.edu.pl">https://depocat.uwr.edu.pl</a>) for specificity,&#xa0;structural classification and comparison of newly identified depolymerases.</p>

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DepoCatalog: mapping diversity of 129 recombinantly produced Klebsiella phage depolymerases

  • 期刊论文

  • 出版模式：

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  • 发表日期：

    2026年5月22日

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  • Aleksandra Otwinowska,
  • Sebastian Olejniczak,
  • Agnieszka Latka,
  • Maria Pozniak,
  • Grazyna Majkowska-Skrobek,
  • Barbara Maciejewska,
  • Janusz Koszucki,
  • Vyshakh R. Panicker,
  • Sara Jablonska,
  • Mathilde Hulsens,
  • Jana Stender,
  • Maha Niazi,
  • Sabrina Green,
  • Joachim J. Bugert,
  • Régis Tournebize,
  • Stan J. J. Brouns,
  • Flavia Squeglia,
  • Rita Berisio,
  • Jens A. Hammerl,
  • Rob Lavigne,
  • Yves Briers,
  • Rafal J. Mostowy,
  • Zuzanna Drulis-Kawa

摘要

Our understanding of how depolymerase sequence and structure determine substrate specificity is fragmentary due to the limited number of experimentally characterized enzymes. Here we show DepoCatalog - an experimentally validated collection of 129 recombinantly prepared Klebsiella phage depolymerases (90 enzymes produced in this study and 39 homologs from the literature), with specificity spanning 75 KL-types. Enzymes originated from podo-, sipho-, myo-, jumbo phages, and prophages. Using activity profiling, structural modeling, and domain dissection, we propose a five‑class framework that captures the architectural and functional diversity of these enzymes. DepoCatalog uncovers cross-reactivity and taxa‑specific enzymes. Structural comparisons indicate that specificity switching or extension is associated with modifications to the C‑terminal domain. We further hypothesize that podoviruses encoding up to two RBPs show greater receptor adaptability than jumbo phages with multiple specialized RBPs. Finally, we develop a publicly accessible, DepoCat dataset (https://depocat.uwr.edu.pl) for specificity, structural classification and comparison of newly identified depolymerases.