{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,2,10]],"date-time":"2026-02-10T18:56:32Z","timestamp":1770749792998,"version":"3.50.0"},"reference-count":68,"publisher":"MDPI AG","issue":"2","license":[{"start":{"date-parts":[[2026,2,10]],"date-time":"2026-02-10T00:00:00Z","timestamp":1770681600000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"DOI":"10.13039\/501100006769","name":"Russian Science Foundation","doi-asserted-by":"publisher","award":["24-24-00304"],"award-info":[{"award-number":["24-24-00304"]}],"id":[{"id":"10.13039\/501100006769","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Pharmaceuticals"],"abstract":"<jats:p>Background: Lyases are used in a wide scope of applications, making them invaluable tools in both industrial biotechnology and molecular biology. Many examples of lyases belong to the extensive family of pyridoxal 5\u2032-phosphate (PLP)-dependent enzymes, which catalyze numerous reactions involved in amino acid metabolism, like tryptophan indole-lyase (Trpase or Tnase), tyrosine phenol-lyase (TPL), and methionine \u03b3-lyase (MGL). Beyond their role in physiological processes, these lyases can also facilitate the synthesis of other biologically active products from non-canonical substrates. Objectives: Up till now there were only two C\u2013S lyases known for the thiosulfinates\u2019 biosynthesis from S-substituted L-cysteine sulfoxides\u2014alliinase and MGL. Our study reveals for the first time that C\u2013C lyases are capable of C\u2013S lyase activity in reactions with S-alkyl, S-allyl and S-benzyl cysteine sulfoxides. Methods: We have compared the kinetic profiles of S-substituted L-cysteine sulfoxide degradation mediated by carbon\u2013sulfur lyase MGL versus carbon\u2013carbon lyases TPL and Trpase. Results: Among other S-alkyl-L-cysteine sulfoxides, petiveriin (S-benzyl-L-cysteine sulfoxide) was proven to be a substrate for all three enzymes. The potential utility of these enzymes in thiosulfinate production was supported by in vitro testing of enzyme-generated thiosulfinates against clinically relevant pathogens such as Candida albicans, Pseudomonas aeruginosa, and Staphylococcus aureus. Conclusions: Both C\u2013S and C\u2013C lyases\u2014MGL, TPL, and Trpase\u2014can be implemented for practical application in thiosulfinate synthesis.<\/jats:p>","DOI":"10.3390\/ph19020291","type":"journal-article","created":{"date-parts":[[2026,2,10]],"date-time":"2026-02-10T12:07:06Z","timestamp":1770725226000},"page":"291","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":0,"title":["Hidden Activities of Tyrosine Phenol-Lyase and Tryptophan Indole-Lyase: Recombinant PLP-Dependent C\u2013C Lyases as New Biocatalysts for Antimicrobial Thiosulfinate Generation"],"prefix":"10.3390","volume":"19","author":[{"ORCID":"https:\/\/orcid.org\/0000-0003-0618-1407","authenticated-orcid":false,"given":"Vitalia V.","family":"Kulikova","sequence":"first","affiliation":[{"name":"Engelhardt Institute of Molecular Biology of the Russian Academy of Sciences, 119991 Moscow, Russia"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-1594-9334","authenticated-orcid":false,"given":"Svetlana V.","family":"Revtovich","sequence":"additional","affiliation":[{"name":"Engelhardt Institute of Molecular Biology of the Russian Academy of Sciences, 119991 Moscow, Russia"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0009-0003-3031-4537","authenticated-orcid":false,"given":"Kseniya P.","family":"Levshina","sequence":"additional","affiliation":[{"name":"Engelhardt Institute of Molecular Biology of the Russian Academy of Sciences, 119991 Moscow, Russia"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0009-0004-3563-6612","authenticated-orcid":false,"given":"Yaroslav V.","family":"Kozmenko","sequence":"additional","affiliation":[{"name":"Engelhardt Institute of Molecular Biology of the Russian Academy of Sciences, 119991 Moscow, Russia"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-6611-8840","authenticated-orcid":false,"given":"Natalya V.","family":"Anufrieva","sequence":"additional","affiliation":[{"name":"Engelhardt Institute of Molecular Biology of the Russian Academy of Sciences, 119991 Moscow, Russia"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-2922-2793","authenticated-orcid":false,"given":"Elena A.","family":"Morozova","sequence":"additional","affiliation":[{"name":"Engelhardt Institute of Molecular Biology of the Russian Academy of Sciences, 119991 Moscow, Russia"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-5546-4975","authenticated-orcid":false,"given":"Pavel N.","family":"Solyev","sequence":"additional","affiliation":[{"name":"Engelhardt Institute of Molecular Biology of the Russian Academy of Sciences, 119991 Moscow, Russia"}],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"1968","published-online":{"date-parts":[[2026,2,10]]},"reference":[{"key":"ref_1","doi-asserted-by":"crossref","unstructured":"Zhang, N., de Mar\u00eda, P.D., and Kara, S. 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