{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,30]],"date-time":"2026-09-30T11:58:16Z","timestamp":1790769496972,"version":"4.1.0"},"reference-count":58,"publisher":"Wiley","issue":"11","license":[{"start":{"date-parts":[[2026,9,30]],"date-time":"2026-09-30T00:00:00Z","timestamp":1790726400000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"},{"start":{"date-parts":[[2026,9,30]],"date-time":"2026-09-30T00:00:00Z","timestamp":1790726400000},"content-version":"tdm","delay-in-days":0,"URL":"http:\/\/doi.wiley.com\/10.1002\/tdm_license_1.1"}],"funder":[{"DOI":"10.13039\/501100006769","name":"Russian Science Foundation","doi-asserted-by":"publisher","award":["23\u201074\u201030004"],"award-info":[{"award-number":["23\u201074\u201030004"]}],"id":[{"id":"10.13039\/501100006769","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["onlinelibrary.wiley.com"],"crossmark-restriction":true},"short-container-title":["Protein Science"],"published-print":{"date-parts":[[2026,11]]},"abstract":"<jats:title>Abstract<\/jats:title>\n                  <jats:p>\n                    Pyridoxal\u20105\u2032\u2010phosphate (PLP)\u2010dependent enzymes of fold type IV exhibit remarkable catalytic diversity, catalyzing either\n                    <jats:italic>S<\/jats:italic>\n                    \u2010 and\n                    <jats:italic>R<\/jats:italic>\n                    \u2010selective transamination or\n                    <jats:italic>\u03b2<\/jats:italic>\n                    \u2010elimination within a highly conserved structural scaffold. Here, we report the identification, biochemical characterization, and structural analysis of PLP fold type IV 4\u2010amino\u20104\u2010deoxychorismate lyase (ADCL) from\n                    <jats:italic>Micromonospora aurantiaca<\/jats:italic>\n                    (Micau5708). Sequence\u2010structural analysis revealed a hybrid architecture of the active site of Micau5708. It combines a D\u2010amino acid transaminase (DATA) conserved phenylalanine (F30) and arginine (R87) residues with an ADCL\u2010specific threonine residue (T32) and a (\n                    <jats:italic>R<\/jats:italic>\n                    )\u2010selective amine transaminase\u2010specific histidine residue (H25). While Micau5708 shows only ADCL activity, substitution H25R introduces transamination activity, preserving ADCL activity. The 1.85\u2009\u00c5 resolution crystal structure of Micau5708 in complex with substrate analog chorismate provides the first direct visualization of substrate binding in an ADCL active site. Site\u2010directed mutagenesis, together with comparative analysis of DATAs of group II demonstrates that ADCL\/DATA catalytic promiscuity is enabled by a specific amino acid combination in the active site: phenylalanine, threonine, and arginine residues (F30, T32, and R87), and arginine at position 25 with a flexible side chain. Furthermore, the Micau5708\u2013chorismite complex structure has helped revise the catalytic mechanism of ADCLs, demonstrating the T32 assistance in protonation of the oxygen atom rather than the\n                    <jats:italic>\u03b2<\/jats:italic>\n                    \u2010methylene carbon of the leaving enol\u2010pyruvate. Together, these findings provide new insights into the structural basis of reaction specificity, catalytic promiscuity, and evolutionary plasticity within the PLP fold type IV enzyme superfamily. They also highlight the limitations of sequence\u2010based functional prediction.\n                  <\/jats:p>","DOI":"10.1002\/pro.70813","type":"journal-article","created":{"date-parts":[[2026,9,30]],"date-time":"2026-09-30T11:16:23Z","timestamp":1790766983000},"update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":0,"title":["Structural and mechanistic insights into catalytic promiscuity of\n                    <scp>PLP<\/scp>\n                    \u2010dependent enzymes of fold type\n                    <scp>IV<\/scp>\n                    : A case study of aminodeoxychorismate lyase from\n                    <i>Micromonospora aurantiaca<\/i>"],"prefix":"10.1002","volume":"35","author":[{"ORCID":"https:\/\/orcid.org\/0000-0002-3884-3893","authenticated-orcid":false,"given":"Alina K.","family":"Bakunova","sequence":"first","affiliation":[{"name":"Bach Institute of Biochemistry Research Centre of Biotechnology of the Russian Academy of Sciences  Moscow Russia"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-6297-8392","authenticated-orcid":false,"given":"Ilya O.","family":"Matyuta","sequence":"additional","affiliation":[{"name":"Bach Institute of Biochemistry Research Centre of Biotechnology of the Russian Academy of Sciences  Moscow Russia"},{"name":"Moscow Center for Advanced Studies  Moscow Russia"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-4089-3697","authenticated-orcid":false,"given":"Mikhail E.","family":"Minyaev","sequence":"additional","affiliation":[{"name":"N.D. Zelinsky Institute of Organic Chemistry Russian Academy of Sciences  Moscow Russia"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-8229-189X","authenticated-orcid":false,"given":"Konstantin M.","family":"Boyko","sequence":"additional","affiliation":[{"name":"Bach Institute of Biochemistry Research Centre of Biotechnology of the Russian Academy of Sciences  Moscow Russia"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-0133-7962","authenticated-orcid":false,"given":"Vladimir O.","family":"Popov","sequence":"additional","affiliation":[{"name":"Bach Institute of Biochemistry Research Centre of Biotechnology of the Russian Academy of Sciences  Moscow Russia"},{"name":"Department of Biology Lomonosov Moscow State University  Moscow Russia"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-4954-7547","authenticated-orcid":false,"given":"Ekaterina Yu.","family":"Bezsudnova","sequence":"additional","affiliation":[{"name":"Bach Institute of Biochemistry Research Centre of Biotechnology of the Russian Academy of Sciences  Moscow 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