<HashMap><database>biostudies-literature</database><scores/><additional><submitter>Li Y</submitter><funding>Key Research Program of Frontier Sciences, Chinese Academy of Sciences</funding><funding>Biological Resources Program, Chinese Academy of Sciences</funding><funding>National Natural Science Foundation of China</funding><funding>China Postdoctoral Science Foundation</funding><funding>National Key Research and Development Program of China</funding><pagination>1001</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC9605436</full_dataset_link><repository>biostudies-literature</repository><omics_type>Unknown</omics_type><volume>8(10)</volume><pubmed_abstract>Nonribosomal peptide synthetase (NRPS)-like enzymes containing A-T-R domain architecture are also known as carboxylate reductases (CARs) for aldehyde generation. To identify new members of CARs, we established a virtual library containing 84 fungal CARs distributed in seven distinct clades by genome mining and phylogenetic analysis. Nine CARs, including PnlA from &lt;i>Pestalotiopsis fici&lt;/i> and eight known CARs, were clustered in clade VI and proposed to catalyze the reduction of nonreducing polyketide synthase (NR-PKS)-derived aryl carboxylic acids. The recombinant protein PnlA was overproduced and purified to apparent homogeneity from &lt;i>Saccharomyces cerevisiae&lt;/i>. In vitro enzyme assays of PnlA with 28 different benzoic acid derivatives (&lt;b>1&lt;/b>-&lt;b>28&lt;/b>) revealed the corresponding a</pubmed_abstract><journal>Journal of fungi (Basel, Switzerland)</journal><pubmed_title>Characterization of a NRPS-like Protein from &lt;i>Pestalotiopsis fici&lt;/i> for Aldehyde Generation.</pubmed_title><pmcid>PMC9605436</pmcid><funding_grant_id>KFJ-BRP-009-005</funding_grant_id><funding_grant_id>31861133004</funding_grant_id><funding_grant_id>2022T150689</funding_grant_id><funding_grant_id>YJ20200201</funding_grant_id><funding_grant_id>2021M693362</funding_grant_id><funding_grant_id>YJ20200309</funding_grant_id><funding_grant_id>ZDBS-LY-SM016</funding_grant_id><funding_grant_id>2020YFA0907800</funding_grant_id><funding_grant_id>2020M680720</funding_grant_id><pubmed_authors>Li Y</pubmed_authors><pubmed_authors>Wei PL</pubmed_authors><pubmed_authors>Yin WB</pubmed_authors><pubmed_authors>Fan J</pubmed_authors><pubmed_authors>Ran H</pubmed_authors></additional><is_claimable>false</is_claimable><name>Characterization of a NRPS-like Protein from &lt;i>Pestalotiopsis fici&lt;/i> for Aldehyde Generation.</name><description>Nonribosomal peptide synthetase (NRPS)-like enzymes containing A-T-R domain architecture are also known as carboxylate reductases (CARs) for aldehyde generation. To identify new members of CARs, we established a virtual library containing 84 fungal CARs distributed in seven distinct clades by genome mining and phylogenetic analysis. Nine CARs, including PnlA from &lt;i>Pestalotiopsis fici&lt;/i> and eight known CARs, were clustered in clade VI and proposed to catalyze the reduction of nonreducing polyketide synthase (NR-PKS)-derived aryl carboxylic acids. The recombinant protein PnlA was overproduced and purified to apparent homogeneity from &lt;i>Saccharomyces cerevisiae&lt;/i>. In vitro enzyme assays of PnlA with 28 different benzoic acid derivatives (&lt;b>1&lt;/b>-&lt;b>28&lt;/b>) revealed the corresponding a</description><dates><release>2022-01-01T00:00:00Z</release><publication>2022 Sep</publication><modification>2025-04-19T12:07:57.636Z</modification><creation>2025-04-19T12:07:57.636Z</creation></dates><accession>S-EPMC9605436</accession><cross_references><pubmed>36294566</pubmed><doi>10.3390/jof8101001</doi></cross_references></HashMap>