<?xml version="1.0" encoding="utf-8"?>
<export-example>
  <doc>
    <id>20669</id>
    <completedYear/>
    <publishedYear>2017</publishedYear>
    <thesisYearAccepted/>
    <language>eng</language>
    <pageFirst>16989</pageFirst>
    <pageLast>67</pageLast>
    <pageNumber>16985</pageNumber>
    <edition/>
    <issue/>
    <volume>23</volume>
    <type>articler</type>
    <publisherName/>
    <publisherPlace/>
    <creatingCorporation/>
    <contributingCorporation/>
    <belongsToBibliography>0</belongsToBibliography>
    <completedDate>2017-12-01</completedDate>
    <publishedDate>--</publishedDate>
    <thesisDateAccepted>--</thesisDateAccepted>
    <title language="eng">Fatty Acid Chain Shortening by a Fungal Peroxygenase</title>
    <abstract language="eng">A recently discovered peroxygenase from the&#13;
fungus Marasmius rotula (MroUPO) is able to catalyze the&#13;
progressive one-carbon shortening of medium and longchain mono- and dicarboxylic acids by itself alone, in the presence of H₂O₂. The mechanism, analyzed using H₂O, starts with an a-oxidation catalyzed by MroUPO generat- ing an α-hydroxy acid, which is further oxidized by the enzyme to a reactive α-keto intermediate whose decarboxylation yields the one-carbon shorter fatty acid. Compared with the previously characterized peroxygenase of Agrocybe aegerita, a wider heme access channel, enabling fatty acid positioning with the carboxylic end near the heme cofactor (as seen in one of the crystal structures available) could be at the origin of the unique ability of MroUPO shortening carboxylic acid chains.</abstract>
    <parentTitle language="eng">Chemistry A European Journal</parentTitle>
    <identifier type="doi">10.1002/chem.201704773</identifier>
    <identifier type="issn">1521-3765</identifier>
    <identifier type="issn">0947-6539</identifier>
    <enrichment key="BTU">an der BTU erstellt / created at BTU</enrichment>
    <enrichment key="review.accepted_by">2</enrichment>
    <author>
      <firstName>Andrés</firstName>
      <lastName>Olmedo</lastName>
    </author>
    <submitter>
      <firstName>Kai-Uwe</firstName>
      <lastName>Schmidtke</lastName>
    </submitter>
    <author>
      <firstName>José C. del</firstName>
      <lastName>Río</lastName>
    </author>
    <author>
      <firstName>Jan</firstName>
      <lastName>Kiebist</lastName>
    </author>
    <author>
      <firstName>René</firstName>
      <lastName>Ullrich</lastName>
    </author>
    <author>
      <firstName>Martin</firstName>
      <lastName>Hofrichter</lastName>
    </author>
    <author>
      <firstName>Katrin</firstName>
      <lastName>Scheibner</lastName>
    </author>
    <author>
      <firstName>Angel T.</firstName>
      <lastName>Martínez</lastName>
    </author>
    <author>
      <firstName>Ana</firstName>
      <lastName>Gutiérrez</lastName>
    </author>
    <subject>
      <language>eng</language>
      <type>uncontrolled</type>
      <value>Peroxygenase</value>
    </subject>
    <collection role="institutes" number="2111">FG Enzymtechnologie</collection>
  </doc>
  <doc>
    <id>22919</id>
    <completedYear/>
    <publishedYear>2018</publishedYear>
    <thesisYearAccepted/>
    <language>eng</language>
    <pageFirst>3964</pageFirst>
    <pageLast>3968</pageLast>
    <pageNumber/>
    <edition/>
    <issue>18</issue>
    <volume>10</volume>
    <type>articler</type>
    <publisherName/>
    <publisherPlace/>
    <creatingCorporation/>
    <contributingCorporation/>
    <belongsToBibliography>0</belongsToBibliography>
    <completedDate>2018-12-18</completedDate>
    <publishedDate>--</publishedDate>
    <thesisDateAccepted>--</thesisDateAccepted>
    <title language="eng">Selective Epoxidation of Fatty Acids and Fatty Acid Methyl Esters by Fungal Peroxygenases</title>
    <abstract language="eng">Recently discovered fungal unspecific peroxygenases from Marasmius rotula and Chaetomium globosum catalyze the epoxidation of unsaturated fatty acids (FA) and FA methyl esters (FAME), unlike the well‐known peroxygenases from Agrocybe aegerita and Coprinopsis cinerea. Reactions of a series of unsaturated FA and FAME with cis‐configuration revealed high (up to 100 %) substrate conversion and selectivity towards epoxidation, although some significant differences were observed between enzymes and substrates with the best results being obtained with the C. globosum enzyme. This and the M. rotula peroxygenase appear as promising biocatalysts for the environmentally‐friendly production of reactive FA epoxides given their self‐sufficient monooxygenase activity and the high conversion rate and epoxidation selectivity.</abstract>
    <parentTitle language="eng">CHEMCATCHEM</parentTitle>
    <identifier type="doi">10.1002/cctc.201800849</identifier>
    <identifier type="issn">1867-3899</identifier>
    <enrichment key="BTU">an der BTU erstellt / created at BTU</enrichment>
    <author>
      <firstName>Carmen</firstName>
      <lastName>Aranda</lastName>
    </author>
    <submitter>
      <firstName>Kai-Uwe</firstName>
      <lastName>Schmidtke</lastName>
    </submitter>
    <author>
      <firstName>Andrés</firstName>
      <lastName>Olmedo</lastName>
    </author>
    <author>
      <firstName>Jan</firstName>
      <lastName>Kiebist</lastName>
    </author>
    <author>
      <firstName>Katrin</firstName>
      <lastName>Scheibner</lastName>
    </author>
    <author>
      <firstName>José C. del</firstName>
      <lastName>Río</lastName>
    </author>
    <author>
      <firstName>Angel T.</firstName>
      <lastName>Martínez</lastName>
    </author>
    <author>
      <firstName>Ana</firstName>
      <lastName>Gutiérrez</lastName>
    </author>
    <subject>
      <language>eng</language>
      <type>uncontrolled</type>
      <value>Peroxygenase</value>
    </subject>
    <collection role="institutes" number="2111">FG Enzymtechnologie</collection>
  </doc>
</export-example>
