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The <jats:styled-content style=\"fixed-case\">EnvD<\/jats:styled-content> gene is carried on the <jats:styled-content style=\"fixed-case\"><jats:italic>P<\/jats:italic><\/jats:styled-content><jats:italic>.\u2009noertemanii<\/jats:italic> genome but co\u2010culture is required for the elaboration of <jats:styled-content style=\"fixed-case\">PDGA<\/jats:styled-content> depolymerase activity. <jats:styled-content style=\"fixed-case\">EnvD<\/jats:styled-content> showed strong sequence homology to dienelactone hydrolases from other <jats:styled-content style=\"fixed-case\">G<\/jats:styled-content>ram\u2010negative bacteria, possessed no general protease activity but cleaved \u03b3\u2010links in both <jats:sc>d<\/jats:sc>\u2010 and <jats:sc>l<\/jats:sc>\u2010glutamic acid\u2010containing polymers. The stability at 37\u00b0<jats:styled-content style=\"fixed-case\">C<\/jats:styled-content> was markedly superior to that of <jats:styled-content style=\"fixed-case\">CapD<\/jats:styled-content>, a \u03b3\u2010glutamyltranspeptidase with <jats:styled-content style=\"fixed-case\">PDGA<\/jats:styled-content> depolymerase activity. Recombinant <jats:styled-content style=\"fixed-case\">EnvD<\/jats:styled-content> was recovered from inclusion bodies in soluble form from an <jats:styled-content style=\"fixed-case\"><jats:italic>E<\/jats:italic><\/jats:styled-content><jats:italic>scherichia coli<\/jats:italic> expression vector and the enzyme stripped the <jats:styled-content style=\"fixed-case\">PDGA<\/jats:styled-content> capsule from the surface of <jats:styled-content style=\"fixed-case\"><jats:italic>B<\/jats:italic><\/jats:styled-content><jats:italic>.\u2009anthracis<\/jats:italic>\u2005<jats:styled-content style=\"fixed-case\">P<\/jats:styled-content>asteur within 5\u2009min. We conclude from this <jats:italic>in vitro<\/jats:italic> study that <jats:styled-content style=\"fixed-case\">rEnvD<\/jats:styled-content> shows promise as a potential therapeutic for the treatment of anthrax.<\/jats:p>","DOI":"10.1111\/mmi.12523","type":"journal-article","created":{"date-parts":[[2014,1,16]],"date-time":"2014-01-16T11:55:51Z","timestamp":1389873351000},"page":"1136-1147","source":"Crossref","is-referenced-by-count":12,"title":["A poly\u2010\u03b3\u2010<scp>d<\/scp>\u2010glutamic acid depolymerase that degrades the protective capsule of <scp><i>B<\/i><\/scp><i>acillus anthracis<\/i>"],"prefix":"10.1111","volume":"91","author":[{"given":"David","family":"Negus","sequence":"first","affiliation":[{"name":"University College London School of Pharmacy  29\u201039 Brunswick Square London WC1N 1AX UK"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Peter W.","family":"Taylor","sequence":"additional","affiliation":[{"name":"University College London School of 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