{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,4,23]],"date-time":"2026-04-23T10:35:07Z","timestamp":1776940507692,"version":"3.51.4"},"reference-count":55,"publisher":"Wiley","issue":"2","license":[{"start":{"date-parts":[[2005,3,3]],"date-time":"2005-03-03T00:00:00Z","timestamp":1109808000000},"content-version":"vor","delay-in-days":4110,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["European Journal of Biochemistry"],"published-print":{"date-parts":[[1993,12]]},"abstract":"<jats:p>Four different DNA fragments each coding for poly(hydroxyalkanoic acid) depolymerase (<jats:italic>phaZ1\u2013phaZ4<\/jats:italic>) were isolated in pUC plasmids from a genomic library of <jats:italic>Pseudomonas lemoignei<\/jats:italic> in <jats:italic>Escherichia coli<\/jats:italic>. All recombinant strains secreted a highly active poly(3\u2010hydroxybutyric acid) depolymerase and produced large translucent halos on an opaque medium containing poly(3\u2010hydroxybutyric acid) granules. One DNA region (<jats:italic>phaZ1<\/jats:italic>) was present in seven independently isolated clones. Three other cloned DNA fragments were different from <jats:italic>phaZ1<\/jats:italic> and from each other (<jats:italic>phaZ2\u2013phaZ4<\/jats:italic>). In <jats:italic>phaZ1<\/jats:italic>, an open\u2010reading frame of 1245 bp was identified from the nucleotide sequence of a 5435\u2010bp <jats:italic>Mbo<\/jats:italic>I fragment (57 mol G+C\/100 mol) of this region and encoded a novel poly(hydroxyalkanoic acid) depolymerase of <jats:italic>P. lemoignei<\/jats:italic>, poly(3\u2010hydroxybutyric acid) depolymerase C. A leader\u2010sequence peptidase\u2010cleavage site was predicted from the deduced amino acid sequence between Ala37 and Leu38. The calculated relative molecular masses of the precursor and the putative mature protein were 43468 and 39581, respectively. The polypeptide contains a lipase consensus sequence (Gly\u2010Xaa\u2010Ser\u2010Xaa\u2010Gly) and an unusually high proportion of threonine residues (22 of 36 amino acids) near the C\u2010terminus. The N\u2010terminus of the deduced amino acid sequence of PhaZ1 differed from that of the purified poly(3\u2010hydroxybutyric acid) depolymerases A, B and the poly(3\u2010hydroxyvaleric acid) depolymerase of <jats:italic>P. lemoignei<\/jats:italic>.<\/jats:p><jats:p>The <jats:italic>phaZ1<\/jats:italic> gene product, poly(3\u2010hydroxybutyric acid) depolymerase C, was partially purified from recombinant <jats:italic>E. coli<\/jats:italic> (pUC91 ::<jats:italic>phaZ1<\/jats:italic>). The purified protein was specific for poly(hydroxyalkanoic acid) consisting of monomers of four or five carbon atoms and for <jats:italic>p<\/jats:italic>\u2010nithrophenylbutyrate as substrates. The polymer\u2010hydrolyzing activity, but not the <jats:italic>p<\/jats:italic>\u2010nitrophenylate esterase activity, was inhibited by complex media such as Luria\u2010Bertani medium and by soluble <jats:italic>E. coli<\/jats:italic> proteins. The enzyme protein did not cross\u2010react with antibodies raised against purified poly(3\u2010hydroxyvaleric acid) depolymerase of <jats:italic>P. lemoignei.<\/jats:italic><\/jats:p>","DOI":"10.1111\/j.1432-1033.1993.tb18424.x","type":"journal-article","created":{"date-parts":[[2005,3,4]],"date-time":"2005-03-04T10:02:52Z","timestamp":1109930572000},"page":"701-710","source":"Crossref","is-referenced-by-count":81,"title":["Cloning and characterization of the poly(hydroxyalkanoic acid)\u2010depolymerase gene locus, <i>phaZ1<\/i>, of <i>Pseudomonas lemoignei<\/i> and its gene product"],"prefix":"10.1111","volume":"218","author":[{"given":"Dieter","family":"JENDROSSEK","sequence":"first","affiliation":[]},{"given":"Beate","family":"M\u00dcLLER","sequence":"additional","affiliation":[]},{"given":"Hans G\u00fcnter","family":"SCHLEGEL","sequence":"additional","affiliation":[]}],"member":"311","published-online":{"date-parts":[[2005,3,3]]},"reference":[{"key":"e_1_2_2_2_1","doi-asserted-by":"crossref","first-page":"450","DOI":"10.1128\/mr.54.4.450-472.1990","article-title":"Occurrence, metabolism, metabolic role, and industrial use of bacterial polyhydroxyalkanoates","volume":"54","author":"Anderson A. 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