%0 Journal Article %1 citeulike:840781 %A Kirner, S. %A Krauss, S. %A Sury, G. %A Lam, S. T. %A Ligon, J. M. %A van Pée, K. H. %C Institut f��r Mikrobiologie, Universit��t Hohenheim, Stuttgart, Germany. %D 1996 %J Microbiology %K natural-products nitro-compounds biosynthesis %P 2129--2135 %T The non-haem chloroperoxidase from Pseudomonas fluorescens and its relationship to pyrrolnitrin biosynthesis. %U http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=8760926 %V 142 ( Pt 8) %X The non-haem chloroperoxidase gene (cpoF) from the pyrrolnitrin producer Pseudomonas fluorescens BL914 was cloned using an oligonucleotide derived from part of the N-terminal amino acid sequence of chloroperoxidase (CPO-P) from Pseudomonas pyrrocina as a probe. Based on the overexpression of cpoF in Escherichia coli and the stability of CPO-F against higher temperatures and proteases, the enzyme was purified to homogeneity. Partial characterization of the enzyme showed that it belongs to the class of bacterial non-haem CPOs. To investigate the role of CPO-F in pyrrolnitrin biosynthesis, the cpoF gene was inactivated by insertion of a kanamycin cassette. Exchange of the chromosomal cpoF gene against the disrupted copy had no influence on pyrrolnitrin production demonstrating that CPO-F was not involved in pyrrolnitrin biosynthesis.

@article{citeulike:840781, abstract = {The non-haem chloroperoxidase gene (cpoF) from the pyrrolnitrin producer Pseudomonas fluorescens BL914 was cloned using an oligonucleotide derived from part of the N-terminal amino acid sequence of chloroperoxidase (CPO-P) from Pseudomonas pyrrocina as a probe. Based on the overexpression of cpoF in Escherichia coli and the stability of CPO-F against higher temperatures and proteases, the enzyme was purified to homogeneity. Partial characterization of the enzyme showed that it belongs to the class of bacterial non-haem CPOs. To investigate the role of CPO-F in pyrrolnitrin biosynthesis, the cpoF gene was inactivated by insertion of a kanamycin cassette. Exchange of the chromosomal cpoF gene against the disrupted copy had no influence on pyrrolnitrin production demonstrating that CPO-F was not involved in pyrrolnitrin biosynthesis.}, added-at = {2007-02-02T11:54:15.000+0100}, address = {Institut f��r Mikrobiologie, Universit��t Hohenheim, Stuttgart, Germany.}, author = {Kirner, S. and Krauss, S. and Sury, G. and Lam, S. T. and Ligon, J. M. and van P{\'{e}}e, K. H.}, biburl = {https://www.bibsonomy.org/bibtex/2f7e86f6ac62febd28df83a283a8b5bc4/robert}, citeulike-article-id = {840781}, interhash = {7d7d1b3d7d8ee3eaa71cd843488905f9}, intrahash = {f7e86f6ac62febd28df83a283a8b5bc4}, issn = {1350-0872}, journal = {Microbiology}, keywords = {natural-products nitro-compounds biosynthesis}, month = {August}, pages = {2129--2135}, priority = {2}, timestamp = {2007-02-02T11:54:15.000+0100}, title = {The non-haem chloroperoxidase from \textit{Pseudomonas fluorescens} and its relationship to pyrrolnitrin biosynthesis.}, url = {http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve\&db=pubmed\&dopt=Abstract\&list_uids=8760926}, volume = {142 ( Pt 8)}, year = 1996 }