| Genetic and Chemical Characterization of Ibuprofen Degradation by Sphingomonas Ibu-2. | |
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MedLine Citation:
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PMID: 23329679 Owner: NLM Status: Publisher |
Abstract/OtherAbstract:
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Sphingomonas Ibu-2 has the unusual ability to cleave the acid side chain from the pharmaceutical ibuprofen and related arylacetic acid derivatives to yield corresponding catechols under aerobic conditions via a previously uncharacterized mechanism. Screening a chromosomal library of Ibu-2 DNA in Escherichia coli EPI300 allowed us to identify one fosmid clone (pFOS3G7) that conferred the ability to metabolize ibuprofen to isobutylcatechol. Characterization of pFOS3G7 loss-of-function transposon mutants permitted identification of five open reading frames, ipfABDEF, whose predicted amino acid sequences bore similarity to the large and small units of an aromatic dioxygenase (ipfAB), an SCPx thiolase (ipfD), a domain of unknown function 35 (DUF35) protein (ipfE), and an aromatic coenzyme A ligase (ipfF). Two additional open reading frames, ipfH and ipfI, which encode putative ferredoxin reductase and ferredoxin components of an aromatic dioxygenase system respectively, were also identified on pFOS3G7. Complementation of a markerless loss-of-function ipfD deletion mutant restored catechol production as did complementation of the ipfF Tn mutant. Expression of subcloned ipfABDEF alone in E. coli did not impart full metabolic activity unless co-expressed with ipfHI. CoA ligation followed by ring oxidation is common to phenylacetic acid pathways. However, the need for a putative SCPx thiolase (IpfD) and DUF35 protein (IpfE) in aerobic arylacetic acid degradation is unprecedented. This work provides preliminary insights into the mechanism behind this novel arylacetic acid deacylating, catechol-generating activity. |
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Authors:
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Robert W Murdoch; Anthony G Hay |
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Publication Detail:
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Type: JOURNAL ARTICLE Date: 2013-1-17 |
Journal Detail:
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Title: Microbiology (Reading, England) Volume: - ISSN: 1465-2080 ISO Abbreviation: Microbiology (Reading, Engl.) Publication Date: 2013 Jan |
Date Detail:
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Created Date: 2013-1-18 Completed Date: - Revised Date: - |
Medline Journal Info:
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Nlm Unique ID: 9430468 Medline TA: Microbiology Country: - |
Other Details:
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Languages: ENG Pagination: - Citation Subset: - |
Affiliation:
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Middle East Technical University; |
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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