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dc.contributor.authorRehm, BHA
dc.contributor.authorKruger, N
dc.contributor.authorSteinbuchel, A
dc.date.accessioned2018-04-20T03:51:46Z
dc.date.available2018-04-20T03:51:46Z
dc.date.issued1998
dc.identifier.issn0021-9258
dc.identifier.doi10.1074/jbc.273.37.24044
dc.identifier.urihttp://hdl.handle.net/10072/373500
dc.description.abstractTo investigate the metabolic link between fatty acid de novo synthesis and polyhydroxyalkanoic acid (PHA) synthesis, we isolated mutants of Pseudomonas putida KT2440 deficient in this metabolic route. The gene phaG was cloned by phenotypic complementation of these mutants; it encoded a protein of 295 amino acids with a molecular mass of 33,876 Da, and the amino acid sequence exhibited 44% amino acid identity to the primary structure of the rhlA gene product, which is involved in the rhamnolipid biosynthesis in Pseudomonas aeruginosa PG201. S1 nuclease protection assay identified the transcriptional start site 239 base pairs upstream of the putative translational start codon. Transcriptional induction of phaG was observed when gluconate was provided, and PHA synthesis occurred from this carbon source. No complementation of the rhlA mutant P. aeruginosa UO299-harboring plasmid pBHR81, expressingphaG gene under lac promoter control, was obtained. Heterologous expression of phaG inPseudomonas oleovorans, which is not capable of PHA synthesis from gluconate, enabled PHA synthesis on gluconate as the carbon source. Native recombinant PhaG was purified by native polyacrylamide gel electrophoresis from P. oleovorans-harboring plasmid pBHR81. It catalyzes the transfer of the acyl moiety from in vitro synthesized 3-hydroxydecanoyl-CoA to acyl carrier protein, indicating that PhaG exhibits a 3-hydroxyacyl-CoA-acyl carrier protein transferase activity.
dc.description.peerreviewedYes
dc.languageEnglish
dc.publisherThe American Society for Biochemistry and Molecular Biology Inc
dc.relation.ispartofpagefrom24044
dc.relation.ispartofpageto24051
dc.relation.ispartofissue37
dc.relation.ispartofjournalJournal of Biological Chemistry
dc.relation.ispartofvolume273
dc.subject.fieldofresearchBiochemistry and Cell Biology not elsewhere classified
dc.subject.fieldofresearchChemical Sciences
dc.subject.fieldofresearchBiological Sciences
dc.subject.fieldofresearchMedical and Health Sciences
dc.subject.fieldofresearchcode060199
dc.subject.fieldofresearchcode03
dc.subject.fieldofresearchcode06
dc.subject.fieldofresearchcode11
dc.titleA new metabolic link between fatty acid de novo synthesis and polyhydroxyalkanoic acid synthesis. The phaG gene from Pseudomonas putida KT2440 encodes a 3-hydroxyacyl-acyl carrier protein-coenzyme a transferase
dc.typeJournal article
dc.type.descriptionC1 - Articles
dc.type.codeC - Journal Articles
dc.description.versionPublished
gro.rights.copyrightThis research was originally published in Journal of Biological Chemistry (JBC). Bernd H. A. Rehm, Niels Krüger and Alexander Steinbüchel, A New Metabolic Link between Fatty Acid de NovoSynthesis and Polyhydroxyalkanoic Acid Synthesis THE PHAG GENE FROM PSEUDOMONAS PUTIDAKT2440 ENCODES A 3-HYDROXYACYL-ACYL CARRIER PROTEIN-COENZYME A TRANSFERASE Journal of Biological Chemistry (JBC), Vol. 273 (37), pp. 24044-24051, 1998. Copyright the American Society for Biochemistry and Molecular Biology. Reproduced in accordance with the copyright policy of the publisher. Please refer to the journal's website for access to the definitive version.
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gro.griffith.authorRehm, Bernd


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