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Two different pathways are involved in the beta-oxidation of n-alkanoic and n-phenylalkanoic acids in Pseudomonas putida U: genetic studies and biotechnological applications

AutorOlivera, Elías R.; Carnicero, David; García, Belén; Miñambres Rodríguez, Baltasar ; Moreno, Miguel A.; Cañedo, Librada M.; Dirusso, Concetta C.; Naharro, Germán; Luengo, José M.
Palabras clavePhenylacetyl-coa catabolon
Transcription factor fadr
Gram-negative bacteria
Coenzyme-a synthetase
Fed-batch culture
Multienzyme complex
Fragi B-0771
Fecha de publicación2001
EditorBlackwell Publishing
CitaciónMolecular microbiology 39(4): 863-874 (2001)
ResumenIn Pseudomonas putida U, the degradation of n-alkanoic and n-phenylalkanoic acids is carried out by two sets of beta-oxidation enzymes (betaI and betaII). Whereas the first one (called betaI) is constitutive and catalyses the degradation of n-alkanoic and n-phenylalkanoic acids very efficiently, the other one (betaII), which is only expressed when some of the genes encoding betaI enzymes are mutated, catabolizes n-phenylalkanoates (n > 4) much more slowly. Genetic studies revealed that disruption or deletion of some of the betaI genes handicaps the growth of P. putida U in media containing n-alkanoic or n-phenylalkanoic acids with an acyl moiety longer than C4. However, all these mutants regained their ability to grow in media containing n-alkanoates as a result of the induction of betaII, but they were still unable to catabolize n-phenylalkanoates completely, as the betaI-FadBA enzymes are essential for the beta-oxidation of certain n-phenylalkanoyl-CoA derivatives when they reach a critical size. Owing to the existence of the betaII system, mutants lacking betaIfadB/A are able to synthesize new poly 3-OH-n-alkanoates (PHAs) and poly 3-OH-n-phenylalkanoates (PHPhAs) efficiently. However, they are unable to degrade these polymers, becoming bioplastic overproducer mutants. The genetic and biochemical importance of these results is reported and discussed.
Descripción12 pages, 4 figures.-- PMID: 11251808 [PubMed].
Versión del editorhttp://dx.doi.org/10.1046/j.1365-2958.2001.02296.x
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