Literature DB >> 11251808

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.

E R Olivera1, D Carnicero, B García, B Miñambres, M A Moreno, L Cañedo, C C Dirusso, G Naharro, J M Luengo.   

Abstract

In 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.

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Year:  2001        PMID: 11251808     DOI: 10.1046/j.1365-2958.2001.02296.x

Source DB:  PubMed          Journal:  Mol Microbiol        ISSN: 0950-382X            Impact factor:   3.501


  16 in total

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Authors:  Beatrix Tettmann; Andreas Dötsch; Olivier Armant; Christopher D Fjell; Joerg Overhage
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5.  Fatty Acid Oxidation Is Required for Myxococcus xanthus Development.

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9.  FadD from Pseudomonas putida CA-3 is a true long-chain fatty acyl coenzyme A synthetase that activates phenylalkanoic and alkanoic acids.

Authors:  Aisling R Hume; Jasmina Nikodinovic-Runic; Kevin E O'Connor
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10.  YfcX enables medium-chain-length poly(3-hydroxyalkanoate) formation from fatty acids in recombinant Escherichia coli fadB strains.

Authors:  Kristi D Snell; Feng Feng; Luhua Zhong; David Martin; Lara L Madison
Journal:  J Bacteriol       Date:  2002-10       Impact factor: 3.490

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