Repercussion of a deficiency in mitochondrial ß-oxidation on the carbon flux of short-chain fatty acids to the peroxisomal ß-oxidation cycle in Aspergillus nidulans

Magliano, Pasqualina; Sanglard, Dominique; Poirier, Yves

doi:10.1016/j.bbalip.2010.08.008

Cited by 5 publications

(2 citation statements)

References 33 publications

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“…For example, A. nidulans contains at least eight proteins with similarity to acyl-CoA dehydrogenases containing PTS1 sequences, in addition to two peroxisomal acylCoA oxidases, AoxA and AoxB (28). Genes other than foxA are also known in A. nidulans that might encode enzymes with enoyl-CoA hydratase and/or 3-hydroxyacyl-CoA dehydrogenase activity (27,34).…”

Section: Discussionmentioning

confidence: 99%

Contributions of the Peroxisome and β-Oxidation Cycle to Biotin Synthesis in Fungi

Magliano

Flipphi

Arpat

et al. 2011

Journal of Biological Chemistry

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Background: Pimeloyl-CoA is an intermediate of the biotin pathway, but it is unknown how it is synthesized in fungi. Results: Aspergillus nidulans mutants in ␤-oxidation are biotin-deficient, and the enzyme utilizing pimeloyl-CoA is targeted to the peroxisome. Conclusion: Pimeloyl-CoA is synthesized in the peroxisome via the ␤-oxidation cycle in filamentous fungi. Significance: This is the first implication of peroxisomal ␤-oxidation in biotin synthesis.

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Section: Discussionmentioning

confidence: 99%

Contributions of the Peroxisome and β-Oxidation Cycle to Biotin Synthesis in Fungi

Magliano

Flipphi

Arpat

et al. 2011

Journal of Biological Chemistry

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“…In most studies conducted in cultured fish, the carnitine inclusion level in the diets range from a few hundred to above 4000 mg kg −1 diet (Chatzifotis & Takeuchi ; Harpaz ; Magliano et al . ; Yang et al . ).…”

Section: The Physicochemical Properties Of L‐carnitine and Its Generamentioning

confidence: 99%

The metabolic regulation of dietary L‐carnitine in aquaculture nutrition: present status and future research strategies

Limbu

et al. 2018

Reviews in Aquaculture

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L-carnitine is a multi-functional nutrient which plays a leading role in fatty acid metabolism in mammals and other eukaryotes. Its main physiological function is to promote fatty acid b-oxidation to produce energy, which reduces body fat content and improves body weight without affecting moisture content in whole body and muscle. In recent years, its dietary supplementation in aquaculture nutrition has been studied in different cultured species. It has been proved that L-carnitine can improve growth and increase lipid utilization rate in some aquatic animals. However, such beneficial effects of dietary L-carnitine are limited or absent in other species. The reasons for the conflicting results obtained on L-carnitine functions in aquatic animals need to be elucidated. This review explores comprehensively the different physiological functions of L-carnitine in various aquatic animals. In the end, research strategies are provided to elucidate the existing conflicts on dietary L-carnitine application in aquaculture nutrition in order to promote its utilization in aquatic feed industry.

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Engineering polyhydroxyalkanoate content and monomer composition in the oleaginous yeast Yarrowia lipolytica by modifying the ß-oxidation multifunctional protein

Haddouche

Poirier

Delessert

et al. 2011

Appl Microbiol Biotechnol

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Recombinant strains of the oleaginous yeast Yarrowia lipolytica expressing the PHA synthase gene (PhaC) from Pseudomonas aeruginosa in the peroxisome were found able to produce polyhydroxyalkanoates (PHA). PHA production yield, but not the monomer composition, was dependent on POX genotype (POX genes encoding acyl-CoA oxidases) (Haddouche et al. FEMS Yeast Res 10:917-927, 2010). In this study of variants of the Y. lipolytica β-oxidation multifunctional enzyme, with deletions or inactivations of the R-3-hydroxyacyl-CoA dehydrogenase domain, we were able to produce hetero-polymers (functional MFE enzyme) or homo-polymers (with no 3-hydroxyacyl-CoA dehydrogenase activity) of PHA consisting principally of 3-hydroxyacid monomers (>80%) of the same length as the external fatty acid used for growth. The redirection of fatty acid flux towards β-oxidation, by deletion of the neutral lipid synthesis pathway (mutant strain Q4 devoid of the acyltransferases encoded by the LRO1, DGA1, DGA2 and ARE1 genes), in combination with variant expressing only the enoyl-CoA hydratase 2 domain, led to a significant increase in PHA levels, to 7.3% of cell dry weight. Finally, the presence of shorter monomers (up to 20% of the monomers) in a mutant strain lacking the peroxisomal 3-hydroxyacyl-CoA dehydrogenase domain provided evidence for the occurrence of partial mitochondrial β-oxidation in Y. lipolytica.

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Repercussion of a deficiency in mitochondrial ß-oxidation on the carbon flux of short-chain fatty acids to the peroxisomal ß-oxidation cycle in Aspergillus nidulans

Cited by 5 publications

References 33 publications

Contributions of the Peroxisome and β-Oxidation Cycle to Biotin Synthesis in Fungi

Contributions of the Peroxisome and β-Oxidation Cycle to Biotin Synthesis in Fungi

The metabolic regulation of dietary L‐carnitine in aquaculture nutrition: present status and future research strategies

Engineering polyhydroxyalkanoate content and monomer composition in the oleaginous yeast Yarrowia lipolytica by modifying the ß-oxidation multifunctional protein

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