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Widespread occurrence of ATP:citrate lyase and carnitine acetyltransferase in filamentous fungi

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Abstract

Ten filamentous fungi, belonging to five different genera of both higher and lower fungi, including oleaginous fungi and fungi known to produce secondary metabolites, all possessed both ATP:citrate lyase (17–84nmol min−1 (mg protein)−1) and carnitine acetyltransferase activity (9–62nmol min−1 (mg protein)−1). The possession of these two enzymes appears to be a common feature in filamentous fungi.

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References

  • Attwood, M.M. 1973 ATP-citrate lyase activity in fungal extracts. Antonie van Leewenhoek 39, 539–544.

    Google Scholar 

  • Botham, P.A. & Ratledge, C. 1979 A biochemical explanation for lipid accumulation in Candida 107 and other oleaginous micro-organisms, Journal of General Microbiology 114, 361–375.

    Google Scholar 

  • Boulton, C.A. & Ratledge, C. 1983 Partial purification and some properties of ATP:citrate lyase from the oleaginous yeast Lipomyces starkeyi. Journal of General Microbiology 129, 2863–2869.

    Google Scholar 

  • Henriksen, C.M., Christensen, L.H., Neilsen, J. & Villadsen, J. 1996 Growth energetics and metabolic fluxes in continuous cultures of Penicillium chrysogenum. Journal of Biotechnology 45, 149–164.

    Google Scholar 

  • Kawamoto, S., Ueda, M., Nozaki, C., Yamamura, M., Tanaka, A & Fukui, S. 1978 Localization of carnitine acetyltransferase in peroxisomes and in mitochondria of n alkane grown Candida tropicalis. FEBS Letters 96, 37–40.

    Google Scholar 

  • Kendrick, A. & Ratledge, C. 1992 Lipids of selected molds grown for the production of n-3 and n-6 polyunsaturated fatty acids. Lipids 27, 15–20.

    Google Scholar 

  • Kohlaw, G.B. & Tan-Wilson, A. 1977 Carnitine acetyltransferase: Candidate for the transfer of acetyl groups through the mitochondrial membrane of yeast. Journal of Bacteriology 129, 1159–1161.

    Google Scholar 

  • McCullough, W., Roberts, C.F., Osmani, S.A. & Scrutton, M.C. 1986 Regulation of carbon metabolism in filamentous fungi. In Carbohydrate Metabolism in Cultured Cells, ed Morgan, M.J. New York and London: Plenum Press. pp. 287–355.

    Google Scholar 

  • Midgley, M. 1993 Carnitine acetyltransferase is absent from acuJ mutants of Aspergillus nidulans. FEMS Microbiology Letters 108, 7–10.

    Google Scholar 

  • Pfitzner, A., Kubicek, C.P., & Rohr, M. 1987 Presence and regulation of ATP:citrate lyase from the citric acid-producing fungus Aspergillus niger. Archives of Microbiology 147, 88–91.

    Google Scholar 

  • Pitt, D. & Mosley, M.J. 1986 Oxidation of carbon sources via the tricarboxylic acid cycle during calcium induced conidiation of Penicillium notatum. Antonie van Leewenhoek 52, 467–482.

    Google Scholar 

  • Ratledge, C. & Gilbert, S.C. 1985 Carnitine acetyltransferase activity in oreagenous yeasts. FEMS Microbiology Letters 27, 273–275.

    Google Scholar 

  • Shashi, K., Bachhawat, A.K. & Joseph, R. 1990 ATP:citrate lyase of Rhodotorula gracilis: Purification and properties. Biochimica et Biophysica Acta 1033, 23–30.

    Google Scholar 

  • Srere, P.A. 1959 The citrate cleavage enzyme. I distribution and purification. Journal of Biological Chemistry 234, 2544–2547.

    Google Scholar 

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Correspondence to J.P. Wynn.

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Wynn, J., Hamid, A., Midgley, M. et al. Widespread occurrence of ATP:citrate lyase and carnitine acetyltransferase in filamentous fungi. World Journal of Microbiology and Biotechnology 14, 145–147 (1997). https://doi.org/10.1023/A:1008853306972

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  • DOI: https://doi.org/10.1023/A:1008853306972

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