Effect of Antimycin A on the Glycolytic Flux in Aspergillus niger


Article Preview

This thesis chose the metabolism of energy and carbon in Aspergillus niger, the citric acid over-producting mycete, as a model system to research the principal physiological and biochemical characteristics. The effects of energy metabolism on the glycolic pathway, and the mechanism of product inhibitory in Aspergillus niger were researched in detail. The relationship between the consistence of intracellular ATP and the glycolytic flux in Aspergillus niger was investigated by adding oxidative phosphorylation inhibitor-antimycin A. When 0.4 mg/L antimycin A was added to the cell cultures, the consistence of intracellular ATP was approximately 31.96% less than that of the control. The specific activity of phosphofructokinase, one of the rate limiting enzymes of the glycolytic pathway, increased by a factor of 0.135 compared with the control. With the specific activity of phosphofructokinase increased, the rate of glucose consumed increased by a factor of 0.137, in comparison of the control. And the rate of citric acid produced increased by 16.15%. The specific activities of hexokinase were not affected by the accretion of antimycin A. These results are the first answer to the fundamental question of what controls the flux through glycolsis in Aspergillus niger.



Advanced Materials Research (Volumes 560-561)

Edited by:

Yue Li




D. P. Wang et al., "Effect of Antimycin A on the Glycolytic Flux in Aspergillus niger", Advanced Materials Research, Vols. 560-561, pp. 385-390, 2012

Online since:

August 2012




[1] Yokota, A., Henmi, M., Takaoka, N., Hayashi, C., Takezawa, Y., Fukumori, Y. and Tomita, F. (1997).

[2] Schmid, A., Dordick, J.S., Hauer, B., Kiener, A., Wubbolts, M. and Witholt, B. (2001) Industrial biocatalysis today and tomorrow. Nature 409, 258–268.

DOI: https://doi.org/10.1038/35051736

[3] Pritchard, L. and Kell, D.B. (2002) Schemes of flux control in a model of Saccharomyces cerevisiae glycolysis. Eur J Biochem 269, 3894–3904.

DOI: https://doi.org/10.1046/j.1432-1033.2002.03055.x

[4] Davies, S.E. and Brindle, K.M. (1992) Effects of overexpression of phosphofructokinase on glycolysis in the yeast Saccharomyces cerevisiae. Biochemistry 31, 4729–4735.

DOI: https://doi.org/10.1021/bi00134a028

[5] Larsson, C., Nilsson, A., Blomberg, A. and Gustafsson, L. (1997).

[6] Thomas, S. and Fell, D.A. (1998) A control analysis exploration of the role of ATP utilisation in glycolytic-flux control and glycolytic-metabolite-concentration regulation. Eur J Biochem 258, 956–967.

DOI: https://doi.org/10.1046/j.1432-1327.1998.2580956.x

[7] Koebmann, B.J., Westerhoff, H.V., Snoep, J.L., Nilsson, D. and Jensen, P.R. (2002) The glycolytic flux in Escherichia coli is controlled by the demand for ATP. J Bacteriol 184, 3909–3916.

DOI: https://doi.org/10.1128/jb.184.14.3909-3916.2002

[8] Jensen, P.R. and Michelsen, O. (1992) Carbon and energy metabolism of ATP mutants of Escherichia coli. J Bacteriol 174, 7635–7641.

DOI: https://doi.org/10.1128/jb.174.23.7635-7641.1992

[9] Wu, K., Aoki, C., Elste, A., Rogalski-Wilk, A.A. and Siekevitz, P. (1997) The synthesis of ATP by glycolytic enzymes in the postsynaptic density and the effect of endogenously generated nitric oxide. Proc Natl Acad Sci USA 94, 13273–13278.

DOI: https://doi.org/10.1073/pnas.94.24.13273

[10] Senior, A.E. (1988) ATP synthesis by oxidative phosphorylation. Physiol Rev 68, 177–231.

[11] Liu, L.M., Li, Y., Li, H.Z. and Chen, J. (2004) Manipulating the pyruvate dehydrogenase bypass of a multi-vitamin auxotrophic yeast Torulopsis glabrata enhanced pyruvate production. Lett Appl Microbiol 39, 199–206.

DOI: https://doi.org/10.1111/j.1472-765x.2004.01563.x

[12] Barnard, E.A. (1975) Hexokinase from yeast. Methods Enzymol 42, 6–20.

[13] Stanley, P.E. (1986) Extraction of adenosine triphosphate from microbial and somatic acid. Methods Enzymol 133, 14–22.

[14] Miseta, A., Tokes-Fuzesi, M., Aiello, D. and Bedwell, D. (2003).

[15] Futai, M. and Kanazawa, H. (1983) Structure and function of proton-translocating adenosine triphosphatase (F0F1): biochemical and molecular biological approaches. Microbiol Rev 47, 285–312.