Calmodulin mediated activation of acetyl-CoA carboxylase during aflatoxin production by Aspergillus parasiticus.


Journal Article

The relevance of Ca2+-calmodulin-mediated processes in channelling acetate for aflatoxin formation was investigated by studying the influence of trifluoperazine (an anticalmodulin agent) on [14C]-acetate incorporation and activity of acetyl-CoA carboxylase in Aspergillus parasiticus NRRL 2999. Culturing the organism in presence of 0.14 mmol l-1 trifluoperazine resulted in 55% decrease of [14C]-acetate incorporation into aflatoxin B1, along with an 80% decrease in acetyl-CoA carboxylase activity at periods corresponding to maximal aflatoxin production. Concomitant decrement (35%) in the activity of glucose-6-phosphate dehydrogenase indicated decreased availability of reduction potential (NADPH) required for aflatoxin biosynthesis. The ability of calmodulin to activate and trifluoperazine to inhibit acetyl-CoA carboxylase activity in a dose-dependent manner was also noted under in vitro conditions. The combined results suggest calmodulin-mediated activation of acetyl-CoA carboxylase as an important event for aflatoxin production.

Full Text

Duke Authors

Cited Authors

  • Rao, JP; Subramanyam, C

Published Date

  • April 2000

Published In

Volume / Issue

  • 30 / 4

Start / End Page

  • 277 - 281

PubMed ID

  • 10792646

Pubmed Central ID

  • 10792646

International Standard Serial Number (ISSN)

  • 0266-8254

Digital Object Identifier (DOI)

  • 10.1046/j.1472-765x.2000.00717.x


  • eng

Conference Location

  • England