English (United Kingdom)

https://curated-unify.zendy.io/wp-json/zendy-region/v1/featured_content/oa?rat=en

https://curated-unify.zendy.io/wp-json/zendy-region/v1/highlighted_journal/

Global: Zendy Plus annual

Presents the access of premium content as premium feature

Premium Content

Presents the keyphrase highlighting as premium feature

Keyphrase Highlighting

Presents the summarisation as premium feature

Summarisation

Insights

Presents the pdf analysis as premium feature

PDF Analysis

Presents the zaia usage as premium feature

ZAIA

Global: Zendy Tools annual

Global: Zendy Free Plan

Global: Zendy Tools monthly

Global: Zendy Plus monthly

Performic acid-oxidized modifications of monoketo-organomycin and cystaurimycin1) were found to possess identical mechanisms of action. Both inhibit mitochondrial ATPase activity in Aspergillus nidulans. The corresponding binding-protein was isolated from whole mitochondria and purified ATPase complex using neutral chloroform-methanol mixture. Gel filtration and amino acid analyses gave an estimated molecular weight of 8, 000-8, 500 dalton and was identified as the smallest subunit of the ATPase complex. This protein is highly hydrophobic (30% polarity) and highly rich in alanine, leucine and glycine. Tyrosine and alanine represent the N- and C-terminal amino acids respectively. Binding studies revealed that neither the N- nor the C- terminal residues of the above two enzyme inhibitors was involved in the binding or inhibition processes. Nonspecific binding to other mitochondrial component(s) was, however, observed with oxidized monoketo-organomycin. This nonspecific binding could be abolished by using the dansylated derivative of the latter compound. The dicyclohexylcarbodiimide (DCCD)-binding protein showed characteristics very similar to what appeared to be the same and one protein capable of binding the performic acid-oxidized compounds. Oligomycin and DCCD had no significant inhibitory effect on binding of the ATPase inhibitors investigated. This mechanism of action differs from that exhibited by the parent nonoxidized compounds, monoketo-organomycin and cystaurimycin. The latter pair were found to inhibit in vitro protein synthesis2) but not ATPase activity.

journal of antibiotics

Mechanism of action of monoketo-organomycin, cystaurimycin and their performic acid-oxidized modifications. II. Inhibition of mitochondrial ATPase activity in Aspergillus nidulans and identification of the performic acid-oxidized modifications-binding protein.