Inhibition of acyl-CoA: cholesterol acyltransferase activity by cyclodepsipeptide antibiotics.
The effect was studied of the fungal cyclodepsipeptide antibiotics beauvericin and seven distinct enniatins on acyl-CoA: cholesterol acyltransferase (ACAT) activity, indicating that the compound is one of the most potent ACAT inhibitors of microbial origin.
Inhibition of acyl-CoA synthetase by triacsins.
- H. Tomoda, K. Igarashi, S. Ōmura
- Chemistry, BiologyBiochimica et Biophysica Acta
- 1987
Kinetic analysis indicates that inhibition of triacsin A is non-competitive withrespect to the two substrates ATP and coenzyme A, but is competitive with respect to long-chain fatty acids, and the N-hydroxytriazene moiety is essential for inhibitory activity against acyl-CoA synthetase.
New cyclodepsipeptides, enniatins D, E and F produced by Fusarium sp. FO-1305.
- H. Tomoda, H. Nishida, X. Huang, R. Masuma, Y. K. Kim, S. Ōmura
- Chemistry, BiologyJournal of antibiotics (Tokyo. )
- 25 August 1992
New cyclodepsipeptides named enniatins D, E and F were isolated from the culture broth of Fusarium sp. FO-1305 as inhibitors of acyl-CoA:cholesterol acyltransferase (ACAT). The respective structures…
Evidence for an essential role of long chain acyl-CoA synthetase in animal cell proliferation. Inhibition of long chain acyl-CoA synthetase by triacsins caused inhibition of Raji cell proliferation.
- H. Tomoda, K. Igarashi, J. Cyong, S. Ōmura
- Biology, ChemistryJournal of Biological Chemistry
- 5 March 1991
The data strongly suggest that the inhibition of acyl-CoA synthetase by triacsins leads to the inhibiting of lipid synthesis and eventually to the inhibited of proliferation of Raji cells.
Purpactins, new inhibitors of acyl-CoA:cholesterol acyltransferase produced by Penicillium purpurogenum. I. Production, isolation and physico-chemical and biological properties.
- H. Tomoda, H. Nishida, R. Masuma, J. Cao, S. Okuda, S. Ōmura
- Biology, ChemistryJournal of antibiotics (Tokyo. )
- 1 February 1991
Penicillium purpurogenum FO-608, a soil isolate, was found to produce a series of new inhibitors of acyl-CoA:cholesterol acyltransferase (ACAT), indicating the inhibition of ACAT activity in the living cells by purpactin A.
Glisoprenins, new inhibitors of acyl-CoA: cholesterol acyltransferase produced by Gliocladium sp. FO-1513. I. Production, isolation and physico-chemical and biological properties.
- H. Tomoda, X. Huang, H. Nishida, R. Masuma, Y. K. Kim, S. Ōmura
- Biology, ChemistryJournal of antibiotics (Tokyo. )
- 25 August 1992
Gliocladium sp. FO-1513 was found to produce novel inhibitors of acyl-CoA: cholesterol acyltransferase (ACAT). Two active compounds, designated glisoprenins A and B, were isolated from the culture…
Structure-specific inhibition of cholesteryl ester transfer protein by azaphilones.
- H. Tomoda, C. Matsushima, S. Ōmura
- Biology, ChemistryJournal of antibiotics (Tokyo. )
- 25 February 1999
The relationship between the structures and their inhibitory activity indicated that the presence of an electrophilic ketone and/or enone at both C-6 and C-8 positions in the isochromane-like ring is essential for eliciting CETP inhibitory Activity.
Amidepsines, inhibitors of diacylglycerol acyltransferase produced by Humicola sp. FO-2942. I. Production, isolation and biological properties.
- H. Tomoda, M. Ito, N. Tabata, R. Masuma, Y. Yamaguchi, S. Ōmura
- Biology, ChemistryJournal of antibiotics (Tokyo. )
- 1 September 1995
Humicola sp. FO-2942, a soil isolate, was found to produce a series of new inhibitors of diacylglycerol acyltransferase (DGAT). Three active compounds, designated amidepsines A, B and C, were…
Pyripyropenes, novel inhibitors of acyl-CoA:cholesterol acyltransferase produced by Aspergillus fumigatus. I. Production, isolation, and biological properties.
- H. Tomoda, Y. K. Kim, H. Nishida, R. Masuma, S. Ōmura
- Biology, ChemistryJournal of antibiotics (Tokyo. )
- 25 February 1994
Aspergillus fumigatus FO-1289, a soil isolate, was found to produce a series of novel inhibitors of acyl-CoA:cholesterol acyltransferase (ACAT), which shows very potent ACAT inhibitory activity in an enzyme assay system using rat liver microsomes.
New strategy for discovery of enzyme inhibitors: screening with intact mammalian cells or intact microorganisms having special functions.
Researchers have revealed the mechanism of action of substances that are practically useful, as well as others that are biologically interesting, that have been providing targets for selective cytotoxicity or pharmacological intervention.
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