Effect of side-chain structure on inhibition of yeast fatty-acid synthase by cerulenin analogues
| Autor: | Shigeo Iwasaki, Akihiko Kawaguchi, Rumiko Shimazawa, Shigenobu Okuda, Hiroshi Funabashi, Naoko Morisaki, Jun Furukawa |
|---|---|
| Rok vydání: | 1993 |
| Předmět: |
chemistry.chemical_classification
Binding Sites ATP synthase biology Double bond Carboxy-Lyases Stereochemistry Saccharomyces cerevisiae In Vitro Techniques Biochemistry Cerulenin Yeast Iodoacetamide chemistry.chemical_compound Fatty acid synthase Enzyme chemistry Acetyl Coenzyme A biology.protein Side chain lipids (amino acids peptides and proteins) Fatty Acid Synthases |
| Zdroj: | European Journal of Biochemistry. 211:111-115 |
| ISSN: | 1432-1033 0014-2956 |
| DOI: | 10.1111/j.1432-1033.1993.tb19876.x |
| Popis: | Yeast fatty-acid synthase (FAS) inhibition by cerulenin analogs with varying side-chain lengths was compared with that of cerulenin, tetrahydrocerulenin and iodoacetamide. Although inhibition by cerulenin was the highest, the analogs having (E,E)-delta 7,10 double bonds showed high inhibition. This strongly suggests that the (E,E)-delta 7,10 double bonds play an important role in the interaction of the inhibitors with the enzyme. It was suggested that the size of the hydrophobic cavity in the condensing enzyme terminates fatty-acid chain elongation by decreasing inhibition by the C18 analog. Like cerulenin itself, the shortest analog (C6) did not induce malonyl-CoA decarboxylase activity. |
| Databáze: | OpenAIRE |
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