Localization of three non-thiol binding sites on polypeptide chain β yeast fatty acid synthetase
| Autor: | Hansjorg Engeser, Feodor Lynen, Felix Wieland |
|---|---|
| Jazyk: | angličtina |
| Předmět: |
Macromolecular Substances
Stereochemistry Biophysics Dithionitrobenzoic Acid Saccharomyces cerevisiae Cleavage (embryo) Biochemistry Acetyl Coenzyme A Structural Biology Genetics Transferase Binding site Molecular Biology chemistry.chemical_classification Gel electrophoresis Binding Sites Palmitoyl Coenzyme A Fatty acid Cell Biology Yeast Malonyl Coenzyme A Enzyme chemistry Nitrobenzoates Thiol Fatty Acid Synthases |
| Zdroj: | FEBS Letters. (1):139-142 |
| ISSN: | 0014-5793 |
| DOI: | 10.1016/0014-5793(77)80904-6 |
| Popis: | The multienzyme complex FAS from yeast is known to consist of two different multifunctional polypeptide chains, (Y and fl [ 1 ] bearing seven different partial enzymic activities [2]. The distribution of six partial enzymes on the subunits has so far only been proposed from genetic studies [ 11. A localization of the partial enzyme acetyl transferase until now has not been achieved. The genetic prediction for the localization of the integrated ACP as well as the condensing activity has been proven by protein chemical methods [ 1,3]. SDS-gel electrophoresis, in our hands, did not yield clear separation of yeast FAS polypeptide chains. Furthermore, the long duration of this method allows the possibility of cleavage of labile chemical bonds between active sites and radioactively labeled markers used for such localization studies. Therefore a rapid, high-resolution, gel electrophoresis system has been developed for the localization of non-thiol binding sites (transferases) for acetyl, malonyl, and palmitoyl residues on fatty acid synthetase subunits. |
| Databáze: | OpenAIRE |
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