Identity of Malonyl and Palmitoyl Transferase of Fatty Acid Synthetase from Yeast. 1. Functional Interrelationships between the Acyl Transferases

Autor:	Jutta Straub, Karin Hübner, Hansjorg Engeser, Feodor Lynen
Rok vydání:	1979
Předmět:	chemistry.chemical_classification Enzyme chemistry Biochemistry Substrate (chemistry) Fatty acid Transferase lipids (amino acids peptides and proteins) macromolecular substances Yeast
Zdroj:	European Journal of Biochemistry. 101:407-412
ISSN:	1432-1033 0014-2956
Popis:	Functional interrelationships between the acyl transferases of yeast fatty acid synthetase were investigated. In binding assays with synthetase modified by 5,5'-dithiobis(2-nitrobenzoic acid), 4--5 malonyl transferase entities per multienzyme complex molecule could be titrated. In the presence of palmitoyl-CoA these malonyl transferases were found inaccessible to malonyl-CoA, whereas the acetyl transferases were reactive towards acetyl-CoA. Between four and five palmitoyl transferase entities per synthetase equivalent were found reactive towards palmitoyl-CoA, the palmitoyl binding being inhibited by malonyl-CoA. Following palmitoyl binding the acetyl transferases were found towards acetyl-CoA. Substrate model assays were consistent with these data. It is concluded that malonyl and palmitoyl transferases are closely coupled enzyme components of the multienzyme complex which are fairly independent of the acetyl transferase entities. The molecular basis for the observed coupling will be given in the following paper.
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=doi_________::0433aac0c4b483d047a79d988dda0732 https://doi.org/10.1111/j.1432-1033.1979.tb19733.x Zobrazit plný text záznamu Plný text ve formátu PDF