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- W1523573435 abstract "Publisher Summary This chapter discusses the present understanding of the mechanisms underlying protein thioacylation and deacylation. The structural requirements for this modification and the intracellular sites where proteins are thioacylated are reviewed in the chapter. The dynamic nature of protein thioacylation dictates that mechanisms exist not only for the addition, but also for the removal of fatty acids from proteins. Significant progress has been made in purifying palmitoyl–protein thioesterase activities and cloning the genes corresponding to these activities, permitting first glimpse of the physiological settings in which protein deacylation is functionally important. The mechanism of fatty acid addition to proteins is controversial. Although several protein acyltransferase activities have been purified to apparent homogeneity, it has not been established that these enzymes mediate protein thioacylation in cells. The chapter discusses the evidence supporting enzymatic versus nonenzymatic mechanisms for the addition of fatty acids to proteins. The properties, localization, and function of palmitoyl–protein thioesterases are discussed in the chapter." @default.
- W1523573435 created "2016-06-24" @default.
- W1523573435 creator A5021448016 @default.
- W1523573435 date "2001-01-01" @default.
- W1523573435 modified "2023-09-27" @default.
- W1523573435 title "8 Reversible modification of proteins with thioester-linked fatty acids" @default.
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- W1523573435 doi "https://doi.org/10.1016/s1874-6047(01)80021-4" @default.
- W1523573435 hasPublicationYear "2001" @default.
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