Farnesyltransferase
Farnesyltransferase is an enzyme that plays a crucial role in the post-translational modification of proteins through a process known as prenylation. Specifically, farnesyltransferase catalyzes the attachment of a farnesyl group, a 15-carbon isoprenoid, to the cysteine residue at the C-terminus of certain proteins. This modification is critical for the proper functioning of these proteins, including their localization within cellular membranes and their involvement in signal transduction pathways.
Function[edit | edit source]
Farnesyltransferase facilitates the attachment of a farnesyl group to the cysteine residue in the CAAX motif (where C is cysteine, A is an aliphatic amino acid, and X is any amino acid) of target proteins. This enzymatic activity is essential for the post-translational modification known as prenylation, which is crucial for the proper localization and function of the modified proteins. Prenylated proteins are typically involved in important cellular processes such as cell growth, differentiation, and apoptosis.
Structure[edit | edit source]
The enzyme is a heterodimer, consisting of an alpha (α) and a beta (β) subunit, which together form the active site where the farnesylation reaction occurs. The structure of farnesyltransferase has been elucidated through X-ray crystallography, revealing insights into its mechanism of action and how it recognizes the CAAX motif of substrate proteins.
Clinical Significance[edit | edit source]
Farnesyltransferase inhibitors (FTIs) have been studied extensively as potential therapeutic agents, particularly in the context of cancer treatment. Many oncogenic proteins, such as Ras, require farnesylation for their activity. By inhibiting farnesyltransferase, FTIs can prevent the proper functioning of these proteins, thereby hindering the growth and proliferation of cancer cells. Although the clinical efficacy of FTIs has been variable, research continues into their potential use in treating various malignancies.
See Also[edit | edit source]
References[edit | edit source]
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