]> 2026-07-31T12:14:40+00:00 WBR0935 0 en Glycosyltransferase Glycosylation refers to the addition of a carbohydrate to a protein. The glycosylation of proteins does not target them for degradation. Glycosylation is often necessary for the proper function or folding of the modified protein. One example of a heavily glycosylated protein family is the heparin sulfate proteoglycans. Farnesyltransferase Farnesyl groups can be added to proteins for their proper localization to cell membranes. Farnesylation does not target proteins for degradation. Gamma-carboxylase Vitamin K is gamma-carboxylated for its normal function. Hydroxylase Hydroxylation refers to the addition of an –OH group to a compound. Hydroxylation is an important step in the synthesis of steroid compounds. Proline hydroxylation is accomplished with Vitamin C as a cofactor in the synthesis of collagen. Ubiquitin ligase Proteins can be targeted for degradation by the addition of ubiquitin molecules to lysine residues. Biochemistry William J Gibson (Reviewed by Serge Korjian) Lenalidomide is a highly effective chemotherapeutic agent against multiple myeloma. A scientist is investigating the anti-neoplatic mechanism of lenalidomide. She finds that addition of lenalidomide to multiple myeloma cells decreases the protein abundance of the plasma cell essential transcription factors IKZF1 and IKZF3. She finds that lenalidomide binds to the CRBN-CRL4 complex, which then induces a post-translational modification of IKZF1 and IKZF3. Which of the following enzymatic activities does CRBN-CRL4 most likely possess? E Hematology General Principles 2020-10-28T02:07:10Z 2459150.5883102 WBR0935