作者: Marilyn D. Resh
DOI: 10.1016/J.PLIPRES.2016.05.002
关键词: Biology 、 Acyl-CoA 、 Fatty acylation 、 Palmitoylation 、 Acylation 、 Fatty acid 、 HHAT 、 Myristoylation 、 Biochemistry 、 Enzyme
摘要: Long, short and medium chain fatty acids are covalently attached to hundreds of proteins. Each acid confers distinct biochemical properties, enabling acylation regulate intracellular trafficking, subcellular localization, protein-protein protein-lipid interactions. Myristate palmitate represent the most common modifying groups. New insights into how reactions catalyzed, regulates protein structure function continue emerge. is typically linked an N-terminal glycine, but recent studies reveal that lysines can also be myristoylated. Enzymes remove myristoyl-glycine or myristate from have now been identified. DHHC proteins catalyze S-palmitoylation, mechanisms substrate recognition by individual family members remain determined. thioesterases S-acylated Another area rapid expansion secreted hedgehog, Wnt Ghrelin, Hhat, Porcupine GOAT, respectively. Understanding these membrane bound O-acyl transferases recognize their acyl CoA substrates active investigation, punctuated finding enzymes potential drug targets in human diseases.