Palmitoylation of rhodopsin with S-protein acyltransferase: enzyme catalyzed reaction versus autocatalytic acylation

Michael Veit , Kristina Sachs , Michael Heckelmann , Dieter Maretzki , Klaus Peter Hofmann , Michael F.G Schmidt
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引用次数: 47

Abstract

Protein palmitoylation in vitro was studied using bovine rhodopsin as the substrate and a partially purified acylating enzymatic activity (PAT) from placental membranes. PAT incorporates fatty acid into rhodopsin with higher efficiency (10 times higher initial rate), as compared to autoacylation. The activity is sensitive to heat and trypsin, indicating a protein-mediated enzymatic process and requires the native conformation of rhodopsin. The presence of deacylated, free cysteine residues in dark-adapted rhodopsin increases palmitoylation via PAT. The sites for non-enzymatic and enzymatic palmitoylation could not be distinguished by peptide mapping. The reversible palmitoylation described here will provide a tool for the study of the role of palmitoylation in photoreceptor function.

s蛋白酰基转移酶对紫红质棕榈酰化的影响:酶催化反应与自催化酰化反应
以牛视紫红质为底物,从胎盘膜中部分纯化的酰化酶活性(PAT),研究了体外蛋白棕榈酰化。与自酰化相比,PAT以更高的效率(初始速率高10倍)将脂肪酸并入视紫红质。该活性对热和胰蛋白酶敏感,表明是蛋白质介导的酶促过程,需要紫红质的天然构象。在适应黑暗的视紫红质中,脱酰基的游离半胱氨酸残基通过PAT增加棕榈酰化。非酶和酶棕榈酰化位点不能通过肽图谱来区分。这里描述的可逆棕榈酰化将为研究棕榈酰化在光感受器功能中的作用提供工具。
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