Silberring J, Castello M E, Nyberg F
Department of Pharmacology, University of Uppsala, Sweden.
J Biol Chem. 1992 Oct 25;267(30):21324-8.
A highly specific proteinase, converting dynorphin A (1-17) to enkephalins, was isolated from the human spinal cord and subjected to further characterization. The enzyme was found to be a thiol-dependent protein with a relative molecular mass of 50 kDa and a pH optimum between 5.0 and 5.5. This proteinase appears to exclusively convert dynorphin A (1-17) to Leu-enkephalin and its COOH-terminal extensions Leu-enkephalin-Arg6 (which was a major conversion product) and Leu-enkephalin-Arg6-Arg7 but not the other prodynorphin- or proenkephalin-derived peptides. This high specificity toward a single structure is suggested to be involved in a distinct processing pathway associated with the generation of the opioid peptides with selectivity for delta-opioid receptors.
从人脊髓中分离出一种高度特异性的蛋白酶，它能将强啡肽A（1-17）转化为脑啡肽，并对其进行了进一步表征。该酶是一种依赖硫醇的蛋白质，相对分子质量为50 kDa，最适pH值在5.0至5.5之间。这种蛋白酶似乎只将强啡肽A（1-17）转化为亮氨酸脑啡肽及其C末端延伸产物亮氨酸脑啡肽-Arg6（这是主要的转化产物）和亮氨酸脑啡肽-Arg6-Arg7，而不转化其他源自前强啡肽或前脑啡肽的肽。对单一结构的这种高特异性表明它参与了一条与生成对δ阿片受体具有选择性的阿片肽相关的独特加工途径。
