Fujisaki M, Sugawara K
J Biochem. 1981 Jan;89(1):257-63. doi: 10.1093/oxfordjournals.jbchem.a133189.
An enzyme which catalyzes the coversion of arginyl residues to citrullyl residues in protein was obtained from the extract of the epidermis of newborn rats. The enzyme required Ca2+ for its activity. The enzyme activity was enhanced in the presence of DTT. The maximum activity was observed at pH 7.5 at 50 degrees C in the presence of 10 mm CaCl2 and 2 mM DTT. The activity was inhibited strongly by treatment of the enzyme with monoiodoacetate or PCMB, which suggests that the epidermal enzyme is an SH-enzyme. The molecular weight of the enzyme was calculated by gel filtration to be about 48,000. It was essential for the alpha-amino or alpha-carboxyl group of the L-arginine substrate to be involved in a peptide linkage. The enzyme showed marked activities towards N-substituted L-arginine derivatives such as BZ-L-Arg, BZ-L-Arg-NH2, and BZ-Gly-L-Arg, But the action of the enzyme on free L-arginine was negligible. The enzyme activity was affected by the nature of the residue neighboring the arginyl residue in proteins. The authors propose the name "peptidylarginine deiminase" for this enzyme. A considerable specificity of the enzyme for proteins from the epidermal cells in terminal differentiation was observed. The results suggest that citrullyl residues in membranous protein of horny cells of the epidermis of newborn rat are formed by the action of epidermal peptidylarginine deiminase.
一种能催化蛋白质中精氨酰残基转化为瓜氨酰残基的酶是从新生大鼠表皮提取物中获得的。该酶的活性需要Ca2+。在二硫苏糖醇（DTT）存在的情况下，酶活性增强。在10 mM氯化钙和2 mM DTT存在的条件下，于50℃、pH 7.5时观察到最大活性。用碘乙酸或对氯汞苯甲酸（PCMB）处理该酶会强烈抑制其活性，这表明表皮酶是一种含巯基（SH）的酶。通过凝胶过滤计算，该酶的分子量约为48,000。L-精氨酸底物的α-氨基或α-羧基参与肽键是必不可少的。该酶对N-取代的L-精氨酸衍生物如苄氧羰基-L-精氨酸（BZ-L-Arg）、苄氧羰基-L-精氨酸酰胺（BZ-L-Arg-NH2）和苄氧羰基-甘氨酰-L-精氨酸（BZ-Gly-L-Arg）表现出显著活性，但对游离L-精氨酸的作用可忽略不计。该酶的活性受蛋白质中与精氨酰残基相邻的残基性质的影响。作者为这种酶提议命名为“肽基精氨酸脱亚氨酶”。观察到该酶对终末分化的表皮细胞中的蛋白质具有相当的特异性。结果表明，新生大鼠表皮角质形成细胞膜蛋白中的瓜氨酰残基是由表皮肽基精氨酸脱亚氨酶的作用形成的。
