Barber J I, Townsend D, Olds D P, King R A
J Invest Dermatol. 1984 Aug;83(2):145-9. doi: 10.1111/1523-1747.ep12263381.
We report our preliminary characterization of a new enzyme in the pigment pathway which we propose to call dopachrome oxidoreductase (DCOR). This enzyme, prepared from mouse melanoma, catalyzed the conversion of dopachrome to 5,6-dihydroxyindole and also appeared to block the pigment pathway at this latter compound in the absence of tyrosinase. DCOR was protease-sensitive, heat-labile, and showed maximum stability in the range of pH 6-8. The molecular weight of DCOR was estimated to be 34,000 by gel filtration. DCOR had a subcellular distribution within the melanocyte which was similar to that of tyrosinase, but DCOR activity was found in melanocytes devoid of tyrosinase activity and was not inhibited by tyrosinase inhibitors. DCOR may prove to be an active regulatory enzyme in melanogenesis.
我们报告了色素途径中一种新酶的初步特性,我们提议将其命名为多巴色素氧化还原酶(DCOR)。这种从小鼠黑色素瘤中制备的酶催化多巴色素转化为5,6 - 二羟基吲哚,并且在没有酪氨酸酶的情况下,似乎在后者这种化合物处阻断色素途径。DCOR对蛋白酶敏感、热不稳定,在pH 6 - 8范围内显示出最大稳定性。通过凝胶过滤估计DCOR的分子量为34,000。DCOR在黑素细胞内具有亚细胞分布,这与酪氨酸酶相似,但在缺乏酪氨酸酶活性的黑素细胞中发现了DCOR活性,并且不受酪氨酸酶抑制剂的抑制。DCOR可能被证明是黑色素生成中的一种活性调节酶。