Hansson C, Rorsman H, Rosengren E, Wittbjer A
Acta Derm Venereol. 1985;65(2):154-7.
A tyrosinase obtained from cultured human melanoma cells was found to oxygenate 2,4-dihydroxyphenylalanine to the strongly cytotoxic amino acid 6-hydroxydopa (2,4,5-trihydroxyphenylalanine). The oxygenation was dependent on the presence of a reducing co-substrate such as dopa or dopamine. The rate of oxygenation of 2,4-dihydroxyphenyl-D,L-alanine was similar to that of L-tyrosine, the normal substrate of tyrosinase. The enzymatic reaction demonstrated may prove of value in the chemotherapy of human melanoma.
从培养的人黑色素瘤细胞中获得的一种酪氨酸酶，被发现可将2,4-二羟基苯丙氨酸氧化为具有强细胞毒性的氨基酸6-羟基多巴（2,4,5-三羟基苯丙氨酸）。这种氧化作用依赖于还原型共底物如多巴或多巴胺的存在。2,4-二羟基苯-D,L-丙氨酸的氧化速率与酪氨酸酶的正常底物L-酪氨酸的氧化速率相似。所展示的酶促反应可能在人类黑色素瘤的化疗中具有价值。
