Black B C, Smarrelli J
Biochim Biophys Acta. 1986 Mar 7;870(1):31-40. doi: 10.1016/0167-4838(86)90005-1.
The kinetic mechanism of dopa decarboxylase (3,4-dihydroxy-L-phenylalanine carboxy-lyase, EC 4.1.1.28) was investigated in Drosophila melanogaster. Based on initial velocity and product inhibition studies, an ordered reaction is proposed for dopa decarboxylase. This kinetic mechanism is interpreted in the context of measured enzyme activities and the catecholamine pools in Drosophila. The 1(2)amd gene is immediately adjacent to the gene coding for dopa decarboxylase (Ddc) and determines hypersensitivity to alpha-methyldopa in Drosophila. Dopa decarboxylase does not decarboxylate alpha-methyldopa and hence does not generate a toxic product capable of inhibiting 1(2)amd gene function. We propose that the 1(2)amd gene is involved with an unknown catecholamine pathway involving dopa but not dopamine.
在黑腹果蝇中研究了多巴脱羧酶（3,4-二羟基-L-苯丙氨酸羧基裂解酶，EC 4.1.1.28）的动力学机制。基于初速度和产物抑制研究，提出了多巴脱羧酶的有序反应。在测量的果蝇酶活性和儿茶酚胺库的背景下解释了这种动力学机制。1(2)amd基因紧邻编码多巴脱羧酶（Ddc）的基因，并决定了果蝇对α-甲基多巴的超敏反应。多巴脱羧酶不能使α-甲基多巴脱羧，因此不会产生能够抑制1(2)amd基因功能的有毒产物。我们提出1(2)amd基因参与了一条未知的涉及多巴但不涉及多巴胺的儿茶酚胺途径。
