Harada T, Kagamiyama H, Hatakeyama K
Department of Biochemistry, Osaka Medical College, Japan.
Science. 1993 Jun 4;260(5113):1507-10. doi: 10.1126/science.8502995.
Guanosine triphosphate (GTP) cyclohydrolase I, the rate-limiting enzyme in the biosynthesis of tetrahydrobiopterin (BH4), is subject to feedback inhibition by BH4, a cofactor for phenylalanine hydroxylase. Inhibition was found to depend specifically on BH4 and the presence of another protein (p35). The inhibition occurred through BH4-dependent complex formation between p35 protein and GTP cyclohydrolase I. Furthermore, the inhibition was specifically reversed by phenylalanine, and, in conjunction with p35, phenylalanine reduced the cooperativity of GTP cyclohydrolase I. These findings also provide a molecular basis for high plasma BH4 concentrations observed in patients with hyperphenylalaninemia caused by phenylalanine hydroxylase deficiency.
鸟苷三磷酸(GTP)环化水解酶I是四氢生物蝶呤(BH4)生物合成中的限速酶,它受到BH4(苯丙氨酸羟化酶的一种辅助因子)的反馈抑制。已发现这种抑制作用特别依赖于BH4以及另一种蛋白质(p35)的存在。抑制作用是通过p35蛋白与GTP环化水解酶I之间依赖于BH4的复合物形成而发生的。此外,苯丙氨酸能特异性地逆转这种抑制作用,并且与p35一起,苯丙氨酸降低了GTP环化水解酶I的协同性。这些发现也为苯丙氨酸羟化酶缺乏导致的高苯丙氨酸血症患者中观察到的高血浆BH4浓度提供了分子基础。