Nakanishi N, Hasegawa H, Watabe S
J Biochem. 1977 Mar;81(3):681-5. doi: 10.1093/oxfordjournals.jbchem.a131504.
An enzyme designated as NADPH-dihydropteridine reductase was found in the extract of bovine liver and partially purified. In contrast to NADH-dpendent dihydropteridine reductase [EC 1.6.99.7], the enzyme catalyzes the reduction of quinonid-dihydropterin to tetrahydropterin in the presence of NADPH. The two enzymes were separated by column chromatography on DEAE-sephadex. Tyrosine formation in the phenylalanine hydroxylation system was also stimulated by NADPH-dihydropteridine reductase. The existence of these two dihydropteridine reductases suggests that the tetrahydro from ofpteridine cofactor may be regenerated in two different ways in vivo.
在牛肝提取物中发现了一种名为NADPH-二氢蝶啶还原酶的酶,并对其进行了部分纯化。与依赖NADH的二氢蝶啶还原酶[EC 1.6.99.7]不同,该酶在NADPH存在的情况下催化醌型二氢蝶呤还原为四氢蝶呤。通过DEAE-葡聚糖凝胶柱色谱法将这两种酶分离。NADPH-二氢蝶啶还原酶也刺激了苯丙氨酸羟化系统中酪氨酸的形成。这两种二氢蝶啶还原酶的存在表明,体内四氢蝶呤辅因子可能通过两种不同的方式再生。