来自大肠杆菌的二氢蝶啶还原酶。
Dihydropteridine reductase from Escherichia coli.
作者信息
Vasudevan S G, Shaw D C, Armarego W L
机构信息
Department of Biochemistry, John Curtin School of Medical Research, Australian National University, Canberra.
出版信息
Biochem J. 1988 Oct 15;255(2):581-8.
A dihydropteridine reductase from Escherichia coli was purified to apparent homogeneity. It is a dimeric enzyme with identical subunits (Mr 27000) and a free N-terminal group. It can use NADH (Vmax./Km 3.36 s-1) and NADPH (Vmax./Km 1.07 s-1) when 6-methyldihydro-(6H)-pterin is the second substrate, as well as quinonoid dihydro-(6H)-biopterin (Vmax./Km 0.69 s-1), dihydro-(6H)-neopterin (Vmax./Km 0.58 s-1), dihydro-(6H)-monapterin 0.66 s-1), 6-methyldihydro-(6H)-pterin and cis-6,7-dimethyldihydro-(6H)-pterin (Vmax./Km 0.66 s-1) when NADH is the second substrate. The pure reductase has a yellow colour and contains bound FAD. The enzyme also has pterin-independent NADH and NADPH oxidoreductase activities when potassium ferricyanide is the electron acceptor.
从大肠杆菌中纯化出一种二氢蝶啶还原酶，达到了表观均一性。它是一种二聚体酶，亚基相同（分子量27000），具有游离的N末端基团。当6-甲基二氢-（6H）-蝶呤作为第二底物时，它可以利用NADH（Vmax./Km为3.36 s-1）和NADPH（Vmax./Km为1.07 s-1），当NADH作为第二底物时，它还可以利用醌型二氢-（6H）-生物蝶呤（Vmax./Km为0.69 s-1）、二氢-（6H）-新蝶呤（Vmax./Km为0.58 s-1）、二氢-（6H）-单蝶呤（Vmax./Km为0.66 s-1）、6-甲基二氢-（6H）-蝶呤和顺式-6,7-二甲基二氢-（6H）-蝶呤（Vmax./Km为0.66 s-1）。纯还原酶呈黄色，含有结合型FAD。当铁氰化钾作为电子受体时，该酶还具有不依赖蝶呤的NADH和NADPH氧化还原酶活性。
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