Keller U, Zocher R, Krengel U, Kleinkauf H
Biochem J. 1984 Mar 15;218(3):857-62. doi: 10.1042/bj2180857.
A D-lysergic acid-activating enzyme from the ergot fungus Claviceps purpurea was purified about 145-fold. The enzyme was able to catalyse both the D-lysergic acid-dependent ATP-pyrophosphate exchange and the formation of ATP from D-lysergic acid adenylate and pyrophosphate. Both reactions were also catalysed to a decreased but significant extent with respect to dihydrolysergic acid. The molecular mass of the enzyme was estimated to lie between 135 and 140 kDa. The involvement of the enzyme in the biosynthesis of ergot peptide alkaloids is discussed.
从麦角菌紫麦角菌中纯化出一种D-麦角酸激活酶，纯化倍数约为145倍。该酶能够催化依赖D-麦角酸的ATP-焦磷酸交换反应以及由D-麦角酸腺苷酸和焦磷酸形成ATP的反应。对于二氢麦角酸，这两个反应也能以降低但显著的程度被催化。该酶的分子量估计在135至140 kDa之间。文中讨论了该酶在麦角肽生物碱生物合成中的作用。
