| Literature DB >> 6326747 |
U Keller, R Zocher, U Krengel, H Kleinkauf.
Abstract
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.Entities:
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Year: 1984 PMID： 6326747 PMCID： PMC1153415 DOI： 10.1042/bj2180857
Source DB: PubMed Journal: Biochem J ISSN： 0264-6021 Impact factor: 3.857