Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
2051938 | FEBS Letters | 2005 | 7 Pages |
Abstract
The polyamine synthesis enzyme spermidine synthase (SPDS) has been cloned from the model nematode Caenorhabditis elegans. Biochemical characterisation of the recombinantly expressed protein revealed a high degree of similarity to other eukaryotic SPDS with the exception of a low affinity towards the substrate decarboxylated S-adenosylmethionine (Km = 110 μM) and a less pronounced feedback inhibition by the second reaction product 5’-methylthioadenosine (IC50 = 430 μM). The C. elegans protein that carries a nematode-specific insertion of 27 amino acids close to its N-terminus was crystallized, leading to the first X-ray structure of a dimeric eukaryotic SPDS.
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Authors
Veronica T. Dufe, Kai Lüersen, Marie-Luise Eschbach, Nashya Haider, Tobias Karlberg, Rolf D. Walter, Salam Al-Karadaghi,