Cloning, expression, characterisation and three-dimensional structure determination of Caenorhabditis elegans spermidine synthase

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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 (K-m = 110 mu M) and a less pronounced feedback inhibition by the second reaction product 5 '-methylthioadenosine (IC50 = 430 mu M). 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. (c) 2005 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.

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  • Biological Sciences
Original languageEnglish
Pages (from-to)6037-6043
JournalFEBS Letters
Volume579
Issue number27
Publication statusPublished - 2005
Publication categoryResearch
Peer-reviewedYes