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Cloning, expression, characterisation and three-dimensional structure determination of Caenorhabditis elegans spermidine synthase |
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| Authors: | Dufe Veronica T Lüersen Kai Eschbach Marie-Luise Haider Nashya Karlberg Tobias Walter Rolf D Al-Karadaghi Salam |
| Institution: | Department of Molecular Biophysics, Center for Chemistry and Chemical Engineering, Lund University, P.O. Box 124, 221 00 Lund, Sweden. |
| 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 microM) and a less pronounced feedback inhibition by the second reaction product 5'-methylthioadenosine (IC50 = 430 microM). 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. |
| Keywords: | AdoDATO S-adenosyl-1 8-diamino-3-thiooctane AdoMetDC S-adenosylmethinone decarboxylase AdoMet S-adenosylmethionine dcAdoMet decarboxylated S-adenosylmethionine DTT dithiothreitol 4-MCHA trans-4-methylcyclohexylamine MTA 5′-methylthioadenosine ODC ornithine decarboxylase 3′-RACE 3′-rapid amplification of cDNA ends SPDS spermidine synthase |
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