Structural highlights
Evolutionary Conservation
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Publication Abstract from PubMed
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.
Cloning, expression, characterisation and three-dimensional structure determination of Caenorhabditis elegans spermidine synthase.,Dufe VT, Luersen K, Eschbach ML, Haider N, Karlberg T, Walter RD, Al-Karadaghi S FEBS Lett. 2005 Nov 7;579(27):6037-43. Epub 2005 Oct 5. PMID:16226262[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Dufe VT, Luersen K, Eschbach ML, Haider N, Karlberg T, Walter RD, Al-Karadaghi S. Cloning, expression, characterisation and three-dimensional structure determination of Caenorhabditis elegans spermidine synthase. FEBS Lett. 2005 Nov 7;579(27):6037-43. Epub 2005 Oct 5. PMID:16226262 doi:10.1016/j.febslet.2005.09.050
