Structural highlights
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
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.
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
