Cloning, expression, characterisation and three-dimensional structure determination of Caenorhabditis elegans spermidine synthase.
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.
Dufe
Veronica T
VT
Department of Molecular Biophysics, Center for Chemistry and Chemical Engineering, Lund University, P.O. Box 124, 221 00 Lund, Sweden.
Lüersen
Kai
K
Eschbach
Marie-Luise
ML
Haider
Nashya
N
Karlberg
Tobias
T
Walter
Rolf D
RD
Al-Karadaghi
Salam
S
D000595:Amino Acid Sequence; D000818:Animals; D017173:Caenorhabditis elegans / Q000201:enzymology* / Q000235:genetics; D003001:Cloning, Molecular; D018360:Crystallography, X-Ray; D019281:Dimerization; D025461:Feedback, Physiological; D008969:Molecular Sequence Data; D011487:Protein Conformation; D011436:Spermidine Synthase / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism
D011436:Spermidine Synthase