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

Dufe, Veronica T (author)
Luersen, K (author)
Eschbach, M L (author)
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Haider, N (author)
Karlberg, Tobias (author)
Lund University,Lunds universitet,Biokemi och Strukturbiologi,Centrum för Molekylär Proteinvetenskap,Kemiska institutionen,Institutioner vid LTH,Lunds Tekniska Högskola,Biochemistry and Structural Biology,Center for Molecular Protein Science,Department of Chemistry,Departments at LTH,Faculty of Engineering, LTH
Walter, R D (author)
Al-Karadaghi, Salam (author)
Lund University,Lunds universitet,Biokemi och Strukturbiologi,Centrum för Molekylär Proteinvetenskap,Kemiska institutionen,Institutioner vid LTH,Lunds Tekniska Högskola,Biochemistry and Structural Biology,Center for Molecular Protein Science,Department of Chemistry,Departments at LTH,Faculty of Engineering, LTH
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 (creator_code:org_t)
2005-10-05
2005
English.
In: FEBS Letters. - : Wiley. - 1873-3468 .- 0014-5793. ; 579:27, s. 6037-6043
  • Journal article (peer-reviewed)
Abstract Subject headings
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  • 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.

Subject headings

NATURVETENSKAP  -- Biologi (hsv//swe)
NATURAL SCIENCES  -- Biological Sciences (hsv//eng)

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