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

Dufe, Veronica T; Luersen, K; Eschbach, M L; Haider, N; Karlberg, Tobias LU ; Walter, R D and Al-Karadaghi, Salam LU (2005) In FEBS Letters 579(27). p.6037-6043
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 (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... (More)
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. (Less)
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author
organization
publishing date
type
Contribution to journal
publication status
published
subject
in
FEBS Letters
volume
579
issue
27
pages
6037 - 6043
publisher
Wiley-Blackwell
external identifiers
  • wos:000233157800007
  • pmid:16226262
  • scopus:27544516410
ISSN
1873-3468
DOI
10.1016/j.febslet.2005.09.050
language
English
LU publication?
yes
id
e7b55348-29e0-470d-a217-01af58eeb406 (old id 152236)
date added to LUP
2007-07-09 14:53:14
date last changed
2017-04-09 04:20:35
@article{e7b55348-29e0-470d-a217-01af58eeb406,
  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 (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.},
  author       = {Dufe, Veronica T and Luersen, K and Eschbach, M L and Haider, N and Karlberg, Tobias and Walter, R D and Al-Karadaghi, Salam},
  issn         = {1873-3468},
  language     = {eng},
  number       = {27},
  pages        = {6037--6043},
  publisher    = {Wiley-Blackwell},
  series       = {FEBS Letters},
  title        = {Cloning, expression, characterisation and three-dimensional structure determination of Caenorhabditis elegans spermidine synthase},
  url          = {http://dx.doi.org/10.1016/j.febslet.2005.09.050},
  volume       = {579},
  year         = {2005},
}