Cloning, expression, characterisation and three-dimensional structure determination of Caenorhabditis elegans spermidine synthase
(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)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/152236
- author
- Dufe, Veronica T ; Luersen, K ; Eschbach, M L ; Haider, N ; Karlberg, Tobias LU ; Walter, R D and Al-Karadaghi, Salam LU
- organization
- publishing date
- 2005
- 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
- pmid:16226262
- 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
- 2016-04-01 16:28:18
- date last changed
- 2022-01-28 19:55:58
@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}}, doi = {{10.1016/j.febslet.2005.09.050}}, volume = {{579}}, year = {{2005}}, }