| Full text | |
| Author(s): |
de Mello Serrano, Guilherme Coutinho
[1, 2]
;
Rezende e Silva Figueira, Thais
[1]
;
Kiyota, Eduardo
[1]
;
Zanata, Natalia
[1]
;
Arruda, Paulo
[1, 2]
Total Authors: 5
|
| Affiliation: | [1] Univ Estadual Campinas, UNICAMP, Ctr Biol Mol & Engn Genet, BR-13083970 Campinas, SP - Brazil
[2] Univ Estadual Campinas, UNICAMP, Inst Biol, Dept Genet & Evolucao, BR-13083970 Campinas, SP - Brazil
Total Affiliations: 2
|
| Document type: | Journal article |
| Source: | FEBS Letters; v. 586, n. 6, p. 905-911, MAR 23 2012. |
| Web of Science Citations: | 13 |
| Abstract | |
Lysine degradation through the saccharopine pathway has been shown only in plants and animals. Here, we show that bacteria possess the genes encoding lysine-ketoglutarate reductase (LKR) and saccharopine dehydrogenase (SDH). In Silicibacter, the contiguous lkr and sdh genes are interspersed, in another frame, by a polypeptide of unknown function. The bacterial enzyme does not contain the 110-amino-acid interdomain (ID) that intersperses the LKR and SDH domains of the plant enzyme. The ID was found in Cyanobacteria interspersing polypeptides without similarities and activities of LKR and SDH. The LKR/SDH bifunctional polypeptide of animals and plants may have arisen from a alpha-proteobacterium with a configuration similar to that of Silicibacter, whereas the ID in the plant enzyme may have been inherited from Cyanobacteria. (C) 2012 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved. (AU) | |
| FAPESP's process: | 10/50114-4 - The role of saccharopine pathway in diverse biological models |
| Grantee: | Paulo Arruda |
| Support Opportunities: | Regular Research Grants |