| Literature DB >> 22449979 |
Guilherme Coutinho de Mello Serrano1, Thaís Rezende e Silva Figueira, Eduardo Kiyota, Natalia Zanata, Paulo Arruda.
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 α-proteobacterium with a configuration similar to that of Silicibacter, whereas the ID in the plant enzyme may have been inherited from Cyanobacteria. Copyright ÂEntities:
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Year: 2012 PMID: 22449979 DOI: 10.1016/j.febslet.2012.02.023
Source DB: PubMed Journal: FEBS Lett ISSN: 0014-5793 Impact factor: 4.124