期刊
FEBS LETTERS
卷 586, 期 6, 页码 905-911出版社
ELSEVIER SCIENCE BV
DOI: 10.1016/j.febslet.2012.02.023
关键词
Lysine metabolism; Lysine-ketoglutarate reductase; Saccharopine dehydrogenase; Bacteria; Mammal; Plant
资金
- Coordenacao de Aperfeicoamento de professores do Ensino Superior (CAPES)
- CNPq
- FAPESP [10/50114-4]
- Fundacao de Amparo a Pesquisa do Estado de Sao Paulo (FAPESP) [10/50114-4] Funding Source: FAPESP
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.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据