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Lysine degradation through the saccharopine pathway in bacteria: LKR and SDH in bacteria and its relationship to the plant and animal enzymes
Author(s) -
de Mello Serrano Guilherme Coutinho,
e Silva Figueira Thaís Rezende,
Kiyota Eduardo,
Zanata Natalia,
Arruda Paulo
Publication year - 2012
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2012.02.023
Subject(s) - bacteria , lysine , enzyme , biochemistry , biology , reductase , cyanobacteria , dehydrogenase , phosphofructokinase 2 , amino acid , genetics
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.