Lysine degradation through the saccharopine pathway in bacteria: LKR and SDH in bacteria and its relationship to the plant and animal enzymes

dc.creatorSerrano, GCD
dc.creatorFigueira, TRES
dc.creatorKiyota, E
dc.creatorZanata, N
dc.creatorArruda, P
dc.date2012
dc.date44986
dc.date2014-08-01T18:36:04Z
dc.date2015-11-26T18:04:57Z
dc.date2014-08-01T18:36:04Z
dc.date2015-11-26T18:04:57Z
dc.date.accessioned2018-03-29T00:47:10Z
dc.date.available2018-03-29T00:47:10Z
dc.identifierFebs Letters. Elsevier Science Bv, v. 586, n. 6, n. 905, n. 911, 2012.
dc.identifier0014-5793
dc.identifierWOS:000301924600040
dc.identifier10.1016/j.febslet.2012.02.023
dc.identifierhttp://www.repositorio.unicamp.br/jspui/handle/REPOSIP/81331
dc.identifierhttp://repositorio.unicamp.br/jspui/handle/REPOSIP/81331
dc.identifier.urihttp://repositorioslatinoamericanos.uchile.cl/handle/2250/1292995
dc.descriptionCoordenação de Aperfeiçoamento de Pessoal de Nível Superior (CAPES)
dc.descriptionConselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)
dc.descriptionFundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)
dc.descriptionLysine 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.
dc.description586
dc.description6
dc.description905
dc.description911
dc.descriptionCoordenação de Aperfeiçoamento de Pessoal de Nível Superior (CAPES)
dc.descriptionConselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)
dc.descriptionFundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)
dc.descriptionCoordenação de Aperfeiçoamento de Pessoal de Nível Superior (CAPES)
dc.descriptionConselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)
dc.descriptionFundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)
dc.descriptionFAPESP [10/50114-4]
dc.languageen
dc.publisherElsevier Science Bv
dc.publisherAmsterdam
dc.publisherHolanda
dc.relationFebs Letters
dc.relationFEBS Lett.
dc.rightsfechado
dc.rightshttp://www.elsevier.com/about/open-access/open-access-policies/article-posting-policy
dc.sourceWeb of Science
dc.subjectLysine metabolism
dc.subjectLysine-ketoglutarate reductase
dc.subjectSaccharopine dehydrogenase
dc.subjectBacteria
dc.subjectMammal
dc.subjectPlant
dc.subjectDeveloping Maize Endosperm
dc.subjectAcid Metabolic Pathway
dc.subjectSequence Alignment
dc.subjectReductase
dc.subjectDehydrogenase
dc.subjectBiosynthesis
dc.subjectOrigin
dc.subjectMitochondria
dc.subjectIntegration
dc.subjectSynthase
dc.titleLysine degradation through the saccharopine pathway in bacteria: LKR and SDH in bacteria and its relationship to the plant and animal enzymes
dc.typeArtículos de revistas


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