Biochemical and molecular characterization of α-ketoisovalerate decarboxylase, an enzyme involved in the formation of aldehydes from amino acids by Lactococcus lactis

8 páginas, 2 figuras, 3 tablas.

Detalles Bibliográficos
Autores: Plaza, Marta de la, Fernández de Palencia, P., Peláez, Carmen, Requena, Teresa
Tipo de recurso: artículo
Fecha de publicación:2004
País:España
Institución:Consejo Superior de Investigaciones Científicas (CSIC)
Repositorio:DIGITAL.CSIC. Repositorio Institucional del CSIC
OAI Identifier:oai:digital.csic.es:10261/113971
Acceso en línea:http://hdl.handle.net/10261/113971
Access Level:acceso abierto
Palabra clave:α-Ketoisovalerate decarboxylase
Lactococcus lactis
Amino acid catabolism
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spelling Biochemical and molecular characterization of α-ketoisovalerate decarboxylase, an enzyme involved in the formation of aldehydes from amino acids by Lactococcus lactisPlaza, Marta de laFernández de Palencia, P.Peláez, CarmenRequena, Teresaα-Ketoisovalerate decarboxylaseLactococcus lactisAmino acid catabolism8 páginas, 2 figuras, 3 tablas.In this paper, we report for the first time on the identification, purification, and characterization of the α-ketoisovalerate decarboxylase from Lactococcus lactis, a novel enzyme responsible for the decarboxylation into aldehydes of α-keto acids derived from amino acid transamination. The kivd gene consisted of a 1647 bp open reading frame encoding a putative peptide of 61 kDa. Analysis of the deduced amino acid sequence indicated that the enzyme is a non-oxidative thiamin diphosphate (ThDP)-dependent α-keto acid decarboxylase included in the pyruvate decarboxylase group of enzymes. The active enzyme is a homo-tetramer that showed optimum activity at 45 °C and at pH 6.5 and exhibited an inhibition pattern typical for metal-dependant enzymes. In addition to Mg2+, activity was observed in presence of other divalent cations such as Ca2+, Co2+ and Mn2+. The enzyme showed the highest specific activity (80.7 U mg−1) for α-ketoisovalerate, an intermediate metabolite in valine and leucine biosynthesis. On the other side, decarboxylation of indole-3-pyruvate and pyruvate only could be detected by a 100-fold increase in the enzyme concentration present in the reactionThis work was performed under the auspices of the Consejo Superior de Investigaciones Científicas and was supported by Research Project AGL2002-03277.Peer reviewedOxford University PressConsejo Superior de Investigaciones Científicas [https://ror.org/02gfc7t72]201520152004info:eu-repo/semantics/articlehttp://purl.org/coar/resource_type/c_6501http://hdl.handle.net/10261/113971reponame:DIGITAL.CSIC. Repositorio Institucional del CSICinstname:Consejo Superior de Investigaciones Científicas (CSIC)Ingléshttp://dx.doi.org/10.1111/j.1574-6968.2004.tb09778.xSíinfo:eu-repo/semantics/openAccessoai:digital.csic.es:10261/1139712026-05-22T06:33:51Z
dc.title.none.fl_str_mv Biochemical and molecular characterization of α-ketoisovalerate decarboxylase, an enzyme involved in the formation of aldehydes from amino acids by Lactococcus lactis
title Biochemical and molecular characterization of α-ketoisovalerate decarboxylase, an enzyme involved in the formation of aldehydes from amino acids by Lactococcus lactis
spellingShingle Biochemical and molecular characterization of α-ketoisovalerate decarboxylase, an enzyme involved in the formation of aldehydes from amino acids by Lactococcus lactis
Plaza, Marta de la
α-Ketoisovalerate decarboxylase
Lactococcus lactis
Amino acid catabolism
title_short Biochemical and molecular characterization of α-ketoisovalerate decarboxylase, an enzyme involved in the formation of aldehydes from amino acids by Lactococcus lactis
title_full Biochemical and molecular characterization of α-ketoisovalerate decarboxylase, an enzyme involved in the formation of aldehydes from amino acids by Lactococcus lactis
title_fullStr Biochemical and molecular characterization of α-ketoisovalerate decarboxylase, an enzyme involved in the formation of aldehydes from amino acids by Lactococcus lactis
title_full_unstemmed Biochemical and molecular characterization of α-ketoisovalerate decarboxylase, an enzyme involved in the formation of aldehydes from amino acids by Lactococcus lactis
title_sort Biochemical and molecular characterization of α-ketoisovalerate decarboxylase, an enzyme involved in the formation of aldehydes from amino acids by Lactococcus lactis
dc.creator.none.fl_str_mv Plaza, Marta de la
Fernández de Palencia, P.
Peláez, Carmen
Requena, Teresa
author Plaza, Marta de la
author_facet Plaza, Marta de la
Fernández de Palencia, P.
Peláez, Carmen
Requena, Teresa
author_role author
author2 Fernández de Palencia, P.
Peláez, Carmen
Requena, Teresa
author2_role author
author
author
dc.contributor.none.fl_str_mv Consejo Superior de Investigaciones Científicas [https://ror.org/02gfc7t72]
dc.subject.none.fl_str_mv α-Ketoisovalerate decarboxylase
Lactococcus lactis
Amino acid catabolism
topic α-Ketoisovalerate decarboxylase
Lactococcus lactis
Amino acid catabolism
description 8 páginas, 2 figuras, 3 tablas.
publishDate 2004
dc.date.none.fl_str_mv 2004
2015
2015
dc.type.none.fl_str_mv info:eu-repo/semantics/article
http://purl.org/coar/resource_type/c_6501
format article
dc.identifier.none.fl_str_mv http://hdl.handle.net/10261/113971
url http://hdl.handle.net/10261/113971
dc.language.none.fl_str_mv Inglés
language_invalid_str_mv Inglés
dc.relation.none.fl_str_mv http://dx.doi.org/10.1111/j.1574-6968.2004.tb09778.x
Sí
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
eu_rights_str_mv openAccess
dc.publisher.none.fl_str_mv Oxford University Press
publisher.none.fl_str_mv Oxford University Press
dc.source.none.fl_str_mv reponame:DIGITAL.CSIC. Repositorio Institucional del CSIC
instname:Consejo Superior de Investigaciones Científicas (CSIC)
instname_str Consejo Superior de Investigaciones Científicas (CSIC)
reponame_str DIGITAL.CSIC. Repositorio Institucional del CSIC
collection DIGITAL.CSIC. Repositorio Institucional del CSIC
repository.name.fl_str_mv
repository.mail.fl_str_mv
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score 15.81155

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