Active-site-mutagenesis study of rat liver betaine-homocysteine S-methyltransferase

8 pages, 5 figures, 3 tables.

Detalles Bibliográficos
Autores: González, Beatriz, Campillo, Nuria E., Garrido, Francisco, Gasset, M., Sanz-Aparicio, J., Pajares, María Ángeles
Tipo de recurso: artículo
Estado:Versión aceptada para publicación
Fecha de publicación:2003
País:España
Institución:Consejo Superior de Investigaciones Científicas (CSIC)
Repositorio:DIGITAL.CSIC. Repositorio Institucional del CSIC
OAI Identifier:oai:digital.csic.es:10261/24661
Acceso en línea:http://hdl.handle.net/10261/24661
Access Level:acceso abierto
Palabra clave:Homocysteine metabolism
Kinetic study
Methionine metabolism
Site-directed mutagenesis
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spelling Active-site-mutagenesis study of rat liver betaine-homocysteine S-methyltransferaseGonzález, BeatrizCampillo, Nuria E.Garrido, FranciscoGasset, M.Sanz-Aparicio, J.Pajares, María ÁngelesHomocysteine metabolismKinetic studyMethionine metabolismSite-directed mutagenesis8 pages, 5 figures, 3 tables.A site-directed-mutagenesis study of putative active-site residues in rat liver betaine–homocysteine S-methyltransferase has been carried out. Identification of these amino acids was based on data derived from a structural model of the enzyme. No alterations in the CD spectra or the gel-filtration chromatography elution pattern were observed with the mutants, thus suggesting no modification in the secondary structure content or in the association state of the proteins. All the mutants obtained showed a reduction of the enzyme activity, the most dramatic effect being that of Glu159, followed by Tyr77 and Asp26. Changes in affinity for either of the substrates, homocysteine or betaine, were detected when substitutions were performed of Glu 21, Asp26, Phe74 and Cys186. Interestingly, Asp26, postulated to be involved in homocysteine binding, has a strong effect on affinity for betaine. The relevance of these results is discussed in the light of very recent structural data obtained for the human enzyme.This work was supported by the Fondo de Investigación Sanitaria (grant no. 01/1077 to M.A. P.) and the Ministerio de Ciencia y Tecnología (grant no. BIO2000-1664 to M.G. and BIO2000-1279 to J. S.-A.).Peer reviewedBiochemical SocietyMinisterio de Ciencia y Tecnología (España)Instituto de Salud Carlos III201020102003info:eu-repo/semantics/articlehttp://purl.org/coar/resource_type/c_6501Postprintinfo:eu-repo/semantics/acceptedVersion345054 bytesapplication/pdfhttp://hdl.handle.net/10261/24661reponame:DIGITAL.CSIC. Repositorio Institucional del CSICinstname:Consejo Superior de Investigaciones Científicas (CSIC)Ingléshttps://dx.doi.org/10.1042/FBJ20021510info:eu-repo/semantics/openAccessoai:digital.csic.es:10261/246612026-05-22T06:33:51Z
dc.title.none.fl_str_mv Active-site-mutagenesis study of rat liver betaine-homocysteine S-methyltransferase
title Active-site-mutagenesis study of rat liver betaine-homocysteine S-methyltransferase
spellingShingle Active-site-mutagenesis study of rat liver betaine-homocysteine S-methyltransferase
González, Beatriz
Homocysteine metabolism
Kinetic study
Methionine metabolism
Site-directed mutagenesis
title_short Active-site-mutagenesis study of rat liver betaine-homocysteine S-methyltransferase
title_full Active-site-mutagenesis study of rat liver betaine-homocysteine S-methyltransferase
title_fullStr Active-site-mutagenesis study of rat liver betaine-homocysteine S-methyltransferase
title_full_unstemmed Active-site-mutagenesis study of rat liver betaine-homocysteine S-methyltransferase
title_sort Active-site-mutagenesis study of rat liver betaine-homocysteine S-methyltransferase
dc.creator.none.fl_str_mv González, Beatriz
Campillo, Nuria E.
Garrido, Francisco
Gasset, M.
Sanz-Aparicio, J.
Pajares, María Ángeles
author González, Beatriz
author_facet González, Beatriz
Campillo, Nuria E.
Garrido, Francisco
Gasset, M.
Sanz-Aparicio, J.
Pajares, María Ángeles
author_role author
author2 Campillo, Nuria E.
Garrido, Francisco
Gasset, M.
Sanz-Aparicio, J.
Pajares, María Ángeles
author2_role author
author
author
author
author
dc.contributor.none.fl_str_mv Ministerio de Ciencia y Tecnología (España)
Instituto de Salud Carlos III
dc.subject.none.fl_str_mv Homocysteine metabolism
Kinetic study
Methionine metabolism
Site-directed mutagenesis
topic Homocysteine metabolism
Kinetic study
Methionine metabolism
Site-directed mutagenesis
description 8 pages, 5 figures, 3 tables.
publishDate 2003
dc.date.none.fl_str_mv 2003
2010
2010
dc.type.none.fl_str_mv info:eu-repo/semantics/article
http://purl.org/coar/resource_type/c_6501
Postprint
info:eu-repo/semantics/acceptedVersion
format article
status_str acceptedVersion
dc.identifier.none.fl_str_mv http://hdl.handle.net/10261/24661
url http://hdl.handle.net/10261/24661
dc.language.none.fl_str_mv Inglés
language_invalid_str_mv Inglés
dc.relation.none.fl_str_mv https://dx.doi.org/10.1042/FBJ20021510
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
eu_rights_str_mv openAccess
dc.format.none.fl_str_mv 345054 bytes
application/pdf
dc.publisher.none.fl_str_mv Biochemical Society
publisher.none.fl_str_mv Biochemical Society
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 15,198674

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