Plant serine proteases: biochemical, physiological and molecular features

Detalhes bibliográficos
Autor(a) principal: Antão, Cecília M.
Data de Publicação: 2005
Outros Autores: Malcata, F. Xavier
Tipo de documento: Artigo
Idioma: eng
Título da fonte: Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)
Texto Completo: http://hdl.handle.net/10400.14/3390
Resumo: In the latest two decades, the interest received by plant proteases has been on the rise. Serine proteases (EC 3.4.21)—in particular those from cucurbits, cereals and trees—share indeed a number of biochemical and physiological features, that may prove useful toward understanding of several mechanisms at the subcellular level. This critical review focuses on the characterization of most plant serine proteases, and comprehensively lists information produced by more and more sophisticated research tools that have led to the current state of the art in knowledge of these unique enzymes.
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spelling Plant serine proteases: biochemical, physiological and molecular featuresEnzymeMechanismSubstrate specificityFunctionIn the latest two decades, the interest received by plant proteases has been on the rise. Serine proteases (EC 3.4.21)—in particular those from cucurbits, cereals and trees—share indeed a number of biochemical and physiological features, that may prove useful toward understanding of several mechanisms at the subcellular level. This critical review focuses on the characterization of most plant serine proteases, and comprehensively lists information produced by more and more sophisticated research tools that have led to the current state of the art in knowledge of these unique enzymes.ElsevierVeritati - Repositório Institucional da Universidade Católica PortuguesaAntão, Cecília M.Malcata, F. Xavier2010-11-11T17:01:23Z20052005-01-01T00:00:00Zinfo:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/articleapplication/pdfhttp://hdl.handle.net/10400.14/3390engANTÃO, Cecília M. ; MALCATA, F. Xavier - Plant serine proteases: biochemical, physiological and molecular features. Plant Physiology and Biochemistry. ISSN 0981-9428. Vol. 43, n.º 7 (2005), p. 637–650info:eu-repo/semantics/openAccessreponame:Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)instname:Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informaçãoinstacron:RCAAP2023-07-12T17:09:26Zoai:repositorio.ucp.pt:10400.14/3390Portal AgregadorONGhttps://www.rcaap.pt/oai/openaireopendoar:71602024-03-19T18:05:04.421321Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) - Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informaçãofalse
dc.title.none.fl_str_mv Plant serine proteases: biochemical, physiological and molecular features
title Plant serine proteases: biochemical, physiological and molecular features
spellingShingle Plant serine proteases: biochemical, physiological and molecular features
Antão, Cecília M.
Enzyme
Mechanism
Substrate specificity
Function
title_short Plant serine proteases: biochemical, physiological and molecular features
title_full Plant serine proteases: biochemical, physiological and molecular features
title_fullStr Plant serine proteases: biochemical, physiological and molecular features
title_full_unstemmed Plant serine proteases: biochemical, physiological and molecular features
title_sort Plant serine proteases: biochemical, physiological and molecular features
author Antão, Cecília M.
author_facet Antão, Cecília M.
Malcata, F. Xavier
author_role author
author2 Malcata, F. Xavier
author2_role author
dc.contributor.none.fl_str_mv Veritati - Repositório Institucional da Universidade Católica Portuguesa
dc.contributor.author.fl_str_mv Antão, Cecília M.
Malcata, F. Xavier
dc.subject.por.fl_str_mv Enzyme
Mechanism
Substrate specificity
Function
topic Enzyme
Mechanism
Substrate specificity
Function
description In the latest two decades, the interest received by plant proteases has been on the rise. Serine proteases (EC 3.4.21)—in particular those from cucurbits, cereals and trees—share indeed a number of biochemical and physiological features, that may prove useful toward understanding of several mechanisms at the subcellular level. This critical review focuses on the characterization of most plant serine proteases, and comprehensively lists information produced by more and more sophisticated research tools that have led to the current state of the art in knowledge of these unique enzymes.
publishDate 2005
dc.date.none.fl_str_mv 2005
2005-01-01T00:00:00Z
2010-11-11T17:01:23Z
dc.type.status.fl_str_mv info:eu-repo/semantics/publishedVersion
dc.type.driver.fl_str_mv info:eu-repo/semantics/article
format article
status_str publishedVersion
dc.identifier.uri.fl_str_mv http://hdl.handle.net/10400.14/3390
url http://hdl.handle.net/10400.14/3390
dc.language.iso.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv ANTÃO, Cecília M. ; MALCATA, F. Xavier - Plant serine proteases: biochemical, physiological and molecular features. Plant Physiology and Biochemistry. ISSN 0981-9428. Vol. 43, n.º 7 (2005), p. 637–650
dc.rights.driver.fl_str_mv info:eu-repo/semantics/openAccess
eu_rights_str_mv openAccess
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dc.publisher.none.fl_str_mv Elsevier
publisher.none.fl_str_mv Elsevier
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repository.name.fl_str_mv Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) - Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informação
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