NMR Studies of Transient Enzyme-Substrate Interactions

Detalhes bibliográficos
Autor(a) principal: Lança Martins, Maria
Data de Publicação: 2022
Tipo de documento: Dissertação
Idioma: eng
Título da fonte: Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)
Texto Completo: http://hdl.handle.net/10362/163218
Resumo: "McoA is a hyperthermostable multicopper oxidase from Aquifex aeolicus with high oxidative power towards a wide range of natural aromatic compounds that holds great potential for biotechnological applications. McoA sets itself apart from other MCOs due to a highly flexible methionine rich long (Met-loop), located near the substrate-binding site and the T1-Cu catalytic center. Previous studies suggest that the Met-loop has a gatekeeping role, regulating substrate access to the binding pocket which is key for an efficient catalysis. We focused on McoA wild-type, a laccase-like variant (2F4) obtained through directed evolution, and their respective loop-truncated variants."
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spelling NMR Studies of Transient Enzyme-Substrate Interactionsmulticopper oxidasesSTD-NMRmethyl isotope-labeling"McoA is a hyperthermostable multicopper oxidase from Aquifex aeolicus with high oxidative power towards a wide range of natural aromatic compounds that holds great potential for biotechnological applications. McoA sets itself apart from other MCOs due to a highly flexible methionine rich long (Met-loop), located near the substrate-binding site and the T1-Cu catalytic center. Previous studies suggest that the Met-loop has a gatekeeping role, regulating substrate access to the binding pocket which is key for an efficient catalysis. We focused on McoA wild-type, a laccase-like variant (2F4) obtained through directed evolution, and their respective loop-truncated variants."Instituto de Tecnologia Química e Biológica António Xavier. Universidade NOVA de LisboaRUNLança Martins, Maria2024-02-07T17:47:54Z2022-10-012022-10-01T00:00:00Zinfo:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/masterThesisapplication/pdfhttp://hdl.handle.net/10362/163218TID:203518799enginfo: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:RCAAP2024-03-11T05:46:21Zoai:run.unl.pt:10362/163218Portal AgregadorONGhttps://www.rcaap.pt/oai/openaireopendoar:71602024-03-20T03:59:19.087518Repositório 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 NMR Studies of Transient Enzyme-Substrate Interactions
title NMR Studies of Transient Enzyme-Substrate Interactions
spellingShingle NMR Studies of Transient Enzyme-Substrate Interactions
Lança Martins, Maria
multicopper oxidases
STD-NMR
methyl isotope-labeling
title_short NMR Studies of Transient Enzyme-Substrate Interactions
title_full NMR Studies of Transient Enzyme-Substrate Interactions
title_fullStr NMR Studies of Transient Enzyme-Substrate Interactions
title_full_unstemmed NMR Studies of Transient Enzyme-Substrate Interactions
title_sort NMR Studies of Transient Enzyme-Substrate Interactions
author Lança Martins, Maria
author_facet Lança Martins, Maria
author_role author
dc.contributor.none.fl_str_mv RUN
dc.contributor.author.fl_str_mv Lança Martins, Maria
dc.subject.por.fl_str_mv multicopper oxidases
STD-NMR
methyl isotope-labeling
topic multicopper oxidases
STD-NMR
methyl isotope-labeling
description "McoA is a hyperthermostable multicopper oxidase from Aquifex aeolicus with high oxidative power towards a wide range of natural aromatic compounds that holds great potential for biotechnological applications. McoA sets itself apart from other MCOs due to a highly flexible methionine rich long (Met-loop), located near the substrate-binding site and the T1-Cu catalytic center. Previous studies suggest that the Met-loop has a gatekeeping role, regulating substrate access to the binding pocket which is key for an efficient catalysis. We focused on McoA wild-type, a laccase-like variant (2F4) obtained through directed evolution, and their respective loop-truncated variants."
publishDate 2022
dc.date.none.fl_str_mv 2022-10-01
2022-10-01T00:00:00Z
2024-02-07T17:47:54Z
dc.type.status.fl_str_mv info:eu-repo/semantics/publishedVersion
dc.type.driver.fl_str_mv info:eu-repo/semantics/masterThesis
format masterThesis
status_str publishedVersion
dc.identifier.uri.fl_str_mv http://hdl.handle.net/10362/163218
TID:203518799
url http://hdl.handle.net/10362/163218
identifier_str_mv TID:203518799
dc.language.iso.fl_str_mv eng
language eng
dc.rights.driver.fl_str_mv info:eu-repo/semantics/openAccess
eu_rights_str_mv openAccess
dc.format.none.fl_str_mv application/pdf
dc.publisher.none.fl_str_mv Instituto de Tecnologia Química e Biológica António Xavier. Universidade NOVA de Lisboa
publisher.none.fl_str_mv Instituto de Tecnologia Química e Biológica António Xavier. Universidade NOVA de Lisboa
dc.source.none.fl_str_mv reponame:Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)
instname:Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informação
instacron:RCAAP
instname_str Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informação
instacron_str RCAAP
institution RCAAP
reponame_str Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)
collection Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)
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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