Uma perspectiva computacional sobre catálise enzimática

Detalhes bibliográficos
Autor(a) principal: Arantes,Guilherme M.
Data de Publicação: 2008
Tipo de documento: Artigo
Idioma: por
Título da fonte: Química Nova (Online)
Texto Completo: http://old.scielo.br/scielo.php?script=sci_arttext&pid=S0100-40422008000200034
Resumo: Enzymes are extremely efficient catalysts. Here, part of the mechanisms proposed to explain this catalytic power will be compared to quantitative experimental results and computer simulations. Influence of the enzymatic environment over species along the reaction coordinate will be analysed. Concepts of transition state stabilisation and reactant destabilisation will be confronted. Divided site model and near-attack conformation hypotheses will also be discussed. Molecular interactions such as covalent catalysis, general acid-base catalysis, electrostatics, entropic effects, steric hindrance, quantum and dynamical effects will also be analysed as sources of catalysis. Reaction mechanisms, in particular that catalysed by protein tyrosine phosphatases, illustrate the concepts.
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spelling Uma perspectiva computacional sobre catálise enzimáticaenzymatic catalysiscomputer simulationreaction mechanismEnzymes are extremely efficient catalysts. Here, part of the mechanisms proposed to explain this catalytic power will be compared to quantitative experimental results and computer simulations. Influence of the enzymatic environment over species along the reaction coordinate will be analysed. Concepts of transition state stabilisation and reactant destabilisation will be confronted. Divided site model and near-attack conformation hypotheses will also be discussed. Molecular interactions such as covalent catalysis, general acid-base catalysis, electrostatics, entropic effects, steric hindrance, quantum and dynamical effects will also be analysed as sources of catalysis. Reaction mechanisms, in particular that catalysed by protein tyrosine phosphatases, illustrate the concepts.Sociedade Brasileira de Química2008-01-01info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersiontext/htmlhttp://old.scielo.br/scielo.php?script=sci_arttext&pid=S0100-40422008000200034Química Nova v.31 n.2 2008reponame:Química Nova (Online)instname:Sociedade Brasileira de Química (SBQ)instacron:SBQ10.1590/S0100-40422008000200034info:eu-repo/semantics/openAccessArantes,Guilherme M.por2017-10-17T00:00:00Zoai:scielo:S0100-40422008000200034Revistahttps://www.scielo.br/j/qn/ONGhttps://old.scielo.br/oai/scielo-oai.phpquimicanova@sbq.org.br1678-70640100-4042opendoar:2017-10-17T00:00Química Nova (Online) - Sociedade Brasileira de Química (SBQ)false
dc.title.none.fl_str_mv Uma perspectiva computacional sobre catálise enzimática
title Uma perspectiva computacional sobre catálise enzimática
spellingShingle Uma perspectiva computacional sobre catálise enzimática
Arantes,Guilherme M.
enzymatic catalysis
computer simulation
reaction mechanism
title_short Uma perspectiva computacional sobre catálise enzimática
title_full Uma perspectiva computacional sobre catálise enzimática
title_fullStr Uma perspectiva computacional sobre catálise enzimática
title_full_unstemmed Uma perspectiva computacional sobre catálise enzimática
title_sort Uma perspectiva computacional sobre catálise enzimática
author Arantes,Guilherme M.
author_facet Arantes,Guilherme M.
author_role author
dc.contributor.author.fl_str_mv Arantes,Guilherme M.
dc.subject.por.fl_str_mv enzymatic catalysis
computer simulation
reaction mechanism
topic enzymatic catalysis
computer simulation
reaction mechanism
description Enzymes are extremely efficient catalysts. Here, part of the mechanisms proposed to explain this catalytic power will be compared to quantitative experimental results and computer simulations. Influence of the enzymatic environment over species along the reaction coordinate will be analysed. Concepts of transition state stabilisation and reactant destabilisation will be confronted. Divided site model and near-attack conformation hypotheses will also be discussed. Molecular interactions such as covalent catalysis, general acid-base catalysis, electrostatics, entropic effects, steric hindrance, quantum and dynamical effects will also be analysed as sources of catalysis. Reaction mechanisms, in particular that catalysed by protein tyrosine phosphatases, illustrate the concepts.
publishDate 2008
dc.date.none.fl_str_mv 2008-01-01
dc.type.driver.fl_str_mv info:eu-repo/semantics/article
dc.type.status.fl_str_mv info:eu-repo/semantics/publishedVersion
format article
status_str publishedVersion
dc.identifier.uri.fl_str_mv http://old.scielo.br/scielo.php?script=sci_arttext&pid=S0100-40422008000200034
url http://old.scielo.br/scielo.php?script=sci_arttext&pid=S0100-40422008000200034
dc.language.iso.fl_str_mv por
language por
dc.relation.none.fl_str_mv 10.1590/S0100-40422008000200034
dc.rights.driver.fl_str_mv info:eu-repo/semantics/openAccess
eu_rights_str_mv openAccess
dc.format.none.fl_str_mv text/html
dc.publisher.none.fl_str_mv Sociedade Brasileira de Química
publisher.none.fl_str_mv Sociedade Brasileira de Química
dc.source.none.fl_str_mv Química Nova v.31 n.2 2008
reponame:Química Nova (Online)
instname:Sociedade Brasileira de Química (SBQ)
instacron:SBQ
instname_str Sociedade Brasileira de Química (SBQ)
instacron_str SBQ
institution SBQ
reponame_str Química Nova (Online)
collection Química Nova (Online)
repository.name.fl_str_mv Química Nova (Online) - Sociedade Brasileira de Química (SBQ)
repository.mail.fl_str_mv quimicanova@sbq.org.br
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