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Publicação
NMR Studies of Transient Enzyme-Substrate Interactions
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| 3.35 MB | Adobe PDF |
Autores
Orientador(es)
Resumo(s)
"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."
Descrição
Palavras-chave
multicopper oxidases STD-NMR methyl isotope-labeling
Contexto Educativo
Citação
Editora
Instituto de Tecnologia Química e Biológica António Xavier. Universidade NOVA de Lisboa