The Catalytic Aspartate Is Protonated in the Michaelis Complex Formed between Trypsin and an in Vitro Evolved Substrate-like Inhibitor: A REFINED MECHANISM OF SERINE PROTEASE ACTION

The mechanism of serine proteases prominently illustrates how charged amino acid residues and proton transfer events facilitate enzyme catalysis. Here we present an ultrahigh resolution (0.93 Å) x-ray structure of a complex formed between trypsin and a canonical inhibitor acting through a substrate-...

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Detalles Bibliográficos
Autores principales: Wahlgren, Weixiao Yuan, Pál, Gábor, Kardos, József, Porrogi, Pálma, Szenthe, Borbála, Patthy, András, Gráf, László, Katona, Gergely
Formato: Texto
Lenguaje:English
Publicado: American Society for Biochemistry and Molecular Biology 2011
Materias:
Enzymology
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3030363/
https://www.ncbi.nlm.nih.gov/pubmed/21097875
http://dx.doi.org/10.1074/jbc.M110.161604

Internet

https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3030363/
https://www.ncbi.nlm.nih.gov/pubmed/21097875
http://dx.doi.org/10.1074/jbc.M110.161604

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