Cargando…
Structure of a Switchable Subtilisin Complexed with a Substrate and with the Activator Azide
[Image: see text] An engineered variant of the protease subtilisin from Bacillus amyloliquefaciens, in which the D32A mutation renders the enzyme’s activity dependent on the presence of certain small anions such as fluoride or azide, has been produced. This modified enzyme has applications as an azi...
Autores principales: | Gallagher, Travis, Ruan, Biao, London, Mariya, Bryan, Molly A., Bryan, Philip N. |
---|---|
Formato: | Texto |
Lenguaje: | English |
Publicado: |
American Chemical Society
2009
|
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2979009/ https://www.ncbi.nlm.nih.gov/pubmed/19761257 http://dx.doi.org/10.1021/bi900577n |
Ejemplares similares
-
Engineering subtilisin proteases that specifically degrade active RAS
por: Chen, Yingwei, et al.
Publicado: (2021) -
The role of substrate specificity and metal binding in defining the activity and structure of an intracellular subtilisin
por: Gamble, Michael, et al.
Publicado: (2012) -
Three-Component Azidation of Styrene-Type Double Bonds: Light-Switchable Behavior of a Copper Photoredox Catalyst**
por: Fumagalli, Gabriele, et al.
Publicado: (2015) -
Late Stage Azidation of Complex Molecules
por: Karimov, Rashad R., et al.
Publicado: (2016) -
Activity Guided Azide-methyllysine
Photo-trapping
for Substrate Profiling of Lysine Demethylases
por: Kuwik, Jordan, et al.
Publicado: (2023)