Cargando…
Experimental and Computational Mutagenesis To Investigate the Positioning of a General Base within an Enzyme Active Site
[Image: see text] The positioning of catalytic groups within proteins plays an important role in enzyme catalysis, and here we investigate the positioning of the general base in the enzyme ketosteroid isomerase (KSI). The oxygen atoms of Asp38, the general base in KSI, were previously shown to be in...
Autores principales: | Schwans, Jason P., Hanoian, Philip, Lengerich, Benjamin J., Sunden, Fanny, Gonzalez, Ana, Tsai, Yingssu, Hammes-Schiffer, Sharon, Herschlag, Daniel |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
American
Chemical Society
2014
|
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4004248/ https://www.ncbi.nlm.nih.gov/pubmed/24597914 http://dx.doi.org/10.1021/bi401671t |
Ejemplares similares
-
Perspectives on Electrostatics and Conformational
Motions in Enzyme Catalysis
por: Hanoian, Philip, et al.
Publicado: (2015) -
Extensive site-directed mutagenesis reveals interconnected functional units in the alkaline phosphatase active site
por: Sunden, Fanny, et al.
Publicado: (2015) -
Using Unnatural
Amino Acids to Probe the Energetics
of Oxyanion Hole Hydrogen Bonds in the Ketosteroid Isomerase Active
Site
por: Natarajan, Aditya, et al.
Publicado: (2014) -
Probing the Electrostatics
of Active Site Microenvironments
along the Catalytic Cycle for Escherichia coli Dihydrofolate Reductase
por: Liu, C. Tony, et al.
Publicado: (2014) -
Enhanced Rigidification within a Double Mutant of
Soybean Lipoxygenase Provides Experimental Support for Vibronically
Nonadiabatic Proton-Coupled Electron Transfer Models
por: Hu, Shenshen, et al.
Publicado: (2017)