Structural Reorganization and Preorganization in Enzyme Active Sites: Comparisons of Experimental and Theoretically Ideal Active Site Geometries in the Multistep Serine Esterase Reaction Cycle

Many enzymes catalyze reactions with multiple chemical steps, requiring the stabilization of multiple transition states during catalysis. Such enzymes must strike a balance between the conformational reorganization required to stabilize multiple transition states of a reaction and the confines of a...

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Veröffentlicht in:	Journal of the American Chemical Society 2008-11, Vol.130 (46), p.15361-15373
Hauptverfasser:	Smith, Adam J. T, Müller, Roger, Toscano, Miguel D, Kast, Peter, Hellinga, Homme W, Hilvert, Donald, Houk, K. N
Format:	Artikel
Sprache:	eng
Schlagworte:	Biocatalysis Butyrylcholinesterase - chemistry Butyrylcholinesterase - metabolism Catalytic Domain Crystallography, X-Ray Esterases - chemistry Esterases - metabolism Models, Molecular Protein Structure, Tertiary
Online-Zugang:	Volltext
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