Designing Substrate Specificity by Protein Engineering of Electrostatic Interactions

Protein engineering of electrostatic interactions between charged substrates and complementary charged amino acids, at two different sites in the substrate binding cleft of the protease subtilisin BPN′, increases kcat/Kmtoward complementary charged substrates (up to 1900 times) and decreases kcat/Km...

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Veröffentlicht in:	Proceedings of the National Academy of Sciences - PNAS 1987-03, Vol.84 (5), p.1219-1223
Hauptverfasser:	Wells, James A., Powers, David B., Bott, Richard R., Graycar, Thomas P., Estell, David A.
Format:	Artikel
Sprache:	eng
Schlagworte:	Analytical, structural and metabolic biochemistry Bacillus amyloliquefaciens Binding Sites Biochemistry Biological and medical sciences Design engineering Electrochemistry electrostatic properties Electrostatics Enzyme substrates Enzymes Fundamental and applied biological sciences. Psychology General aspects, investigation methods Genes Genetic Engineering - methods Ions Models, Molecular Mutation Permittivity Protein Conformation Protein engineering Proteins Recombinant Proteins - metabolism Substrate Specificity subtilisin Subtilisins - genetics Subtilisins - metabolism X-Ray Diffraction
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