Impact of the lysine-188 and aspartic acid-189 inversion on activity of trypsin

The impact of the charge rearrangement on the specificity of trypsin was tested by an inversion of sequence K188D/D189K maintaining the integrity of the charges of the substrate binding pocket when switching their polarity. In native trypsin, aspartate 189 situated at the bottom of the primary subst...

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Veröffentlicht in:	FEBS letters 1999-01, Vol.442 (1), p.43-47
Hauptverfasser:	Briand, Loı̈c, Chobert, Jean-Marc, Gantier, René, Declerck, Nathalie, Tran, Vinh, Léonil, Joëlle, Mollé, Daniel, Haertlé, Thomas
Format:	Artikel
Sprache:	eng
Schlagworte:	Animals Aspartic Acid - chemistry Catalytic Domain - genetics Cellular Biology Computer Simulation Escherichia coli - genetics In Vitro Techniques Kinetics Life Sciences Lysine - chemistry Models, Molecular Mutagenesis, Site-Directed Protease Protein Conformation Rats Recombinant Proteins - chemistry Recombinant Proteins - metabolism Site-directed mutagenesis Substrate Specificity Synthetic substrate Toxicology Trypsin Trypsin - chemistry Trypsin - genetics Trypsin - metabolism
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