Significance of hydrophobic S4-P4 interactions in subtilisin 309 from Bacillus lentus

The subtilisins have an extended substrate binding cleft comprising at least 8 subsites. Two pockets at the S1 and S4 sites are particularly conspicuous, and the interactions between substrate and these two pockets are very important for the substrate specificity. Phe residues have mutationally been...

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Veröffentlicht in:	Biochemistry (Easton) 1993-03, Vol.32 (11), p.2845-2852
Hauptverfasser:	Bech, Lene M, Soerensen, Steen Bech, Breddam, Klaus
Format:	Artikel
Sprache:	eng
Schlagworte:	Amino Acid Sequence Analytical, structural and metabolic biochemistry Bacillus - enzymology Bacillus - genetics Binding Sites Biological and medical sciences Calorimetry Cloning, Molecular Enzymes and enzyme inhibitors Escherichia coli - genetics Fundamental and applied biological sciences. Psychology Hydrolases Kinetics Models, Molecular Molecular Sequence Data Mutagenesis, Site-Directed Oligopeptides - metabolism Protein Conformation Recombinant Proteins - chemistry Recombinant Proteins - metabolism Serine Endopeptidases - chemistry Serine Endopeptidases - genetics Serine Endopeptidases - metabolism Substrate Specificity Subtilisins - chemistry Subtilisins - genetics Subtilisins - metabolism
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