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subtilisin 309

National Institutes of Health

Papers overview

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1996
1996
Substrate specificity of natural variants and genetically engineered intermediates of Bacillus lentus alkaline proteases.
Three natural variants of subtilisin lentus could be differentiated by their amino acid sequence and their specific activity with… 
1993
1993
Mutational replacements of the amino acid residues forming the hydrophobic S4 binding pocket of subtilisin 309 from Bacillus lentus.
The amino acid side chains of Ile107, Leu126, and Leu135 participate in the formation of the important hydrophobic S4 binding… 
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