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National Institutes of Health
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Display of active subtilisin 309 on phage: analysis of parameters influencing the selection of subtilisin variants with changed substrate specificity from libraries using phosphonylating inhibitors.
Journal of molecular biology
Corpus ID: 40388730
Many attempts have been made to endow enzymes with new catalytic activities. One general strategy involves the creation of random…
Substrate specificity of natural variants and genetically engineered intermediates of Bacillus lentus alkaline proteases.
Advances in experimental medicine and biology
Corpus ID: 11089058
Three natural variants of subtilisin lentus could be differentiated by their amino acid sequence and their specific activity with…
Mutational replacements of the amino acid residues forming the hydrophobic S4 binding pocket of subtilisin 309 from Bacillus lentus.
Corpus ID: 42339862
The amino acid side chains of Ile107, Leu126, and Leu135 participate in the formation of the important hydrophobic S4 binding…
Mutational replacements in subtilisin 309. Val104 has a modulating effect on the P4 substrate preference.
European journal of biochemistry
Corpus ID: 33004806
The previous notion that the amino acid side chain at position 104 of subtilisins is involved in the binding of the side chain at…
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