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Article

The role of tryptophan residues in the autoprocessing of prosubtilisin E.

Biochimica et biophysica acta - 20 May 2005

Sone Michio, Falzon Liliana, Inouye Masayori

Abstract excerpt

Subtilisin E, a serine protease from Bacillus subtilis, requires an N-terminal propeptide for its correct folding. The propeptide is autocleaved and digested by the subtilisin domain upon proper folding. Here we investigated the individual roles of the three Trp residues within the subtilisin domain (Trp106, Trp113 and Trp241) on propeptide processing, enzymatic activity and stability of subtilisin. When the...

Topics

Bacillus subtilis
Bacterial Proteins
Enzyme Precursors
Mutation
Peptide Fragments
Protein Folding
Protein Structure, Secondary
Protein Structure, Tertiary
Subtilisins
Tryptophan

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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PMID: 15848132
DOI: 10.1016/j.bbapap.2005.01.011

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