Converting trypsin to elastase: substitution of the S1 site and adjacent loops reconstitutes esterase specificity but not amidase activity.

doi:10.1093/protein/11.8.669

Back to search

Article

Converting trypsin to elastase: substitution of the S1 site and adjacent loops reconstitutes esterase specificity but not amidase activity.

Protein engineering - 1 Aug 1998

Hung S H, Hedstrom L

Abstract excerpt

The conversion of trypsin into a protease with chymotrypsin-like activity and specificity required substitution of fifteen residues in the S1 site and two surface loops with their chymotrypsin counterparts [Hedstrom,L., Szilagyi,L. and Rutter,W.J. (1992) Science, 255, 1249-1253]. These residues m...

Topics

Amidohydrolases
Amino Acid Sequence
Chymotrypsin
Esterases
Magnetic Resonance Spectroscopy
Molecular Sequence Data
Mutation
Pancreatic Elastase
Recombinant Proteins
Substrate Specificity
Trypsin

Community interpretation

Discuss the evidence

Ask a question, add context or challenge an interpretation. Community activity is separate from scientific evidence strength.

discussions

replies

Citations encouraged

Claims remain attributable.

No discussion yet

Be the first to add a careful, cited interpretation.