Unusual ligand binding at the active site domain of an engineered mutant of subtilisin BL.

doi:10.1007/978-1-4613-0319-0_27

Back to search

Article

Unusual ligand binding at the active site domain of an engineered mutant of subtilisin BL.

Advances in experimental medicine and biology - 1 Jan 1996

Paech C, Goddette D W, Christianson T, Wilson C R

Abstract excerpt

As an attempt to recruit the third calcium binding site of thermitase into subtilisin BL, a Bacillus lentus alkaline protease (BLAP), the amino acid sequence from position 50 to 60 and position 92 was modified to the equivalent amino acids in thermitase. The resulting protein, designated BLAPm109...

Topics

Amino Acid Sequence
Bacillus
Binding Sites
Dimerization
Molecular Sequence Data
Mutation
Peptide Mapping
Protein Engineering
Protein Structure, Tertiary
Subtilisins

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.