Article
Mutational analysis of residues in and around the active site of human fibroblast-type collagenase.
The Journal of biological chemistry - 21 Oct 1994
Windsor L J, Bodden M K, Birkedal-Hansen B, Engler J A, Birkedal-Hansen H
Abstract excerpt
Mutants in and around the catalytic zinc-binding site of human fibroblast-type collagenase have been expressed in Escherichia coli. Replacement of each of the three zinc ligands, His-199, His-203, and His-209, in the active site sequence: VAAHEXGHXXGXXH, not only destroyed catalytic activity but also led to improper folding of the polypeptide, suggesting that this sequence also serves as a structural zinc-binding...
Topics
- Amino Acid Sequence
- Base Sequence
- Binding Sites
- Caseins
- Collagenases
- Escherichia coli
- Fibroblasts
- Glycoproteins
- Humans
- Molecular Sequence Data
- Mutation
