Article
Changes in activity of porcine phospholipase A2 brought about by charge engineering of a major structural element to alter stability.
Protein engineering - 1 Dec 1991
Goodenough P W, Bhat K M, Collins M E, Perry B N, Pickersgill R W, Sumner I G, Warwicker J, de Haas G H, Verheij H M
Abstract excerpt
We have modified the stability of porcine phospholipase A2 by charge engineering. The mutations are situated at the N-terminal of a major helix and are N89D and N89D/E92Q. This engineering has significantly altered the activity of the enzyme to aggregated and monomeric substrates. A N89D/E92K mutant is more stable but considerably less active than wild type. An N89D mutant is more stable and of similar activity...
Topics
- Animals
- Base Sequence
- Binding Sites
- Calcium
- Enzyme Stability
- Escherichia coli
- Gene Expression
- Models, Chemical
- Models, Molecular
- Molecular Sequence Data
- Mutagenesis