Article
Formation of disulfide bonds in insect prophenoloxidase enhances immunity through improving enzyme activity and stability.
Developmental and comparative immunology - 1 Jun 2014
Lu Anrui, Peng Qin, Ling Erjun
Abstract excerpt
Type 3 copper proteins, including insect prophenoloxidase (PPO), contain two copper atoms in the active site pocket and can oxidize phenols. Insect PPO plays an important role in immunity. Insects and other invertebrates show limited recovery from pathogen invasion and wounds if phenoloxidase (PO) activity is low. In most insect PPOs, two disulfide bonds are present near the C-terminus. However, in Pimpla...
Topics
- Animals
- Bacillus subtilis
- Catechol Oxidase
- Cells, Cultured
- Copper
- Drosophila melanogaster
- Enzyme Activation
- Enzyme Precursors
- Enzyme Stability
- Escherichia coli
- Escherichia coli Infections
- Gram-Positive Bacterial Infections
- Immunity
- Insect Proteins
- Molecular Structure
- Mutation
- Recombinant Proteins
- Wasps