Article
ACE-domain selectivity extends beyond direct interacting residues at the active site.
The Biochemical journal - 17 Apr 2020
Cozier Gyles E, Lubbe Lizelle, Sturrock Edward D, Acharya K Ravi
Abstract excerpt
Angiotensin-converting enzyme (ACE) is best known for its formation of the vasopressor angiotensin II that controls blood pressure but is also involved in other physiological functions through the hydrolysis of a variety of peptide substrates. The enzyme contains two catalytic domains (nACE and cACE) that have different affinities for ACE substrates and inhibitors. We investigated whether nACE inhibitor backbones...
Topics
- Angiotensin-Converting Enzyme Inhibitors
- Blood Pressure
- Catalytic Domain
- Crystallography, X-Ray
- Glycosylation
- Humans
- Kinetics
- Ligands
- Metalloendopeptidases
- Mutant Proteins
- Mutation
- Peptidyl-Dipeptidase A
- Protein Binding
- Protein Conformation, beta-Strand
- Renin-Angiotensin System