The dataset from a 2001 study by researchers including E. Cama at the University of Pennsylvania details the X-ray crystal structure of human arginase II. It includes data on the enzyme's structure determined at 2.7 Å resolution, complexed with a boronic acid inhibitor. The study links arginase II activity to the regulation of nitric oxide synthase in male and female sexual arousal tissues.
Use Cases
- Modeling enzyme-inhibitor interactions based on the described boronic acid transition state analogue.
- Studying metal-activated hydroxide mechanisms in metalloenzymes based on the described catalytic process.
- Investigating l-arginine bioavailability regulation in smooth muscle tissue as mentioned in the physiological role.
- Identifying potential drug targets for erectile dysfunction based on the described inhibition strategy.
Strengths
- Structure determined at a specific 2.7 Å resolution.
- Data is linked to a specific, peer-reviewed publication (Biochemistry, 2001, 40, 2678-2688).
- Includes physiological context for both male and female sexual arousal based on described hemodynamic studies.
Limitations
- Column-level documentation is absent; field semantics must be inferred after download.
- Row count is unknown, which may limit suitability assessment.
- Last update date is unknown; freshness unverified.
Provenance
- Source
- University of Pennsylvania
- Collection Method
- X-ray crystallography and physiological studies, as described in the referenced paper.