6UX1
Carbonic Anhydrase II Complexed with Salicylic Acid
Summary for 6UX1
| Entry DOI | 10.2210/pdb6ux1/pdb |
| Descriptor | Carbonic anhydrase 2, ZINC ION, GLYCEROL, ... (6 entities in total) |
| Functional Keywords | aspirin salicylic acid, esterase, lyase |
| Biological source | Homo sapiens (Human) |
| Total number of polymer chains | 1 |
| Total formula weight | 30121.19 |
| Authors | Andring, J.T.,Combs, J.E.,McKenna, R. (deposition date: 2019-11-06, release date: 2020-04-22, Last modification date: 2023-10-11) |
| Primary citation | Andring, J.,Combs, J.,McKenna, R. Aspirin: A Suicide Inhibitor of Carbonic Anhydrase II. Biomolecules, 10:-, 2020 Cited by PubMed Abstract: Carbonic anhydrase II (CAII) is a metalloenzyme that catalyzes the reversible hydration/dehydration of CO/HCO. In addition, CAII is attributed to other catalytic reactions, including esterase activity. Aspirin (acetyl-salicylic acid), an everyday over-the-counter drug, has both ester and carboxylic acid moieties. Recently, compounds with a carboxylic acid group have been shown to inhibit CAII. Hence, we hypothesized that Aspirin could act as a substrate for esterase activity, and the product salicylic acid (SA), an inhibitor of CAII. Here, we present the crystal structure of CAII in complex with SA, a product of CAII crystals pre-soaked with Aspirin, to 1.35Å resolution. In addition, we provide kinetic data to support the observation that CAII converts Aspirin to its deacetylated form, SA. This data may also explain the short half-life of Aspirin, with CAII so abundant in blood, and that Aspirin could act as a suicide inhibitor of CAII. PubMed: 32244293DOI: 10.3390/biom10040527 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.36 Å) |
Structure validation
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