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Literature summary for 4.2.1.1 extracted from
- X-ray absorption spectra and the coordination number of Zn and Co carbonic anhydrase as a function of pH and inhibitor binding (1983), J. Am. Chem. Soc., 105, 6596-6604.
No PubMed abstract available
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| acetate | - |
Bos taurus |  |
| acetazolamide | - |
Bos taurus | |
| Cl- | - |
Bos taurus | |
| CN- | - |
Bos taurus | |
| HCO3- | - |
Bos taurus | |
| imidazole | - |
Bos taurus | |
| NO3- | - |
Bos taurus | |
| OCN- | - |
Bos taurus | |
| SCN- | - |
Bos taurus | |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Co2+ | the Co2+-enzyme shows a definite propensity for five-coordination | Bos taurus | |
| Zinc | the Zn2+ enzyme remains essentially fourcoordinate in all its forms, although alterations in the K-edge shape imply differences in coordination geometry | Bos taurus | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Bos taurus | - |
- |
- |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| CO2 + H2O | - |
Bos taurus | H2CO3 | - |
? | |
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