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Literature summary extracted from

  • Yachandra, V.; Powers, L.; Spiro, T.G.
    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

EC Number Inhibitors Comment Organism Structure
4.2.1.1 acetate
-
Bos taurus
4.2.1.1 acetazolamide
-
Bos taurus
4.2.1.1 Cl-
-
Bos taurus
4.2.1.1 CN-
-
Bos taurus
4.2.1.1 HCO3-
-
Bos taurus
4.2.1.1 imidazole
-
Bos taurus
4.2.1.1 NO3-
-
Bos taurus
4.2.1.1 OCN-
-
Bos taurus
4.2.1.1 SCN-
-
Bos taurus

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
4.2.1.1 Co2+ the Co2+-enzyme shows a definite propensity for five-coordination Bos taurus
4.2.1.1 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

EC Number Organism UniProt Comment Textmining
4.2.1.1 Bos taurus
-
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4.2.1.1 CO2 + H2O
-
Bos taurus H2CO3
-
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