Overview for MACiE Entry M0216
EC Number: 188.8.131.52 (A member of the Lyases, Carbon-oxygen lyases, Hydro-lyases)
Enzyme Name: carbonate dehydratase
Biological Species: Homo sapiens (Human)
Catalytic Chain UniprotKB Accession Codes:
Representative PDB Code: 1ca2 - REFINED STRUCTURE OF HUMAN CARBONIC ANHYDRASE II AT 2.0ANGSTROMS RESOLUTION (Resolution = 2.00 Å).
Catalytic CATH Codes:
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Overall Comment: Although the mechanism of action between the prokaryotic and eukaryotic carbonic anhydrase enzymes is the same, the ligands binding the zinc cofactor are different.
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Stepwise Description of the Reaction
|Step 1||Zinc activated water attacks the carbon of carbon dioxide in a nucleophilic addition, which results in the bicarbonate moiety being bound to the zinc in a bidentate manner.|
|Step 2||Bicarbonate is displaced by water. His64 deprotonates the zinc bound water.|
|Step 3||Water deprotonates His64.|
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Catalytic Residues Involved
||Location of Function
Metal Cofactors for M0216
- Z. Fisher et al. (2005), Biochemistry, 44, 1097-1105. Structural and kinetic characterization of active-site histidine as a proton shuttle in catalysis by human carbonic anhydrase II.
- C. Tu et al. (1989), Biochemistry, 28, 7913-7918. Role of histidine 64 in the catalytic mechanism of human carbonic anhydrase II studied with a site-specific mutant.
- A. E. Eriksson et al. (1988), Proteins, 4, 274-282. Refined structure of human carbonic anhydrase II at 2.0 A resolution.
- S. Huang et al. (1998), J. Mol. Biol., 283, 301-310. Crystal structure of carbonic anhydrase from Neisseria gonorrhoeae and its complex with the inhibitor acetazolamide.
- C. T. Supuran et al. (2003), Med. Res. Rev., 23, 1460189-0. Carbonic anhydrase inhibitors.
- S. Lindskog (1997), Pharmacol. Ther., 74, 1-20. Structure and mechanism of carbonic anhydrase.
Homologue information for M0216 (1ca2)
MACiE Homologues (within the PDB)
MACiE Homologues (within UniprotKB/SwissProt)
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