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Overview for MACiE Entry M0216

Version history

General Information

EC Number: 4.2.1.1 (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:

Display structure information

Overall Reaction:

Image of Carbon dioxide

Image of Water

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Image of Carbonic acid

Carbon dioxide
C00011
CHEBI:16526
Water
C00001
CHEBI:15377
Carbonic acid
C01353
CHEBI:28976

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 1Zinc 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 2Bicarbonate is displaced by water. His64 deprotonates the zinc bound water.
Step 3Water deprotonates His64.

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Catalytic Residues Involved

Type Number Chain Location of Function
His 64 A Side Chain
Glu 106 A Side Chain
Thr 199 A Side Chain

Metal Cofactors for M0216

Type Het group Number Chain
zinc ZN 262 _ Overview

References

  1. 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.
    Medline: 15667203
  2. 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.
    Medline: 2514797
  3. A. E. Eriksson et al. (1988), Proteins, 4, 274-282. Refined structure of human carbonic anhydrase II at 2.0 A resolution.
    Medline: 3151019
  4. 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.
    Medline: 9761692
  5. C. T. Supuran et al. (2003), Med. Res. Rev., 23, 1460189-0. Carbonic anhydrase inhibitors.
    Medline: 12500287
  6. S. Lindskog (1997), Pharmacol. Ther., 74, 1-20. Structure and mechanism of carbonic anhydrase.
    Medline: 9336012

Homologue information for M0216 (1ca2)

CSA Homologues

MACiE Homologues (within the PDB)

MACiE Homologues (within UniprotKB/SwissProt)


Links to this entry in other databases

Link to EC-PDB-SUM Link to PDB-SUM Link to RCSB PDB Link to PDBe Link to CSA
Link to MetaCyc Link to KEGG Link to BRENDA Link to ExplorENZ

GOA logo
kidney development (biological process)
morphogenesis of an epithelium (biological process)
carbonate dehydratase activity (molecular function)
extracellular space (cellular component)
cytoplasm (cellular component)
cytosol (cellular component)
microvillus (cellular component)
one-carbon metabolic process (biological process)
response to stress (biological process)
zinc ion binding (molecular function)
response to pH (biological process)
response to organic substance (biological process)
response to zinc ion (biological process)
carbon dioxide transport (biological process)
basolateral plasma membrane (cellular component)
lyase activity (molecular function)
axon (cellular component)
positive regulation of cellular pH reduction (biological process)
odontogenesis of dentin-containing tooth (biological process)
response to estrogen (biological process)
apical part of cell (cellular component)
positive regulation of osteoclast differentiation (biological process)
positive regulation of bone resorption (biological process)
metal ion binding (molecular function)
secretion (biological process)
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