Read more about EC 4.2.1.1 ...
EC 4.2.1.1 - Carbonic anhydrase

  IntEnz view ENZYME view
XML

IntEnz Enzyme Nomenclature
EC 4.2.1.1

Names

Accepted name:
carbonic anhydrase
Other names:
anhydrase
carbonate anhydrase
carbonic acid anhydrase
carbonate dehydratase
carbonic anhydrase A
carboxyanhydrase
carbonic dehydratase
carbonate hydro-lyase
Systematic name:
carbonic acid hydro-lyase (carbon-dioxide-forming)

Reaction

Cofactor

Comments:

The enzyme catalyses the reversible hydration of gaseous CO2 to carbonic acid, which spontaneously converts to hydrogencarbonate under neutral pH. It is widespread and found in archaea, bacteria, and eukaryotes. Three distinct classes exist, and appear to have evolved independently. Contains zinc.

Links to other databases

Enzymes and pathways: NC-IUBMB , BRENDA , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , UniPathway
Protein domains and families: PROSITE:PDOC00146 , PROSITE:PDOC00586
Structural data: CSA , EC2PDB
Gene Ontology: GO:0004089
CAS Registry Number: 9001-03-0
UniProtKB/Swiss-Prot: (148) [show] [UniProt]

References

  1. Keilin, D. and Mann, T.
    Carbonic anhydrase.
    Nature 144 : 442-443 (1939).
  2. Kannan, K. K., Ramanadham, M., Jones, T. A.
    Structure, refinement, and function of carbonic anhydrase isozymes: refinement of human carbonic anhydrase I.
    Ann. N. Y. Acad. Sci. 429 : 49-60 (1984). [PMID: 6430186]
  3. Murakami, H., Sly, W. S.
    Purification and characterization of human salivary carbonic anhydrase.
    J. Biol. Chem. 262 : 1382-1388 (1987). [PMID: 2433278]
  4. Iverson, T. M., Alber, B. E., Kisker, C., Ferry, J. G., Rees, D. C.
    A closer look at the active site of gamma-class carbonic anhydrases: high-resolution crystallographic studies of the carbonic anhydrase from Methanosarcina thermophila.
    Biochemistry 39 : 9222-9231 (2000). [PMID: 10924115]
  5. Smith, K. S., Ferry, J. G.
    Prokaryotic carbonic anhydrases.
    FEMS Microbiol. Rev. 24 : 335-366 (2000). [PMID: 10978542]
  6. Cronk, J. D., Endrizzi, J. A., Cronk, M. R., O'neill, J. W., Zhang, K. Y.
    Crystal structure of E. coli beta-carbonic anhydrase, an enzyme with an unusual pH-dependent activity.
    Protein Sci. 10 : 911-922 (2001). [PMID: 11316870]
  7. Merlin, C., Masters, M., McAteer, S., Coulson, A.
    Why is carbonic anhydrase essential to Escherichia coli?
    J. Bacteriol. 185 : 6415-6424 (2003). [PMID: 14563877]

[EC 4.2.1.1 created 1961, modified 2016]