The Enzyme Database

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EC 4.2.1.1     
Accepted name: carbonic anhydrase
Reaction: H2CO3 = CO2 + H2O
Other name(s): carbonate dehydratase; anhydrase; carbonate anhydrase; carbonic acid anhydrase; carboxyanhydrase; carbonic anhydrase A; carbonate hydro-lyase; carbonate hydro-lyase (carbon-dioxide-forming)
Systematic name: carbonic acid hydro-lyase (carbon-dioxide-forming)
Comments: The enzyme catalyses the reversible hydration of dissolved CO2 to carbonic acid, which dissociates to give hydrogencarbonate above neutral pH. It is widespread and found in archaea, bacteria, and eukaryotes. At least eight distinct classes exist and appear to have evolved independently. A large majority of the enzymes contain a metal cofactor. Zn2+ is the most prevalent, but Cd2+, Co2+, Fe2+, and Mn2+ are also found [8].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9001-03-0
References:
1.  Keilin, D. and Mann, T. Carbonic anhydrase. Nature 144 (1939) 442–443. [DOI]
2.  Kannan, K.K., Ramanadham, M. and Jones, T.A. Structure, refinement, and function of carbonic anhydrase isozymes: refinement of human carbonic anhydrase I. Ann. N.Y. Acad. Sci. 429 (1984) 49–60. [DOI] [PMID: 6430186]
3.  Murakami, H. and Sly, W.S. Purification and characterization of human salivary carbonic anhydrase. J. Biol. Chem. 262 (1987) 1382–1388. [DOI] [PMID: 2433278]
4.  Iverson, T.M., Alber, B.E., Kisker, C., Ferry, J.G. and Rees, D.C. A closer look at the active site of γ-class carbonic anhydrases: high-resolution crystallographic studies of the carbonic anhydrase from Methanosarcina thermophila. Biochemistry 39 (2000) 9222–9231. [DOI] [PMID: 10924115]
5.  Smith, K.S. and Ferry, J.G. Prokaryotic carbonic anhydrases. FEMS Microbiol. Rev. 24 (2000) 335–366. [DOI] [PMID: 10978542]
6.  Cronk, J.D., Endrizzi, J.A., Cronk, M.R., O'neill, J.W. and Zhang, K.Y. Crystal structure of E. coli β-carbonic anhydrase, an enzyme with an unusual pH-dependent activity. Protein Sci. 10 (2001) 911–922. [DOI] [PMID: 11316870]
7.  Merlin, C., Masters, M., McAteer, S. and Coulson, A. Why is carbonic anhydrase essential to Escherichia coli. J. Bacteriol. 185 (2003) 6415–6424. [DOI] [PMID: 14563877]
8.  Hirakawa, Y., Senda, M., Fukuda, K., Yu, H.Y., Ishida, M., Taira, M., Kinbara, K. and Senda, T. Characterization of a novel type of carbonic anhydrase that acts without metal cofactors. BMC Biol 19:105 (2021). [DOI] [PMID: 34006275]
[EC 4.2.1.1 created 1961, modified 2016]
 
 


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