Encyclopedia of Metalloproteins

2013 Edition
| Editors: Robert H. Kretsinger, Vladimir N. Uversky, Eugene A. Permyakov

Cadmium Carbonic Anhydrase

  • Claudiu T. Supuran
Reference work entry
DOI: https://doi.org/10.1007/978-1-4614-1533-6_34

Synonyms

Definition

Cadmium: Cadmium is a metallic element with the oxidation state of +2, occurring rarely in metalloproteins, except some carbonic anhydrases. It is currently considered highly toxic, but in Cd-CAs, this metal ion has a catalytic role.

Carbonic anhydrase: Superfamily of metalloenzymes catalyzing CO2 hydration to bicarbonate and protons. Ubiquitous in all life kingdoms.

Biological implications: Cd-CAs are involved in CO2 fixations and photosynthesis in many diatoms.

Carbonic Anhydrase Families

The carbonic anhydrases (CAs, EC 4.2.1.1.) are a superfamily of metalloenzyme which evolved independently several times, with five genetically distinct enzyme classes known to date: the α-, β-, γ-, δ-, and ζ-CAs (Supuran 2008). The α-, β-, and δ-CAs use Zn(II) ions at the active site (Supuran 2008, 2010); the γ-CAs are probably Fe(II) enzymes (but they are active also with bound Zn(II) or Co(II) ions) (Ferry 2010), whereas the...

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References

  1. Ferry JG (2010) The gamma class of carbonic anhydrases. Biochim Biophys Acta 1804:374–381CrossRefPubMedGoogle Scholar
  2. Supuran CT (2008) Carbonic anhydrases: novel therapeutic applications for inhibitors and activators. Nat Rev Drug Discov 7:168–181CrossRefPubMedGoogle Scholar
  3. Supuran CT (2010) Carbonic anhydrase inhibitors. Bioorg Med Chem Lett 20:3467–3474CrossRefPubMedGoogle Scholar
  4. Viparelli F, Monti SM, De Simone G, Innocenti A, Scozzafava A, Xu Y, Morel FM, Supuran CT (2010) Inhibition of the R1 fragment of the cadmium- containg ζ class carbonic anhydrase from the diatom Thalassiosira weissflogii with anions. Bioorg Med Chem Lett 20:4745–4748CrossRefPubMedGoogle Scholar
  5. Xu Y, Feng L, Jeffrey PD, Shi Y, Morel FM (2008) Structure and metal exchange in the cadmium carbonic anhydrase of marine diatoms. Nature 452:56–61CrossRefPubMedGoogle Scholar

Copyright information

© Springer Science+Business Media New York 2013

Authors and Affiliations

  1. 1.Department of ChemistryUniversity of FlorenceSesto Fiorentino (Florence)Italy