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Literature summary extracted from

  • Amata, O.; Marino, T.; Russo, N.; Toscano, M.
    Catalytic activity of a zeta-class zinc and cadmium containing carbonic anhydrase. Compared work mechanisms (2011), Phys. Chem. Chem. Phys., 13, 3468-3477.
    View publication on PubMed

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
4.2.1.1 Cd2+ replacement of zinc ion with cadmium does not entail significant differences in the catalytic performance of the enzyme Methanosarcina thermophila
4.2.1.1 Cd2+ replacement of zinc ion with cadmium does not entail significant differences in the catalytic performance of the enzyme Conticribra weissflogii
4.2.1.1 Zn2+ required for activity. Replacement of zinc ion with cadmium does not entail significant differences in the catalytic performance of the enzyme Methanosarcina thermophila
4.2.1.1 Zn2+ required for activity. Replacement of zinc ion with cadmium does not entail significant differences in the catalytic performance of the enzyme Conticribra weissflogii

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
4.2.1.1 H2CO3 Methanosarcina thermophila
-
CO2 + H2O
-
r
4.2.1.1 H2CO3 Conticribra weissflogii
-
CO2 + H2O
-
r

Organism

EC Number Organism UniProt Comment Textmining
4.2.1.1 Conticribra weissflogii
-
-
-
4.2.1.1 Methanosarcina thermophila
-
-
-

Reaction

EC Number Reaction Comment Organism Reaction ID
4.2.1.1 H2CO3 = CO2 + H2O reaction mechanism, model of the active site designed on the basis of the X-ray crystal structure, proposed for both metal ions similar reaction pathways consisting in the nucleophilic attack by the metal bound hydroxide to the carbon dioxide with bicarbonate formation, in a next internal rotation of this last fragment, and then in the formation of a species ready for the product removal, overview Methanosarcina thermophila
4.2.1.1 H2CO3 = CO2 + H2O reaction mechanism, model of the active site designed on the basis of the X-ray crystal structure, proposed for both metal ions similar reaction pathways consisting in the nucleophilic attack by the metal bound hydroxide to the carbon dioxide with bicarbonate formation, in a next internal rotation of this last fragment, and then in the formation of a species ready for the product removal, overview Conticribra weissflogii

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4.2.1.1 H2CO3
-
Methanosarcina thermophila CO2 + H2O
-
r
4.2.1.1 H2CO3
-
Conticribra weissflogii CO2 + H2O
-
r

Synonyms

EC Number Synonyms Comment Organism
4.2.1.1 carbonic anhydrase
-
Methanosarcina thermophila
4.2.1.1 carbonic anhydrase
-
Conticribra weissflogii
4.2.1.1 carbonic anhydrase cambialistic enzyme
-
Methanosarcina thermophila
4.2.1.1 carbonic anhydrase cambialistic enzyme
-
Conticribra weissflogii
4.2.1.1 CDCA1
-
Methanosarcina thermophila
4.2.1.1 More the enzyme from Methanosorcina thermophila belongs to the gamma class carbonic anhydrases Methanosarcina thermophila
4.2.1.1 TWCA1
-
Conticribra weissflogii

General Information

EC Number General Information Comment Organism
4.2.1.1 evolution carbonic anhydrase represents one of the most ancient proteins Methanosarcina thermophila
4.2.1.1 evolution carbonic anhydrase represents one of the most ancient proteins Conticribra weissflogii