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Literature summary for 4.2.1.1 extracted from

  • Koester, M.K.; Noltmann, E.A.
    Unique conformational properties of muscle carbonic anhydrase III as demonstrated by circular dichroism spectrometry (1979), Biochemistry, 18, 343-348.
    View publication on PubMed

Organism

Organism UniProt Comment Textmining
Oryctolagus cuniculus
-
-
-

Source Tissue

Source Tissue Comment Organism Textmining
erythrocyte anhydrase I and II Oryctolagus cuniculus
-
muscle carbonic anhydrase III Oryctolagus cuniculus
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
CO2 + H2O
-
Oryctolagus cuniculus H2CO3
-
?

pH Stability

pH Stability pH Stability Maximum Comment Organism
5 11 carbonic anhydrase II holoenzyme is stable Oryctolagus cuniculus