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Literature summary extracted from

  • Mananes, A.A.L.; Daleo, G.R.; Vega, F.V.
    pH-dependent association of carbonic anhydrase (CA) with gastric light microsomal membranes isolated from bovine abomasum. Partial characterization of membrane-associated activity (1993), Comp. Biochem. Physiol. B, 105, 175-182.
    View publication on PubMed

Inhibitors

EC Number Inhibitors Comment Organism Structure
4.2.1.1 acetate
-
Bos taurus
4.2.1.1 acetazolamide 100 mM, the firmly-membrane-associated activity is less sensitive to inhibition than the loosely-membrane associated enzyme Bos taurus
4.2.1.1 Br-
-
Bos taurus
4.2.1.1 Cl- 100 mM, the firmly-membrane-associated activity is less sensitive to inhibition than the loosely-membrane associated enzyme Bos taurus
4.2.1.1 I- 100 mM, the firmly-membrane-associated activity is less sensitive to inhibition than the loosely-membrane associated enzyme Bos taurus
4.2.1.1 NO3-
-
Bos taurus

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
4.2.1.1 microsome association of the enzyme with light microsomal membranes is dependent on pH, being lower at neutral or alkaline pH. 2 Enzyme forms: a loosely-membrane-associated enzyme and a firmly-membrane-associated enzyme Bos taurus
-
-

Organism

EC Number Organism UniProt Comment Textmining
4.2.1.1 Bos taurus
-
-
-

Source Tissue

EC Number Source Tissue Comment Organism Textmining
4.2.1.1 gastric mucosa
-
Bos taurus
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4.2.1.1 CO2 + H2O
-
Bos taurus H2CO3
-
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