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BRENDA support

Literature summary for 4.2.1.1 extracted from

  • Andrade, F.H.; Hatala, D.A.; McMullen, C.A.
    Carbonic anhydrase isoform expression and functional role in rodent extraocular muscle (2004), Pflugers Arch., 448, 547-551.
    View publication on PubMed

Inhibitors

Inhibitors Comment Organism Structure
6-ethoxyzolamide
-
Rattus norvegicus

Localization

Localization Comment Organism GeneOntology No. Textmining
sarcolemma in extensor digitorum longus. Extraocular muscle has very low sarcolemmal or cytosolic carbonic anhydrase activity Rattus norvegicus 42383
-

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Rattus norvegicus carbonic anhydrase does not influence the fast contractile kinetics characteristic of the extraocular muscles ?
-
?

Organism

Organism UniProt Comment Textmining
Rattus norvegicus
-
Sprague Dawley
-

Source Tissue

Source Tissue Comment Organism Textmining
extensor digitorum longus fast limb muscle, high activity of isoenzyme CA3, message levels of isoenzyme CA2 and CA4 are higher in extraocular muscle than in extensor digitorum longus, expression of isoenzyme CA5 is equivalent in extraocular muscle and extensor digitorum longus Rattus norvegicus
-
extraocular muscle isoenzyme CA3 is depressed, message levels of isoenzyme CA2 and CA4 are higher in extraocular muscle than in extensor digitorum longus, expression of isoenzyme CA5 is equivalent in extraocular muscle and extensor digitorum longus Rattus norvegicus
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information carbonic anhydrase does not influence the fast contractile kinetics characteristic of the extraocular muscles Rattus norvegicus ?
-
?