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Literature summary for 4.2.1.1 extracted from

  • Weise, A.; Schneider, H.P.; McKenna, R.; Deitmer, J.W.
    Substrate-dependent interference of carbonic anhydrases with the glutamine transporter SNAT3-induced conductance (2011), Cell. Physiol. Biochem., 27, 79-90.
    View publication on PubMed

Protein Variants

Protein Variants Comment Organism
H64A shuttling mutant CAII-H64A shows lower catalytic activity compared to wild-type. Mutant displays catalytic activity in intact oocytes, also reduces the SNAT3-associated membrane conductance, when glutamine, but not when asparagine is the substrate Escherichia coli

Inhibitors

Inhibitors Comment Organism Structure
ethoxyzolamide
-
Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Synonyms

Synonyms Comment Organism
CAI
-
Escherichia coli
CAII
-
Escherichia coli
CAIII
-
Escherichia coli
CAIV
-
Escherichia coli
carbonic anhydrase
-
Escherichia coli

General Information

General Information Comment Organism
physiological function carbonic anhydrase which displays significant catalytic activity in intact oocytes, also reduces the SNAT3-associated membrane conductance, when glutamine, but not when asparagine is the substrate Escherichia coli