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Literature summary extracted from

  • Ceyhun, S.B.; Sentuerk, M.; Yerlikaya, E.; Erdogan, O.; Kuefrevioglu, O.I.; Ekinci, D.
    Purification and characterization of carbonic anhydrase from the teleost fish Dicentrarchus labrax (European seabass) liver and toxicological effects of metals on enzyme activity (2011), Environ. Toxicol. Pharmacol., 32, 69-74.
    View publication on PubMed

Inhibitors

EC Number Inhibitors Comment Organism Structure
4.2.1.1 Ag+ competitive, strong inhibition of carbonic anhydrase esterase activity Dicentrarchus labrax
4.2.1.1 Al3+ competitive, very strong inhibition of carbonic anhydrase esterase activity Dicentrarchus labrax
4.2.1.1 Co3+ competitive, strong inhibition of carbonic anhydrase esterase activity Dicentrarchus labrax
4.2.1.1 Cu2+ competitive, very strong inhibition of carbonic anhydrase esterase activity Dicentrarchus labrax
4.2.1.1 Hg2+ competitive, strong inhibition of carbonic anhydrase esterase activity Dicentrarchus labrax
4.2.1.1 additional information the inhibitory metals might be dangerous at low micromolar concentrations for fish carbonic anhydrase enzymes Dicentrarchus labrax
4.2.1.1 Pb2+ competitive, moderate inhibition of carbonic anhydrase esterase activity Dicentrarchus labrax
4.2.1.1 Zn2+ competitive, strong inhibition of carbonic anhydrase esterase activity Dicentrarchus labrax

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
4.2.1.1 additional information
-
 additional information kinetics of the esterase activity with 4-nitrophenylacetate as substrate Dicentrarchus labrax

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
4.2.1.1 additional information the enzyme shows an optimum ionic strength at 10mM Dicentrarchus labrax

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
4.2.1.1 30200
-
 x * 30200, SDS-PAGE Dicentrarchus labrax

Organism

EC Number Organism UniProt Comment Textmining
4.2.1.1 Dicentrarchus labrax
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
4.2.1.1 native enzyme 78.8fold from liver by single step tyrosine sulfanilamide affinity chromatography Dicentrarchus labrax

Source Tissue

EC Number Source Tissue Comment Organism Textmining
4.2.1.1 liver
-
 Dicentrarchus labrax
-

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
4.2.1.1 751.7
-
 purified enzyme, esterase activity with 4-nitrophenylacetate as substrate, pH 7.5, 25°C Dicentrarchus labrax

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4.2.1.1 additional information the enzyme also shows esterase activity with 4-nitrophenylacetate as substrate Dicentrarchus labrax ?
-
 ?

Subunits

EC Number Subunits Comment Organism
4.2.1.1 ? x * 30200, SDS-PAGE Dicentrarchus labrax

Synonyms

EC Number Synonyms Comment Organism
4.2.1.1 carbonic anhydrase
-
 Dicentrarchus labrax

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
4.2.1.1 25
-
 optimum temperature for the esterase activity with 4-nitrophenylacetate as substrate Dicentrarchus labrax

Temperature Range [°C]

EC Number Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
4.2.1.1 5 70 assay range Dicentrarchus labrax

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
4.2.1.1 7.5
-
 optimum pH for the esterase activity with 4-nitrophenylacetate as substrate Dicentrarchus labrax

pH Stability

EC Number pH Stability pH Stability Maximum Comment Organism
4.2.1.1 8.5
-
 purified native enzyme, optimally stable, 93% of maximum activity remaining after 14 days in 10 mM Tris-HCl buffer, pH 8.5 Dicentrarchus labrax

Ki Value [mM]

EC Number Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
4.2.1.1 additional information
-
 additional information Ki values of esterase activity with 4-nitrophenylacetate as substrate Dicentrarchus labrax

IC50 Value

EC Number IC50 Value IC50 Value Maximum Comment Organism Inhibitor Structure
4.2.1.1 additional information
-
 IC50 values of esterase activity with 4-nitrophenylacetate as substrate, competitive inhibition type Dicentrarchus labrax additional information