Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 4.2.1.1 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

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

KM Value [mM]

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

Metals/Ions

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

Molecular Weight [Da]

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

Organism

Organism UniProt Comment Textmining
Dicentrarchus labrax
-
-
-

Purification (Commentary)

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

Source Tissue

Source Tissue Comment Organism Textmining
liver
-
Dicentrarchus labrax
-

Specific Activity [micromol/min/mg]

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

Substrates and Products (Substrate)

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

Subunits

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

Synonyms

Synonyms Comment Organism
carbonic anhydrase
-
Dicentrarchus labrax

Temperature Optimum [°C]

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

Temperature Range [°C]

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

pH Optimum

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

pH Stability

pH Stability pH Stability Maximum Comment Organism
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]

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

IC50 Value

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