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

BRENDA support

Literature summary extracted from

  • Patrikainen, M.S.; Tolvanen, M.E.E.; Aspatwar, A.; Barker, H.R.; Ortutay, C.; Jaenis, J.; Laitaoja, M.; Hytoenen, V.P.; Azizi, L.; Manandhar, P.; Jager, E.; Vullo, D.; Kukkurainen, S.; Hilvo, M.; Supuran, C.T.; Parkkila, S.
    Identification and characterization of a novel zebrafish (Danio rerio) pentraxin-carbonic anhydrase (2017), PeerJ, 5, e4128 .
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
4.2.1.1 gene ca6, isolation and sequencing of Danio rerio CA VI cDNA, complete with the sequence coding for the PTX domain, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis, expression of the recombinant CA VI-PTX protein in Spodoptera frugiperda Sf9 cells using the baculovirus expression system, quantitative real-time PCR Danio rerio

Protein Variants

EC Number Protein Variants Comment Organism
4.2.1.1 additional information knockdown of gene ca6 via two different antisense gene ca6-morpholino oligonucleotides-injected larvae. Zebrafish cannot swim properly in the ca6 knockdown model, in underdeveloped or deflated swim bladder in ca6 morphant larvae is observed, swimming pattern analysis of ca6 morphant and wild-type zebrafish, phenotype, overview Danio rerio

Inhibitors

EC Number Inhibitors Comment Organism Structure
4.2.1.1 acetazolamide 5-acetamido-1,3,4-thiadiazole-2-sulfonamide Danio rerio

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
4.2.1.1 6.5
-
 H2CO3 carbonate dehydratase activity, recombinant enzyme, pH and temperature not specified in the publication Danio rerio

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
4.2.1.1 Zn2+ required, metalloenzyme Danio rerio

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
4.2.1.1 280000
-
 recombinant enzyme CA VI-PTX, gel filtration, light scattering, and dynamic light scattering Danio rerio

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
4.2.1.1 H2CO3 Danio rerio
-
 CO2 + H2O
-
 r

Organism

EC Number Organism UniProt Comment Textmining
4.2.1.1 Danio rerio E7F742
-
-

Posttranslational Modification

EC Number Posttranslational Modification Comment Organism
4.2.1.1 glycoprotein four potentially N-glycosylated Asn residues (in the motif Asn-X-Ser/Thr) are all on the surface of the monomer Danio rerio

Purification (Commentary)

EC Number Purification (Comment) Organism
4.2.1.1 recombinant enzyme CA VI-PTX from Spodoptera frugiperda Sf9 cells Danio rerio

Source Tissue

EC Number Source Tissue Comment Organism Textmining
4.2.1.1 brain highest expression level of isozyme pentraxin-carbonic anhydrase Danio rerio
-
4.2.1.1 egg very low expression level of isozyme pentraxin-carbonic anhydrase Danio rerio
-
4.2.1.1 fin high expression level of isozyme pentraxin-carbonic anhydrase Danio rerio
-
4.2.1.1 gill
-
 Danio rerio
-
4.2.1.1 heart very low expression level of isozyme pentraxin-carbonic anhydrase Danio rerio
-
4.2.1.1 intestine very low expression level of isozyme pentraxin-carbonic anhydrase Danio rerio
-
4.2.1.1 kidney
-
 Danio rerio
-
4.2.1.1 liver very low expression level of isozyme pentraxin-carbonic anhydrase Danio rerio
-
4.2.1.1 additional information immunohistochemic analysis of enzyme distribution in zebrafish tissues, quantitative expression analysis of ca6 mRNA in wild-type and the ca6 morphant zebrafish at different stages of development Danio rerio
-
4.2.1.1 pancreas very low expression level of isozyme pentraxin-carbonic anhydrase Danio rerio
-
4.2.1.1 skin very low expression level of isozyme pentraxin-carbonic anhydrase Danio rerio
-
4.2.1.1 spleen very low expression level of isozyme pentraxin-carbonic anhydrase Danio rerio
-
4.2.1.1 swim bladder very low expression level of isozyme pentraxin-carbonic anhydrase Danio rerio
-
4.2.1.1 tail
-
 Danio rerio
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4.2.1.1 H2CO3
-
 Danio rerio CO2 + H2O
-
 r

Subunits

EC Number Subunits Comment Organism
4.2.1.1 pentamer 5 * 58600, recombinant enzyme CA VI-PTX, SDS-PAGE, 5 * 58107, enzyme sequence without glycans and signal peptide excluded, sequence calculation Danio rerio

Synonyms

EC Number Synonyms Comment Organism
4.2.1.1 CA VI
-
 Danio rerio
4.2.1.1 CA6
-
 Danio rerio
4.2.1.1 pentraxin-CA VI
-
 Danio rerio
4.2.1.1 pentraxin-carbonic anhydrase
-
 Danio rerio

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
4.2.1.1 890000
-
 H2CO3 carbonate dehydratase activity, recombinant enzyme, pH and temperature not specified in the publication Danio rerio

Ki Value [mM]

EC Number Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
4.2.1.1 0.000005
-
 acetazolamide recombinant enzyme, pH and temperature not specified in the publication Danio rerio

General Information

EC Number General Information Comment Organism
4.2.1.1 malfunction swimming pattern analysis of ca6 morphant and wild-type zebrafish, mutant phenotype of ca6 knockout fish, overview Danio rerio
4.2.1.1 additional information homology modeling of isozyme CA VI including PTX domain (residues 317-530) using the structure of human isozyme CA IV as template, PDB ID 3FE4. Structure comparisons Danio rerio

kcat/KM [mM/s]

EC Number kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
4.2.1.1 130000
-
 H2CO3 carbonate dehydratase activity, recombinant enzyme, pH and temperature not specified in the publication Danio rerio