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Literature summary for 4.2.1.1 extracted from

  • Karakostis, K.; Costa, C.; Zito, F.; Bruemmer, F.; Matranga, V.
    Characterization of an alpha type carbonic anhydrase from Paracentrotus lividus sea urchin embryos (2016), Mar. Biotechnol., 18, 384-395 .
    View publication on PubMed
Search for more literature for 4.2.1.1

Cloned(Commentary)

Cloned (Comment) Organism
gene Ca, DNA and amino acid sequence determination and analysis, phylogenetic analysis and tree, comparative real-time quantitative PCR, recombinant expression of His6-tagged enzyme in Escherichia coli strain BL21(DE3) Paracentrotus lividus

Metals/Ions

Metals/Ions Comment Organism Structure
Zn2+ required, metalloenzyme, three histidine residues predicted to form the Zn2+ coordination center, H233, H235, and H258, are conserved in Pl-CAN Paracentrotus lividus

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
H2CO3 Paracentrotus lividus
-
 CO2 + H2O
-
 r

Organism

Organism UniProt Comment Textmining
Paracentrotus lividus A0A193PYR8 collected from the Northwestern coast of Sicily (Mediterranean Sea)
-

Posttranslational Modification

Posttranslational Modification Comment Organism
proteolytic modification a signal peptide of 21 amino acids is identified at the N-terminal of the protein (MNAYILLSLTTLTVLYQECLG), followed by a cleavage site between the G21 and A22 residues, suggesting that Pl-CAN is a secreted protein Paracentrotus lividus

Purification (Commentary)

Purification (Comment) Organism
recombinant His6-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography, ultrafiltration, and dialysis Paracentrotus lividus

Source Tissue

Source Tissue Comment Organism Textmining
embryo Pl-can temporal and spatial expression profiles, analyzed throughout embryo development by comparative quantitative PCR and whole-mount in situ hybridization (WMISH), shows that Pl-can mRNA is specifically expressed in the primary mesenchyme cells of the embryo and levels increase along with the growth of the embryonic skeleton, reaching a peak at the pluteus stage Paracentrotus lividus
-
gastrula
-
 Paracentrotus lividus
-
pluteus
-
 Paracentrotus lividus
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
H2CO3
-
 Paracentrotus lividus CO2 + H2O
-
 r
additional information activity measurement by colorimetric reaction with P-nitrophenyl acetate as substrate Paracentrotus lividus ?
-
 ?

Subunits

Subunits Comment Organism
? x * 48500, recombinant premature enzyme, SDS-PAGE, x * 46200, recombinant mature enzyme, SDS-PAGE Paracentrotus lividus
More in addition to the alpha-type CA-specific domain, the enzyme has a glycine-rich region at the N-terminal of the molecule functional domains Paracentrotus lividus

Synonyms

Synonyms Comment Organism
Pl-can
-
 Paracentrotus lividus

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8.2
-
 assay at Paracentrotus lividus

pI Value

Organism Comment pI Value Maximum pI Value
Paracentrotus lividus sequence calculation
-
 6.83

General Information

General Information Comment Organism
evolution phylogenetic analysis indicates that Pl-CAN is evolutionarily closer to humans among chordates than to other species Paracentrotus lividus
additional information three histidine residues predicted to form the Zn2+ coordination center, H233, H235, and H258, are conserved in Pl-CAN, together with four additional sites, H206, Q231, E245, and T340 Paracentrotus lividus