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Literature summary for 4.2.1.1 extracted from

  • Pinter, T.B.; Stillman, M.J.
    Kinetics of zinc and cadmium exchanges between metallothionein and carbonic anhydrase (2015), Biochemistry, 54, 6284-6293 .
    View publication on PubMed
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Metals/Ions

Metals/Ions Comment Organism Structure
Zn2+ required, carbonic anhydrase is a metalloenzyme, that binds a single zinc atom in its active site using three histidine ligands. The enzyme binds zinc relatively strongly with an apparent stability constant (log(KF)) of approximately 11.4 at pH 7.0. Following de novo protein synthesis, apocarbonic anhydrase must acquire and insert the enzymatically necessary zinc atom into the active site. The enzyme accepts donation of a single zinc atom from zinc-saturated metallothioneins at rates and concentrations that supports in vivo zinc donation by metallothionein (MT), fully saturated Zn-MT is capable of donating zinc to the apoenzyme. Competitive zinc titration to a solution containing equal concentrations of apo-rhMT1A and apoCA, formation of the fully metalated Zn7MT and holo-ZnCA, kinetics, simulation and modelling, overview Bos taurus

Natural Substrates/ Products (Substrates)

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

Organism

Organism UniProt Comment Textmining
Bos taurus P00921
-
-

Purification (Commentary)

Purification (Comment) Organism
the enzyme from a commercial preparation is further purified by gel filtration and ultrafiltration Bos taurus

Source Tissue

Source Tissue Comment Organism Textmining
commercial preparation
-
 Bos taurus
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
H2CO3
-
 Bos taurus CO2 + H2O
-
 r

Synonyms

Synonyms Comment Organism
carbonic anhydrase 2
-
 Bos taurus
carbonic anhydrase II
-
 Bos taurus