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Carbonic anyhdrase is useful in carboxy group transfers and reduction reactions.Carbonic anhydrase from bovine erythrocytes (BCA) has been used to study the effect of removal of enzyme-bound metal ion, Zn2+, on aggregation behavior of the enzyme. Removal of metal ion by a chelator such as EDTA enhances the propensity of the enzyme to adopt the molten-globule state. This state of the enzyme is found to bind to the chaperone-like α-crystallin and prevent aggregation. The enzyme from Aladdin has been immobilized to electrochemical transducers in order to obtain develop an analytical device for dissolved CO2 measurement. It has also been used for the thermodynamic analysis of conformational changes in BCA.

Specificity:

Blood CO2 transport and excretion is largely dependent on the rapid catalysis of the CO2 reactions within the erythrocyte by CA (Tufts et al. 2003). Bovine CA reversibly hydrates alkyl pyruvates and it exhibits hydratase activity toward a wide variety of substrates (Pocker et al. 1974, and Wells et al. 1975).

Protein Accession Number: P00921

CATH Classification (v. 3.2.0):

Class: Alpha Beta

Architecture: Roll

Topology: Carbonic Anhydrase II

Molecular Weight:

29.0 kDa (Theoretical)

30 kDa (Lindskog et al. 1971)

Optimal pH: 7.0-7.5 (Demir et al. 2000, and Tasgin et al. 2009)

Isoelectric Point: 6.40 (Theoretical)

Extinction Coefficient：

50,070 cm-1M-1 (Theoretical)

E1%, 280 = 19.0 (Nyman and Lindskog 1964)

Active Site Residues：

Histidine (H63)

Asparagine (N66)

Lysine (K126)

Activators:

HPO42- (Rowlett et al. 1991)

SO32- (Rowlett et al. 1991)

Inhibitors:

Monovalent anions (Lindskog et al. 1971, and Ward and Cull 1972)

Sulfonates and sulfonamides (Pocker and Watamori 1973, and Binford et al. 1974)

Imidazole (Edsall 1968)

Applications:

CO2 determination in blood

Elimination of CO2 in reagents for acidity testing

Carboxy group transfers

Reduction reactions