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Literature summary for 4.2.1.1 extracted from

  • Hoffmann, K.M.; Samardzic, D.; Heever, K.; Rowlett, R.S.
    Co(II)-substituted Haemophilus influenzae beta-carbonic anhydrase: spectral evidence for allosteric regulation by pH and bicarbonate ion (2011), Arch. Biochem. Biophys., 511, 80-87.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
overexpression of HICA in Escherichia coli in minimal media supplemented with CoCl2 Haemophilus influenzae

Crystallization (Commentary)

Crystallization (Comment) Organism
purified recombinant Co-HICA by hanging drop vapor diffusion, 10 mg/ml protein crystallized in 0.2 M sodium acetate, 0.1 M Tris-HCl, pH 8.5, 0.1 M (NH4)2SO4, and 27% PEG 4000, 22°C, several days, X-ray diffraction structure determination and analysis at 2.5 A resolution Haemophilus influenzae

Inhibitors

Inhibitors Comment Organism Structure
bicarbonate is hypothesized to be an allosteric inhibitor of HICA Haemophilus influenzae

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
additional information steady-state kinetic analysis of the Co2+-substituted enzyme, overview Haemophilus influenzae

Metals/Ions

Metals/Ions Comment Organism Structure
Co2+ preparation of a Co(II)-substituted HICA, Co-HICA. Co(II)-substituted HICA, Co-HICA, has comparable, 20% enhanced kcat and 2.3fold increased Km/kcat compared to that of the wild-type enzyme Haemophilus influenzae
Zn2+ required, can be substituted by Co2+ Haemophilus influenzae

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
100000
-
about, recombinant Co-HICA, gel filtration Haemophilus influenzae

Natural Substrates/ Products (Substrates)

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

Organism

Organism UniProt Comment Textmining
Haemophilus influenzae
-
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant Co-HICA from Escherichia coli by gel filtration Haemophilus influenzae

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
H2CO3
-
Haemophilus influenzae CO2 + H2O
-
r

Subunits

Subunits Comment Organism
More overall secondary and tertiary structure of Co-HICA differ from wild-type Zn-enzyme structure, active R-state and inactive T-state conformations, overview Haemophilus influenzae
tetramer recombinant Co-HICA, the crystal structure shows a four-coordinate geometry for Co-HICA with pH-dependent changes in the absorption spectrum of Co-HICA, overview Haemophilus influenzae

Synonyms

Synonyms Comment Organism
beta-carbonic anhydrase
-
Haemophilus influenzae
carbonate hydrolyase
-
Haemophilus influenzae
HICA
-
Haemophilus influenzae

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
25
-
assay at Haemophilus influenzae

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8
-
and above Haemophilus influenzae

pH Range

pH Minimum pH Maximum Comment Organism
6.5 10.5 pH profile, pH-dependent changes in the absorption spectrum of Co-HICA including an increase in molar absorptivity and a red shift of a 580 nm peak with decreasing pH, correlate with the pH-dependence of kcat/Km, overview Haemophilus influenzae