Cloned (Comment) | Organism |
---|---|
gene Tcr_1545, sequence comparisons, recombinant enzyme expression in Escherichia coli strain BL21(DE3) | Hydrogenovibrio crunogenus |
Crystallization (Comment) | Organism |
---|---|
purified recombinant enzyme, sitting drop vapour diffusion, using a precipitant solution consisting of 2% v/v Tacsimate, pH 4.0, 0.1 M sodium acetate trihydrate, pH 4.6, and 16% w/v PEG 3350, 10 days at 17°C, X-ray diffraction structure determination and analysis at 2.6 A resolution | Hydrogenovibrio crunogenus |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
p-(aminomethyl)-benzenesulfonamide | p-AMBS | Hydrogenovibrio crunogenus |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
additional information | - |
additional information | during the second catalytic stage, the zinc-bound 18O-labeled hydroxide is protonated, forming H2 18O, which is then released into solution, 18O-exchange kinetic analysis, overview | Hydrogenovibrio crunogenus |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Zn2+ | required, metalloenzyme | Hydrogenovibrio crunogenus |
Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|
66000 | - |
about, recombinant enzyme, ge filtration | Hydrogenovibrio crunogenus |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
H2CO3 | Hydrogenovibrio crunogenus | - |
CO2 + H2O | - |
r | |
H2CO3 | Hydrogenovibrio crunogenus XCL-2 | - |
CO2 + H2O | - |
r |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Hydrogenovibrio crunogenus | Q31FD6 | - |
- |
Hydrogenovibrio crunogenus XCL-2 | Q31FD6 | - |
- |
Purification (Comment) | Organism |
---|---|
recombinant enzyme from Escherichia coli strain BL21(DE3) by p-(aminomethyl)-benzenesulfonamide affinity chromatography | Hydrogenovibrio crunogenus |
Reaction | Comment | Organism | Reaction ID |
---|---|---|---|
H2CO3 = CO2 + H2O | interconversion of CO2 and water to bicarbonate and a proton. The general catalysis of CA is a metal-hydroxide ping-pong mechanism composed of two independent steps. The first step of catalysis is initiated by nucleophilic attack on the carbon of CO2 by the metal-bound hydroxide to yield bicarbonate, which is subsequently displaced by a water molecule. The second step is the removal of a proton from the now metal-bound water via an ordered water network and a residue acting as a weak base, which is typically a His at the opening of the active site | Hydrogenovibrio crunogenus |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
H2CO3 | - |
Hydrogenovibrio crunogenus | CO2 + H2O | - |
r | |
H2CO3 | - |
Hydrogenovibrio crunogenus XCL-2 | CO2 + H2O | - |
r |
Subunits | Comment | Organism |
---|---|---|
dimer | 2 * 33000, recombinant enzyme, SDS-PAGE | Hydrogenovibrio crunogenus |
More | the dimeric enzyme TcruCA has a highly conserved yet compact structure compared with other alpha-CAs, interface structure, structure comparisons, detailed overview. The TcruCA monomer has the signature secondary structure typical of an alpha-CA fold, with helical and loop structures present towards the surface and a conical active-site cavity comprised of mostly beta-structure | Hydrogenovibrio crunogenus |
Synonyms | Comment | Organism |
---|---|---|
alpha-CA | - |
Hydrogenovibrio crunogenus |
alpha-carbonic anhydrase | - |
Hydrogenovibrio crunogenus |
Tcru | - |
Hydrogenovibrio crunogenus |
Tcr_1545 | - |
Hydrogenovibrio crunogenus |
Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
---|---|---|---|
71.9 | - |
the enzyme has a melting temperature of 71.9°C at pH 8.0. TcruCA presents two transition peaks: one between 58°C and 62°C and the other between 68°C and 72°C, dependent on the pH | Hydrogenovibrio crunogenus |
General Information | Comment | Organism |
---|---|---|
additional information | the TcruCA monomer has the signature secondary structure typical of an alpha-CA fold, with helical and loop structures present towards the surface and a conical active-site cavity comprised of mostly beta-structure, structure comparisons, especially with human carbonic anhydrase 2, CA2, overview | Hydrogenovibrio crunogenus |