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Literature summary for 4.2.1.1 extracted from

  • Diaz-Torres, N.A.; Mahon, B.P.; Boone, C.D.; Pinard, M.A.; Tu, C.; Ng, R.; Agbandje-McKenna, M.; Silverman, D.; Scott, K.; McKenna, R.
    Structural and biophysical characterization of the alpha-carbonic anhydrase from the gammaproteobacterium Thiomicrospira crunogena XCL-2 insights into engineering thermostable enzymes for CO2 sequestration (2015), Acta Crystallogr. Sect. D, 71, 1745-1756 .
    View publication on PubMedView publication on EuropePMC
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Cloned(Commentary)

Cloned (Comment) Organism
gene Tcr_1545, sequence comparisons, recombinant enzyme expression in Escherichia coli strain BL21(DE3) Hydrogenovibrio crunogenus

Crystallization (Commentary)

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

Inhibitors Comment Organism Structure
p-(aminomethyl)-benzenesulfonamide p-AMBS Hydrogenovibrio crunogenus

KM Value [mM]

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

Metals/Ions Comment Organism Structure
Zn2+ required, metalloenzyme Hydrogenovibrio crunogenus

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
66000
-
 about, recombinant enzyme, ge filtration Hydrogenovibrio crunogenus

Natural Substrates/ Products (Substrates)

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

Organism UniProt Comment Textmining
Hydrogenovibrio crunogenus Q31FD6
-
-
Hydrogenovibrio crunogenus XCL-2 Q31FD6
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant enzyme from Escherichia coli strain BL21(DE3) by p-(aminomethyl)-benzenesulfonamide affinity chromatography Hydrogenovibrio crunogenus

Reaction

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
a

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
H2CO3
-
 Hydrogenovibrio crunogenus CO2 + H2O
-
 r
H2CO3
-
 Hydrogenovibrio crunogenus XCL-2 CO2 + H2O
-
 r

Subunits

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

Synonyms Comment Organism
alpha-CA
-
 Hydrogenovibrio crunogenus
alpha-carbonic anhydrase
-
 Hydrogenovibrio crunogenus
Tcru
-
 Hydrogenovibrio crunogenus
Tcr_1545
-
 Hydrogenovibrio crunogenus

Temperature Stability [°C]

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

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