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Literature summary extracted from

  • Di Fiore, A.; Alterio, V.; Monti, S.M.; De Simone, G.; D'Ambrosio, K.
    Thermostable carbonic anhydrases in biotechnological applications (2015), Int. J. Mol. Sci., 16, 15456-15480 .
    View publication on PubMedView publication on EuropePMC

Application

EC Number Application Comment Organism
4.2.1.1 environmental protection the enzyme is useful to capture CO2 from flue gas in bio-mimetic CO2 capture systems to reduce the concentration of CO2 in the atmosphere, method technology, overview Methanosarcina thermophila
4.2.1.1 environmental protection the enzyme is useful to capture CO2 from flue gas in bio-mimetic CO2 capture systems to reduce the concentration of CO2 in the atmosphere, method technology, overview Homo sapiens
4.2.1.1 environmental protection the enzyme is useful to capture CO2 from flue gas in bio-mimetic CO2 capture systems to reduce the concentration of CO2 in the atmosphere, method technology, overview Sulfurihydrogenibium azorense
4.2.1.1 environmental protection the enzyme is useful to capture CO2 from flue gas in bio-mimetic CO2 capture systems to reduce the concentration of CO2 in the atmosphere, method technology, overview Pyrococcus horikoshii
4.2.1.1 environmental protection the enzyme is useful to capture CO2 from flue gas in bio-mimetic CO2 capture systems to reduce the concentration of CO2 in the atmosphere, method technology, overview Sulfurihydrogenibium sp. YO3AOP1
4.2.1.1 environmental protection the enzyme is useful to capture CO2 from flue gas in bio-mimetic CO2 capture systems to reduce the concentration of CO2 in the atmosphere, method technology, overview Caminibacter mediatlanticus
4.2.1.1 environmental protection the enzyme is useful to capture CO2 from flue gas in bio-mimetic CO2 capture systems to reduce the concentration of CO2 in the atmosphere, method technology, overview Desulfovibrio vulgaris
4.2.1.1 environmental protection the enzyme is useful to capture CO2 from flue gas in bio-mimetic CO2 capture systems to reduce the concentration of CO2 in the atmosphere, method technology, overview Methanothermobacter thermautotrophicus
4.2.1.1 environmental protection the enzyme is useful to capture CO2 from flue gas in bio-mimetic CO2 capture systems to reduce the concentration of CO2 in the atmosphere, method technology, overview Serratia sp. ISTD04
4.2.1.1 environmental protection the enzyme is useful to capture CO2 from flue gas in bio-mimetic CO2 capture systems to reduce the concentration of CO2 in the atmosphere, method technology, overview Citrobacter freundii
4.2.1.1 environmental protection the enzyme is useful to capture CO2 from flue gas in bio-mimetic CO2 capture systems to reduce the concentration of CO2 in the atmosphere, method technology, overview Persephonella marina
4.2.1.1 environmental protection the enzyme is useful to capture CO2 from flue gas in bio-mimetic CO2 capture systems to reduce the concentration of CO2 in the atmosphere, method technology, overview Thermovibrio ammonificans
4.2.1.1 environmental protection the enzyme is useful to capture CO2 from flue gas in bio-mimetic CO2 capture systems to reduce the concentration of CO2 in the atmosphere, method technology, overview Bos taurus

Cloned(Commentary)

EC Number Cloned (Comment) Organism
4.2.1.1 recombinant enzyme expression in Escherichia coli or in Methanosarcina acetivorans Methanosarcina thermophila

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
4.2.1.1 crystal structure determination and analysis, PDB ID 4C3T Thermovibrio ammonificans
4.2.1.1 crystal structure determination and analysis, PDB ID 4X5S Sulfurihydrogenibium azorense
4.2.1.1 enzyme crystal structure determination and analysis, Cab dimer, PDB ID 1G5C Methanothermobacter thermautotrophicus
4.2.1.1 purified enzyme in complex with inhibitor acetazolamide, X-ray diffraction structure determination and analysis, PDB ID 4G7A Sulfurihydrogenibium sp. YO3AOP1
4.2.1.1 purified enzyme in complex with Zn2+ and Co2+, X-ray diffraction structure determination and analysis, PDB ID 1QRG Methanosarcina thermophila

Protein Variants

EC Number Protein Variants Comment Organism
4.2.1.1 E234P site-directed mutagenesis, residue Glu234, which is positioned in a surface loop, is substituted with a proline residue. Thermal stability analysis of this variant indicates an enhanced melting temperature of about 3°C compared to the wild-type enzyme Homo sapiens
4.2.1.1 additional information capture of CO2 from flue gas in bio-mimetic CO2 capture systems to reduce the concentration of CO2 in the atmosphere, method technology, overview Sulfurihydrogenibium sp. YO3AOP1
4.2.1.1 additional information capture of CO2 from flue gas in bio-mimetic CO2 capture systems to reduce the concentration of CO2 in the atmosphere, method technology, overview Caminibacter mediatlanticus
4.2.1.1 additional information capture of CO2 from flue gas in bio-mimetic CO2 capture systems to reduce the concentration of CO2 in the atmosphere, method technology, overview Desulfovibrio vulgaris
4.2.1.1 additional information capture of CO2 from flue gas in bio-mimetic CO2 capture systems to reduce the concentration of CO2 in the atmosphere, method technology, overview Methanothermobacter thermautotrophicus
4.2.1.1 additional information capture of CO2 from flue gas in bio-mimetic CO2 capture systems to reduce the concentration of CO2 in the atmosphere, method technology, overview Serratia sp. ISTD04
4.2.1.1 additional information capture of CO2 from flue gas in bio-mimetic CO2 capture systems to reduce the concentration of CO2 in the atmosphere, method technology, overview Citrobacter freundii
4.2.1.1 additional information capture of CO2 from flue gas in bio-mimetic CO2 capture systems to reduce the concentration of CO2 in the atmosphere, method technology, overview Persephonella marina
4.2.1.1 additional information capture of CO2 from flue gas in bio-mimetic CO2 capture systems to reduce the concentration of CO2 in the atmosphere, method technology, overview Thermovibrio ammonificans
4.2.1.1 additional information capture of CO2 from flue gas in bio-mimetic CO2 capture systems to reduce the concentration of CO2 in the atmosphere, method technology, overview. Immobilizing the enzyme within solid supports improves the method. Formation of gamma-CA nanoassemblies, where individual enzymes are connected to each other and make multiple linked interactions with the reactor surface. This can be achieved by mutating specific enzyme residues to cysteines, in order to introduce sites for biotinylation, thus allowing the subsequent formation of stable nanostructures by cross-linking of biotinylated-gamma-CAs with streptavidin tetramers. Further addition of an immobilization sequence at amino- or carboxy-terminus also allows for a controlled and reversible immobilization of the gamma-CA to a functionalized surface Methanosarcina thermophila
4.2.1.1 additional information capture of CO2 from flue gas in bio-mimetic CO2 capture systems to reduce the concentration of CO2 in the atmosphere, method technology, overview. Immobilizing the enzyme within solid supports improves the method. Formation of gamma-CA nanoassemblies, where individual enzymes are connected to each other and make multiple linked interactions with the reactor surface. This can be achieved by mutating specific enzyme residues to cysteines, in order to introduce sites for biotinylation, thus allowing the subsequent formation of stable nanostructures by cross-linking of biotinylated-gamma-CAs with streptavidin tetramers. Further addition of an immobilization sequence at amino- or carboxy-terminus also allows for a controlled and reversible immobilization of the gamma-CA to a functionalized surface Pyrococcus horikoshii
4.2.1.1 additional information substitution in hCA II of residues 23 and 203 with two cysteines (dsHCA II) to reproduce a disulfide bridge conserved in many members of alpha-CA class. Thermal stability investigations of this variant shows that the melting temperature is enhanced by 14°C compared to the wild-type enzyme, while the catalytic efficiency is similar to that of native enzyme Homo sapiens

Inhibitors

EC Number Inhibitors Comment Organism Structure
4.2.1.1 acetazolamide
-
 Sulfurihydrogenibium sp. YO3AOP1

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
4.2.1.1 additional information
-
 additional information kinetics Homo sapiens
4.2.1.1 additional information
-
 additional information kinetics Sulfurihydrogenibium sp. YO3AOP1
4.2.1.1 additional information
-
 additional information kinetics Persephonella marina
4.2.1.1 additional information
-
 additional information kinetics Thermovibrio ammonificans
4.2.1.1 additional information
-
 additional information kinetics, stopped-flow assay method Sulfurihydrogenibium azorense

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
4.2.1.1 Co2+ activates to a 2fold activity compared to the activity with Zn2+ Methanosarcina thermophila
4.2.1.1 Fe2+ when overproduced in Escherichia coli or in Methanosarcina acetivorans and subsequently anaerobically purified, the enzyme contains Fe2+ in the active site and is 4fold more active. In these conditions, catalytic activity is rapidly lost after exposure to air, as a consequence of the oxidation of Fe2+ to Fe3+ and loss of the metal from the active site, thus convincing evidence is that iron is the physiologically relevant metal for this enzyme Methanosarcina thermophila
4.2.1.1 additional information analysis of three-dimensional structures of MtCam, in both Zn- and Co-bound forms, overview. Structure comparisons Methanosarcina thermophila
4.2.1.1 Zn2+ metalloenzyme, the metal ion is required for catalytic activity, coordinated by three histidine residues: His89, His91 and His108, zinc cordination site structure, PDB ID 4G7A Sulfurihydrogenibium sp. YO3AOP1
4.2.1.1 Zn2+ metalloenzyme, the metal ion is required for catalytic activity, coordinated by three residues Methanosarcina thermophila
4.2.1.1 Zn2+ metalloenzyme, the metal ion is required for catalytic activity, coordinated by three residues Homo sapiens
4.2.1.1 Zn2+ metalloenzyme, the metal ion is required for catalytic activity, coordinated by three residues Sulfurihydrogenibium azorense
4.2.1.1 Zn2+ metalloenzyme, the metal ion is required for catalytic activity, coordinated by three residues Pyrococcus horikoshii
4.2.1.1 Zn2+ metalloenzyme, the metal ion is required for catalytic activity, coordinated by three residues Caminibacter mediatlanticus
4.2.1.1 Zn2+ metalloenzyme, the metal ion is required for catalytic activity, coordinated by three residues Desulfovibrio vulgaris
4.2.1.1 Zn2+ metalloenzyme, the metal ion is required for catalytic activity, coordinated by three residues Serratia sp. ISTD04
4.2.1.1 Zn2+ metalloenzyme, the metal ion is required for catalytic activity, coordinated by three residues Citrobacter freundii
4.2.1.1 Zn2+ metalloenzyme, the metal ion is required for catalytic activity, coordinated by three residues Persephonella marina
4.2.1.1 Zn2+ metalloenzyme, the metal ion is required for catalytic activity, coordinated by three residues Thermovibrio ammonificans
4.2.1.1 Zn2+ metalloenzyme, the metal ion is required for catalytic activity, coordinated by three residues Bos taurus
4.2.1.1 Zn2+ metalloenzyme, the metal ion is required for catalytic activity, coordinated by three residues. Each monomer of the enzyme dimer contains a zinc ion tetrahedrally coordinated by two cysteines (Cys32 and Cys90), one histidine (His87) and a water molecule/hydroxide ion Methanothermobacter thermautotrophicus

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
4.2.1.1 H2CO3 Methanosarcina thermophila
-
 CO2 + H2O
-
 r
4.2.1.1 H2CO3 Homo sapiens
-
 CO2 + H2O
-
 r
4.2.1.1 H2CO3 Sulfurihydrogenibium azorense
-
 CO2 + H2O
-
 r
4.2.1.1 H2CO3 Pyrococcus horikoshii
-
 CO2 + H2O
-
 r
4.2.1.1 H2CO3 Sulfurihydrogenibium sp. YO3AOP1
-
 CO2 + H2O
-
 r
4.2.1.1 H2CO3 Caminibacter mediatlanticus
-
 CO2 + H2O
-
 r
4.2.1.1 H2CO3 Desulfovibrio vulgaris
-
 CO2 + H2O
-
 r
4.2.1.1 H2CO3 Methanothermobacter thermautotrophicus
-
 CO2 + H2O
-
 r
4.2.1.1 H2CO3 Serratia sp. ISTD04
-
 CO2 + H2O
-
 r
4.2.1.1 H2CO3 Citrobacter freundii
-
 CO2 + H2O
-
 r
4.2.1.1 H2CO3 Persephonella marina
-
 CO2 + H2O
-
 r
4.2.1.1 H2CO3 Thermovibrio ammonificans
-
 CO2 + H2O
-
 r
4.2.1.1 H2CO3 Bos taurus
-
 CO2 + H2O
-
 r
4.2.1.1 H2CO3 Caminibacter mediatlanticus TB-2
-
 CO2 + H2O
-
 r
4.2.1.1 H2CO3 Desulfovibrio vulgaris Hildenborough / ATCC 29579 / DSM 644 / NCIMB 8303
-
 CO2 + H2O
-
 r
4.2.1.1 H2CO3 Persephonella marina DSM 14350 / EX-H1
-
 CO2 + H2O
-
 r
4.2.1.1 H2CO3 Methanothermobacter thermautotrophicus ATCC BAA-927 / DSM 2133 / JCM 14651 / NBRC 100331 / OCM 82 / Marburg
-
 CO2 + H2O
-
 r
4.2.1.1 H2CO3 Thermovibrio ammonificans DSM 15698 / JCM 12110 / HB-1
-
 CO2 + H2O
-
 r

Organism

EC Number Organism UniProt Comment Textmining
4.2.1.1 Bos taurus P00921
-
-
4.2.1.1 Caminibacter mediatlanticus A6DAW8
-
-
4.2.1.1 Caminibacter mediatlanticus TB-2 A6DAW8
-
-
4.2.1.1 Citrobacter freundii A0A0D7LLM5
-
-
4.2.1.1 Desulfovibrio vulgaris Q72B61
-
-
4.2.1.1 Desulfovibrio vulgaris Hildenborough / ATCC 29579 / DSM 644 / NCIMB 8303 Q72B61
-
-
4.2.1.1 Homo sapiens P00918
-
-
4.2.1.1 Methanosarcina thermophila
-
-
-
4.2.1.1 Methanothermobacter thermautotrophicus D9PU79
-
-
4.2.1.1 Methanothermobacter thermautotrophicus ATCC BAA-927 / DSM 2133 / JCM 14651 / NBRC 100331 / OCM 82 / Marburg D9PU79
-
-
4.2.1.1 Persephonella marina C0QRB5
-
-
4.2.1.1 Persephonella marina DSM 14350 / EX-H1 C0QRB5
-
-
4.2.1.1 Pyrococcus horikoshii O59257
-
-
4.2.1.1 Serratia sp. ISTD04 K4N028
-
-
4.2.1.1 Sulfurihydrogenibium azorense
-
-
-
4.2.1.1 Sulfurihydrogenibium sp. YO3AOP1 B2V8E3
-
-
4.2.1.1 Thermovibrio ammonificans E8T502
-
-
4.2.1.1 Thermovibrio ammonificans DSM 15698 / JCM 12110 / HB-1 E8T502
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
4.2.1.1 recombinant enzyme from Escherichia coli anaerobically or aerobically, recombinant enzyme from Methanosarcina acetivorans anaerobically Methanosarcina thermophila

Reaction

EC Number Reaction Comment Organism Reaction ID
4.2.1.1 H2CO3 = CO2 + H2O the catalytic mechanism for the CO2 hydration reaction consists of two steps. In the first step a zinc-bound hydroxide leads the nucleophilic attack on a CO2 molecule with formation of bicarbonate bound to the zinc ion, which is then substituted by a water molecule. The second step, the rate limiting one, consists of the regeneration of the enzyme reactive species, the zinc-bound hydroxide, via a proton transfer reaction, which occurs from the zinc-bound water molecule to the external buffer. This process is generally assisted by an enzyme residue which acts as proton shuttle Methanosarcina thermophila
a
4.2.1.1 H2CO3 = CO2 + H2O the catalytic mechanism for the CO2 hydration reaction consists of two steps. In the first step a zinc-bound hydroxide leads the nucleophilic attack on a CO2 molecule with formation of bicarbonate bound to the zinc ion, which is then substituted by a water molecule. The second step, the rate limiting one, consists of the regeneration of the enzyme reactive species, the zinc-bound hydroxide, via a proton transfer reaction, which occurs from the zinc-bound water molecule to the external buffer. This process is generally assisted by an enzyme residue which acts as proton shuttle Homo sapiens
a
4.2.1.1 H2CO3 = CO2 + H2O the catalytic mechanism for the CO2 hydration reaction consists of two steps. In the first step a zinc-bound hydroxide leads the nucleophilic attack on a CO2 molecule with formation of bicarbonate bound to the zinc ion, which is then substituted by a water molecule. The second step, the rate limiting one, consists of the regeneration of the enzyme reactive species, the zinc-bound hydroxide, via a proton transfer reaction, which occurs from the zinc-bound water molecule to the external buffer. This process is generally assisted by an enzyme residue which acts as proton shuttle Sulfurihydrogenibium azorense
a
4.2.1.1 H2CO3 = CO2 + H2O the catalytic mechanism for the CO2 hydration reaction consists of two steps. In the first step a zinc-bound hydroxide leads the nucleophilic attack on a CO2 molecule with formation of bicarbonate bound to the zinc ion, which is then substituted by a water molecule. The second step, the rate limiting one, consists of the regeneration of the enzyme reactive species, the zinc-bound hydroxide, via a proton transfer reaction, which occurs from the zinc-bound water molecule to the external buffer. This process is generally assisted by an enzyme residue which acts as proton shuttle Pyrococcus horikoshii
a
4.2.1.1 H2CO3 = CO2 + H2O the catalytic mechanism for the CO2 hydration reaction consists of two steps. In the first step a zinc-bound hydroxide leads the nucleophilic attack on a CO2 molecule with formation of bicarbonate bound to the zinc ion, which is then substituted by a water molecule. The second step, the rate limiting one, consists of the regeneration of the enzyme reactive species, the zinc-bound hydroxide, via a proton transfer reaction, which occurs from the zinc-bound water molecule to the external buffer. This process is generally assisted by an enzyme residue which acts as proton shuttle Sulfurihydrogenibium sp. YO3AOP1
a
4.2.1.1 H2CO3 = CO2 + H2O the catalytic mechanism for the CO2 hydration reaction consists of two steps. In the first step a zinc-bound hydroxide leads the nucleophilic attack on a CO2 molecule with formation of bicarbonate bound to the zinc ion, which is then substituted by a water molecule. The second step, the rate limiting one, consists of the regeneration of the enzyme reactive species, the zinc-bound hydroxide, via a proton transfer reaction, which occurs from the zinc-bound water molecule to the external buffer. This process is generally assisted by an enzyme residue which acts as proton shuttle Caminibacter mediatlanticus
a
4.2.1.1 H2CO3 = CO2 + H2O the catalytic mechanism for the CO2 hydration reaction consists of two steps. In the first step a zinc-bound hydroxide leads the nucleophilic attack on a CO2 molecule with formation of bicarbonate bound to the zinc ion, which is then substituted by a water molecule. The second step, the rate limiting one, consists of the regeneration of the enzyme reactive species, the zinc-bound hydroxide, via a proton transfer reaction, which occurs from the zinc-bound water molecule to the external buffer. This process is generally assisted by an enzyme residue which acts as proton shuttle Desulfovibrio vulgaris
a
4.2.1.1 H2CO3 = CO2 + H2O the catalytic mechanism for the CO2 hydration reaction consists of two steps. In the first step a zinc-bound hydroxide leads the nucleophilic attack on a CO2 molecule with formation of bicarbonate bound to the zinc ion, which is then substituted by a water molecule. The second step, the rate limiting one, consists of the regeneration of the enzyme reactive species, the zinc-bound hydroxide, via a proton transfer reaction, which occurs from the zinc-bound water molecule to the external buffer. This process is generally assisted by an enzyme residue which acts as proton shuttle Methanothermobacter thermautotrophicus
a
4.2.1.1 H2CO3 = CO2 + H2O the catalytic mechanism for the CO2 hydration reaction consists of two steps. In the first step a zinc-bound hydroxide leads the nucleophilic attack on a CO2 molecule with formation of bicarbonate bound to the zinc ion, which is then substituted by a water molecule. The second step, the rate limiting one, consists of the regeneration of the enzyme reactive species, the zinc-bound hydroxide, via a proton transfer reaction, which occurs from the zinc-bound water molecule to the external buffer. This process is generally assisted by an enzyme residue which acts as proton shuttle Serratia sp. ISTD04
a
4.2.1.1 H2CO3 = CO2 + H2O the catalytic mechanism for the CO2 hydration reaction consists of two steps. In the first step a zinc-bound hydroxide leads the nucleophilic attack on a CO2 molecule with formation of bicarbonate bound to the zinc ion, which is then substituted by a water molecule. The second step, the rate limiting one, consists of the regeneration of the enzyme reactive species, the zinc-bound hydroxide, via a proton transfer reaction, which occurs from the zinc-bound water molecule to the external buffer. This process is generally assisted by an enzyme residue which acts as proton shuttle Citrobacter freundii
a
4.2.1.1 H2CO3 = CO2 + H2O the catalytic mechanism for the CO2 hydration reaction consists of two steps. In the first step a zinc-bound hydroxide leads the nucleophilic attack on a CO2 molecule with formation of bicarbonate bound to the zinc ion, which is then substituted by a water molecule. The second step, the rate limiting one, consists of the regeneration of the enzyme reactive species, the zinc-bound hydroxide, via a proton transfer reaction, which occurs from the zinc-bound water molecule to the external buffer. This process is generally assisted by an enzyme residue which acts as proton shuttle Persephonella marina
a
4.2.1.1 H2CO3 = CO2 + H2O the catalytic mechanism for the CO2 hydration reaction consists of two steps. In the first step a zinc-bound hydroxide leads the nucleophilic attack on a CO2 molecule with formation of bicarbonate bound to the zinc ion, which is then substituted by a water molecule. The second step, the rate limiting one, consists of the regeneration of the enzyme reactive species, the zinc-bound hydroxide, via a proton transfer reaction, which occurs from the zinc-bound water molecule to the external buffer. This process is generally assisted by an enzyme residue which acts as proton shuttle Thermovibrio ammonificans
a
4.2.1.1 H2CO3 = CO2 + H2O the catalytic mechanism for the CO2 hydration reaction consists of two steps. In the first step a zinc-bound hydroxide leads the nucleophilic attack on a CO2 molecule with formation of bicarbonate bound to the zinc ion, which is then substituted by a water molecule. The second step, the rate limiting one, consists of the regeneration of the enzyme reactive species, the zinc-bound hydroxide, via a proton transfer reaction, which occurs from the zinc-bound water molecule to the external buffer. This process is generally assisted by an enzyme residue which acts as proton shuttle Bos taurus
a

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4.2.1.1 H2CO3
-
 Methanosarcina thermophila CO2 + H2O
-
 r
4.2.1.1 H2CO3
-
 Homo sapiens CO2 + H2O
-
 r
4.2.1.1 H2CO3
-
 Sulfurihydrogenibium azorense CO2 + H2O
-
 r
4.2.1.1 H2CO3
-
 Pyrococcus horikoshii CO2 + H2O
-
 r
4.2.1.1 H2CO3
-
 Sulfurihydrogenibium sp. YO3AOP1 CO2 + H2O
-
 r
4.2.1.1 H2CO3
-
 Caminibacter mediatlanticus CO2 + H2O
-
 r
4.2.1.1 H2CO3
-
 Desulfovibrio vulgaris CO2 + H2O
-
 r
4.2.1.1 H2CO3
-
 Methanothermobacter thermautotrophicus CO2 + H2O
-
 r
4.2.1.1 H2CO3
-
 Serratia sp. ISTD04 CO2 + H2O
-
 r
4.2.1.1 H2CO3
-
 Citrobacter freundii CO2 + H2O
-
 r
4.2.1.1 H2CO3
-
 Persephonella marina CO2 + H2O
-
 r
4.2.1.1 H2CO3
-
 Thermovibrio ammonificans CO2 + H2O
-
 r
4.2.1.1 H2CO3
-
 Bos taurus CO2 + H2O
-
 r
4.2.1.1 H2CO3
-
 Caminibacter mediatlanticus TB-2 CO2 + H2O
-
 r
4.2.1.1 H2CO3
-
 Desulfovibrio vulgaris Hildenborough / ATCC 29579 / DSM 644 / NCIMB 8303 CO2 + H2O
-
 r
4.2.1.1 H2CO3
-
 Persephonella marina DSM 14350 / EX-H1 CO2 + H2O
-
 r
4.2.1.1 H2CO3
-
 Methanothermobacter thermautotrophicus ATCC BAA-927 / DSM 2133 / JCM 14651 / NBRC 100331 / OCM 82 / Marburg CO2 + H2O
-
 r
4.2.1.1 H2CO3
-
 Thermovibrio ammonificans DSM 15698 / JCM 12110 / HB-1 CO2 + H2O
-
 r
4.2.1.1 additional information stopped-flow enzyme assay Methanothermobacter thermautotrophicus ?
-
 ?
4.2.1.1 additional information the enzyme also presents esterase activity Sulfurihydrogenibium sp. YO3AOP1 ?
-
 ?
4.2.1.1 additional information the enzyme shows very high activity compared to other carbonic anhydrases, it has also esterase activity Sulfurihydrogenibium azorense ?
-
 ?
4.2.1.1 additional information stopped-flow enzyme assay Methanothermobacter thermautotrophicus ATCC BAA-927 / DSM 2133 / JCM 14651 / NBRC 100331 / OCM 82 / Marburg ?
-
 ?

Subunits

EC Number Subunits Comment Organism
4.2.1.1 dimer enzyme Cab is a dimer with the typical alpha/beta fold of beta-CAs. The two monomers within the dimer are related by a 2fold axis and their structure consists of a central beta-sheet core composed of five strands. Upon dimer formation, an extended beta-sheet core encompassing the entire dimer is formed. Several alpha-helices pack onto this beta-structural motif, resulting in a large interface area between the two enzyme subunits Methanothermobacter thermautotrophicus
4.2.1.1 dimer enzyme SspCA forms a dimer characterized by a large interface area and stabilized by several polar and hydrophobic interactions Sulfurihydrogenibium sp. YO3AOP1
4.2.1.1 More enzyme Cab shows significant structural differences with respect to the other enzymes of beta-class in the N-terminus, C-terminus and in the region encompassing residues 90-125. Moreover, it presents a less extended C-terminal region, being the smallest beta-CA so far characterized Methanothermobacter thermautotrophicus
4.2.1.1 More the alpha-CA presents a fold characterized by a central ten-stranded beta-sheet surrounded by several helices and additional beta-strands. The active site is found in a deep conical cavity which extends from the protein surface to the center of the molecule, with the catalytic zinc ion positioned at the bottom of this cavity Sulfurihydrogenibium sp. YO3AOP1

Synonyms

EC Number Synonyms Comment Organism
4.2.1.1 alpha-CA
-
 Homo sapiens
4.2.1.1 alpha-CA
-
 Sulfurihydrogenibium azorense
4.2.1.1 alpha-CA
-
 Sulfurihydrogenibium sp. YO3AOP1
4.2.1.1 alpha-CA
-
 Persephonella marina
4.2.1.1 alpha-CA
-
 Thermovibrio ammonificans
4.2.1.1 alpha-CA
-
 Bos taurus
4.2.1.1 beta-CA
-
 Methanothermobacter thermautotrophicus
4.2.1.1 Cab
-
 Methanothermobacter thermautotrophicus
4.2.1.1 carbonic anhydrase II
-
 Homo sapiens
4.2.1.1 carbonic anhydrase II
-
 Bos taurus
4.2.1.1 CmCA
-
 Caminibacter mediatlanticus
4.2.1.1 cynT
-
 Desulfovibrio vulgaris
4.2.1.1 cynT
-
 Citrobacter freundii
4.2.1.1 DVU_1777
-
 Desulfovibrio vulgaris
4.2.1.1 gamma-CA
-
 Methanosarcina thermophila
4.2.1.1 gamma-CA
-
 Pyrococcus horikoshii
4.2.1.1 HCA II
-
 Homo sapiens
4.2.1.1 HCA II
-
 Bos taurus
4.2.1.1 MtCam
-
 Methanosarcina thermophila
4.2.1.1 PERMA_1443
-
 Persephonella marina
4.2.1.1 PhCamH
-
 Pyrococcus horikoshii
4.2.1.1 PMCA
-
 Persephonella marina
4.2.1.1 SazCA
-
 Sulfurihydrogenibium azorense
4.2.1.1 SspCA
-
 Sulfurihydrogenibium sp. YO3AOP1
4.2.1.1 TacA
-
 Thermovibrio ammonificans
4.2.1.1 Theam_1576
-
 Thermovibrio ammonificans

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
4.2.1.1 20
-
 assay at Homo sapiens
4.2.1.1 20
-
 assay at Persephonella marina
4.2.1.1 20
-
 assay at Thermovibrio ammonificans
4.2.1.1 25
-
 assay at Methanosarcina thermophila
4.2.1.1 25
-
 assay at Methanothermobacter thermautotrophicus
4.2.1.1 80
-
-
 Sulfurihydrogenibium azorense
4.2.1.1 95
-
-
 Sulfurihydrogenibium sp. YO3AOP1

Temperature Range [°C]

EC Number Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
4.2.1.1
-
 100 esterase and CO2 hydration activity, activity range Sulfurihydrogenibium azorense

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
4.2.1.1 40
-
 half-life of the enzyme is 152 days Thermovibrio ammonificans
4.2.1.1 40
-
 half-life of the enzyme is 53 days Sulfurihydrogenibium sp. YO3AOP1
4.2.1.1 40
-
 half-life of the enzyme is 6 days Bos taurus
4.2.1.1 40
-
 half-life of the enzyme is 75 days Persephonella marina
4.2.1.1 55 75 the purified enzyme retains catalytic activity if incubated for 15 min at 55°C, but only a little activity is recovered when the enzyme is incubated above 75°C Methanosarcina thermophila
4.2.1.1 60
-
 half-life of the enzyme is 29 days Persephonella marina
4.2.1.1 60
-
 half-life of the enzyme is 77 days Thermovibrio ammonificans
4.2.1.1 70
-
 half-life of the enzyme is 8 days Sulfurihydrogenibium sp. YO3AOP1
4.2.1.1 70
-
 half-life of the enzyme is less than one day Bos taurus
4.2.1.1 75 90 enzyme Cab retains its activity after incubation at temperatures up to 75°C for 15 min, whereas poor activity is recovered when the enzyme is incubated at temperatures of 90°C or higher Methanothermobacter thermautotrophicus
4.2.1.1 100
-
 purified enzyme SazCA is able to retain CO2 hydration activity after incubation for 3 h Sulfurihydrogenibium azorense

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
4.2.1.1 17000
-
 H2CO3 pH 8.5, 25°C Methanothermobacter thermautotrophicus
4.2.1.1 68000
-
 H2CO3 pH 7.5, 25°C, recombinant enzyme expressed from Escherichia coli and aerobically purified Methanosarcina thermophila
4.2.1.1 231000
-
 H2CO3 pH 7.5, 25°C, recombinant enzyme expressed from Methanosarcina acetivorans and anaerobically purified Methanosarcina thermophila
4.2.1.1 243000
-
 H2CO3 pH 7.5, 25°C, recombinant enzyme expressed from Escherichia coli and anaerobically purified Methanosarcina thermophila
4.2.1.1 320000
-
 H2CO3 pH 7.5, 20°C Persephonella marina
4.2.1.1 935000
-
 H2CO3 pH 7.5, 20°C Sulfurihydrogenibium sp. YO3AOP1
4.2.1.1 1400000
-
 H2CO3 pH 7.5, 20°C Homo sapiens
4.2.1.1 1600000
-
 H2CO3 pH 7.5, 20°C Thermovibrio ammonificans
4.2.1.1 4400000
-
 H2CO3 pH 7.5, 20°C Sulfurihydrogenibium azorense

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
4.2.1.1 7.5
-
 assay at Methanosarcina thermophila
4.2.1.1 7.5
-
 assay at Homo sapiens
4.2.1.1 7.5
-
 assay at Sulfurihydrogenibium azorense
4.2.1.1 7.5
-
 assay at Sulfurihydrogenibium sp. YO3AOP1
4.2.1.1 7.5
-
 assay at Persephonella marina
4.2.1.1 7.5
-
 assay at Thermovibrio ammonificans
4.2.1.1 8.5
-
 assay at Methanothermobacter thermautotrophicus

General Information

EC Number General Information Comment Organism
4.2.1.1 evolution the dimeric arrangement is a peculiar feature of all bacterial alpha-CAs so far structurally characterized Homo sapiens
4.2.1.1 evolution the dimeric arrangement is a peculiar feature of all bacterial alpha-CAs so far structurally characterized Sulfurihydrogenibium azorense
4.2.1.1 evolution the dimeric arrangement is a peculiar feature of all bacterial alpha-CAs so far structurally characterized Sulfurihydrogenibium sp. YO3AOP1
4.2.1.1 evolution the dimeric arrangement is a peculiar feature of all bacterial alpha-CAs so far structurally characterized Persephonella marina
4.2.1.1 evolution the dimeric arrangement is a peculiar feature of all bacterial alpha-CAs so far structurally characterized Thermovibrio ammonificans
4.2.1.1 evolution the dimeric arrangement is a peculiar feature of all bacterial alpha-CAs so far structurally characterized Bos taurus
4.2.1.1 additional information structure analysis. Enzyme Cab shows significant structural differences with respect to the other enzymes of beta-class in the N-terminus, C-terminus and in the region encompassing residues 90-125. Moreover, it presents a less extended C-terminal region, being the smallest beta-CA so far characterized Methanothermobacter thermautotrophicus
4.2.1.1 additional information structure comparisons Homo sapiens
4.2.1.1 additional information structure comparisons Pyrococcus horikoshii
4.2.1.1 additional information structure comparisons, residues His2 and His207 in enzyme SazCA from Sulphurihydrogenibium azorense, as compared to Glu2 and Gln207 in enzyme SspCA from Sulfurihydrogenibium yellowstonense, are proposed to be responsible for the higher SazCA catalytic activity Sulfurihydrogenibium sp. YO3AOP1
4.2.1.1 additional information structure comparisons, residues His2 and His207 in SazCA, compared Glu2 and Gln207 in enzyme SspCA from Sulfurihydrogenibium yellowstonense, are proposed to be responsible for the higher SazCA catalytic activity Sulfurihydrogenibium azorense
4.2.1.1 physiological function gamma-CAs are widely distributed in all three phylogenetic domains of life, playing important roles in the global carbon cycle Methanosarcina thermophila
4.2.1.1 physiological function gamma-CAs are widely distributed in all three phylogenetic domains of life, playing important roles in the global carbon cycle Pyrococcus horikoshii

kcat/KM [mM/s]

EC Number kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
4.2.1.1 3100
-
 H2CO3 pH 7.5, 25°C, recombinant enzyme expressed from Escherichia coli and aerobically purified Methanosarcina thermophila
4.2.1.1 3900
-
 H2CO3 pH 7.5, 25°C, recombinant enzyme expressed from Methanosarcina acetivorans and anaerobically purified Methanosarcina thermophila
4.2.1.1 5400
-
 H2CO3 pH 7.5, 25°C, recombinant enzyme expressed from Escherichia coli and anaerobically purified Methanosarcina thermophila
4.2.1.1 5900
-
 H2CO3 pH 8.5, 25°C Methanothermobacter thermautotrophicus
4.2.1.1 30000
-
 H2CO3 pH 7.5, 20°C Persephonella marina
4.2.1.1 110000
-
 H2CO3 pH 7.5, 20°C Sulfurihydrogenibium sp. YO3AOP1
4.2.1.1 150000
-
 H2CO3 pH 7.5, 20°C Homo sapiens
4.2.1.1 160000
-
 H2CO3 pH 7.5, 20°C Thermovibrio ammonificans
4.2.1.1 350000
-
 H2CO3 pH 7.5, 20°C Sulfurihydrogenibium azorense