Literature summary for 4.2.1.1 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 .

Application

Application	Comment	Organism
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
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
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
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
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
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
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
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
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
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
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
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
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)

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

Crystallization (Commentary)

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

Protein Variants

Protein Variants	Comment	Organism
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
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
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
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
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
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
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
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
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
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
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
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

Inhibitors	Comment	Organism	Structure
acetazolamide	-	Sulfurihydrogenibium sp. YO3AOP1

KM Value [mM]

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

Metals/Ions

Metals/Ions	Comment	Organism
Co2+	activates to a 2fold activity compared to the activity with Zn2+	Methanosarcina thermophila
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
additional information	analysis of three-dimensional structures of MtCam, in both Zn- and Co-bound forms, overview. Structure comparisons	Methanosarcina thermophila
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
Zn2+	metalloenzyme, the metal ion is required for catalytic activity, coordinated by three residues	Methanosarcina thermophila
Zn2+	metalloenzyme, the metal ion is required for catalytic activity, coordinated by three residues	Homo sapiens
Zn2+	metalloenzyme, the metal ion is required for catalytic activity, coordinated by three residues	Sulfurihydrogenibium azorense
Zn2+	metalloenzyme, the metal ion is required for catalytic activity, coordinated by three residues	Pyrococcus horikoshii
Zn2+	metalloenzyme, the metal ion is required for catalytic activity, coordinated by three residues	Caminibacter mediatlanticus
Zn2+	metalloenzyme, the metal ion is required for catalytic activity, coordinated by three residues	Desulfovibrio vulgaris
Zn2+	metalloenzyme, the metal ion is required for catalytic activity, coordinated by three residues	Serratia sp. ISTD04
Zn2+	metalloenzyme, the metal ion is required for catalytic activity, coordinated by three residues	Citrobacter freundii
Zn2+	metalloenzyme, the metal ion is required for catalytic activity, coordinated by three residues	Persephonella marina
Zn2+	metalloenzyme, the metal ion is required for catalytic activity, coordinated by three residues	Thermovibrio ammonificans
Zn2+	metalloenzyme, the metal ion is required for catalytic activity, coordinated by three residues	Bos taurus
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)

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

Organism

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

Purification (Commentary)

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

Reaction

Reaction	Comment	Organism	Reaction ID
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
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
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
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
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
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
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
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
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
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
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
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
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)

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

Subunits

Subunits	Comment	Organism
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
dimer	enzyme SspCA forms a dimer characterized by a large interface area and stabilized by several polar and hydrophobic interactions	Sulfurihydrogenibium sp. YO3AOP1
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
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

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

Temperature Optimum [°C]

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

Temperature Range [°C]

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

Temperature Stability [°C]

Temperature Stability Minimum [°C]	Temperature Stability Maximum [°C]	Comment	Organism
40	-	half-life of the enzyme is 152 days	Thermovibrio ammonificans
40	-	half-life of the enzyme is 53 days	Sulfurihydrogenibium sp. YO3AOP1
40	-	half-life of the enzyme is 6 days	Bos taurus
40	-	half-life of the enzyme is 75 days	Persephonella marina
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
60	-	half-life of the enzyme is 29 days	Persephonella marina
60	-	half-life of the enzyme is 77 days	Thermovibrio ammonificans
70	-	half-life of the enzyme is 8 days	Sulfurihydrogenibium sp. YO3AOP1
70	-	half-life of the enzyme is less than one day	Bos taurus
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
100	-	purified enzyme SazCA is able to retain CO2 hydration activity after incubation for 3 h	Sulfurihydrogenibium azorense

Turnover Number [1/s]

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

pH Optimum

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

General Information

General Information	Comment	Organism
evolution	the dimeric arrangement is a peculiar feature of all bacterial alpha-CAs so far structurally characterized	Homo sapiens
evolution	the dimeric arrangement is a peculiar feature of all bacterial alpha-CAs so far structurally characterized	Sulfurihydrogenibium azorense
evolution	the dimeric arrangement is a peculiar feature of all bacterial alpha-CAs so far structurally characterized	Sulfurihydrogenibium sp. YO3AOP1
evolution	the dimeric arrangement is a peculiar feature of all bacterial alpha-CAs so far structurally characterized	Persephonella marina
evolution	the dimeric arrangement is a peculiar feature of all bacterial alpha-CAs so far structurally characterized	Thermovibrio ammonificans
evolution	the dimeric arrangement is a peculiar feature of all bacterial alpha-CAs so far structurally characterized	Bos taurus
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
additional information	structure comparisons	Homo sapiens
additional information	structure comparisons	Pyrococcus horikoshii
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
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
physiological function	gamma-CAs are widely distributed in all three phylogenetic domains of life, playing important roles in the global carbon cycle	Methanosarcina thermophila
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]

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