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Literature summary extracted from
- Highly thermostable carbonic anhydrase from Persephonella marina EX-H1 its expression and characterization for CO2-sequestration applications (2014), Process Biochem., 49, 2114-2121 .
No PubMed abstract available
Cloned(Commentary)
| EC Number | Cloned (Comment) | Organism |
|---|---|---|
| 4.2.1.1 | gene PERMA_1443, phylogenetic tree, recombinant expression of His-tagged enzyme lacking the signal peptide from codon-optimized carbonic anhydrase gene in Escherichia coli strain BL21(DE3), real-time PCR enzyme expression analysis | Persephonella marina |
Inhibitors
| EC Number | Inhibitors | Comment | Organism | Structure |
|---|---|---|---|---|
| 4.2.1.1 | Ag+ | - |
Persephonella marina |  |
| 4.2.1.1 | Al3+ | - |
Persephonella marina | |
| 4.2.1.1 | Cu2+ | - |
Persephonella marina | |
| 4.2.1.1 | Fe3+ | - |
Persephonella marina | |
| 4.2.1.1 | Hg2+ | - |
Persephonella marina | |
| 4.2.1.1 | Pb2+ | - |
Persephonella marina | |
KM Value [mM]
| EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 4.2.1.1 | 10.8 | - |
CO2 | pH 7.8, 25°C, recombinant enzyme | Persephonella marina | |
Metals/Ions
| EC Number | Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|---|
| 4.2.1.1 | Co2+ | activates the recombinant enzyme lacking the signal peptide | Persephonella marina | |
| 4.2.1.1 | additional information | the recombinant enzyme activity is not affected significantly by the presence of Ca2+, Mg2+, or K+ ions | Persephonella marina | |
| 4.2.1.1 | Zn2+ | required, metalloenzyme, activates the recombinant enzyme lacking the signal peptide | Persephonella marina | |
Natural Substrates/ Products (Substrates)
| EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 4.2.1.1 | H2CO3 | Persephonella marina | - |
CO2 + H2O | - |
r | |
| 4.2.1.1 | H2CO3 | Persephonella marina DSM 14350 / EX-H1 | - |
CO2 + H2O | - |
r | |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 4.2.1.1 | Persephonella marina | C0QRB5 | - |
- |
| 4.2.1.1 | Persephonella marina DSM 14350 / EX-H1 | C0QRB5 | - |
- |
Purification (Commentary)
| EC Number | Purification (Comment) | Organism |
|---|---|---|
| 4.2.1.1 | recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography, dialysis, and ultrafiltration | Persephonella marina |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 4.2.1.1 | CO2 + H2O | - |
Persephonella marina | H2CO3 | - |
r | |
| 4.2.1.1 | CO2 + H2O | - |
Persephonella marina DSM 14350 / EX-H1 | H2CO3 | - |
r | |
| 4.2.1.1 | H2CO3 | - |
Persephonella marina | CO2 + H2O | - |
r | |
| 4.2.1.1 | H2CO3 | - |
Persephonella marina DSM 14350 / EX-H1 | CO2 + H2O | - |
r | |
| 4.2.1.1 | additional information | enzyme activity measurement by determining the enzyme's CO2 hydration activity and esterase activity with substrate 4-nitrophenyl acetate. The recombinant enzyme lacking the signal peptide can efficiently catalyze the hydration of CO2, precipitating CaCO3 as calcite in the presence of Ca2+ | Persephonella marina | ? | - |
? | |
| 4.2.1.1 | additional information | enzyme activity measurement by determining the enzyme's CO2 hydration activity and esterase activity with substrate 4-nitrophenyl acetate. The recombinant enzyme lacking the signal peptide can efficiently catalyze the hydration of CO2, precipitating CaCO3 as calcite in the presence of Ca2+ | Persephonella marina DSM 14350 / EX-H1 | ? | - |
? | |
Subunits
| EC Number | Subunits | Comment | Organism |
|---|---|---|---|
| 4.2.1.1 | homodimer | - |
Persephonella marina |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 4.2.1.1 | alpha-type CA | - |
Persephonella marina |
| 4.2.1.1 | PERMA_1443 | - |
Persephonella marina |
| 4.2.1.1 | PMCA | - |
Persephonella marina |
Temperature Optimum [°C]
| EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 4.2.1.1 | - |
4 | esterase assay at | Persephonella marina |
| 4.2.1.1 | 25 | - |
CO2hydration reaction, assay at | Persephonella marina |
| 4.2.1.1 | 35 | 45 | CA-catalyzed sequestration of CO2 hydration, assay at | Persephonella marina |
Temperature Stability [°C]
| EC Number | Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 4.2.1.1 | 30 | 100 | purified recombinant His-tagged enzyme lacking the signal peptide, pH 7.6, 15 min, slow decrease in the enzyme activity at temperatures up to 50°C and almost no effect beyond 50°C up to 100°C. The enzyme retains over 80% of its activity between 60°C and 100°C, the Tm is 84.5°C | Persephonella marina |
Turnover Number [1/s]
| EC Number | Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 4.2.1.1 | 320000 | - |
CO2 | pH 7.8, 25°C, recombinant enzyme | Persephonella marina | |
pH Optimum
| EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|---|
| 4.2.1.1 | 7.4 | - |
esterase assay at | Persephonella marina |
| 4.2.1.1 | 7.8 | 8.3 | assay at, the pH drops during the CO2 hydration reaction to pH 6.2 | Persephonella marina |
pH Range
| EC Number | pH Minimum | pH Maximum | Comment | Organism |
|---|---|---|---|---|
| 4.2.1.1 | 4 | 10 | activity range, recombinant enzyme | Persephonella marina |
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 | 30000 | - |
CO2 | pH 7.8, 25°C, recombinant enzyme | Persephonella marina | |
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