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Literature summary extracted from
- Enhanced biomimetic sequestration of CO2 into CaCO3 using purified carbonic anhydrase from indigenous bacterial strains (2010), J. Mol. Catal. B, 67, 122-128.
No PubMed abstract available
Application
| EC Number | Application | Comment | Organism |
|---|---|---|---|
| 4.2.1.1 | environmental protection | the enzyme can be useful in biomimetic sequestration of CO2 into CaCO3 as a biological catalyst | Bos taurus |
| 4.2.1.1 | environmental protection | the enzyme can be useful in biomimetic sequestration of CO2 into CaCO3 as a biological catalyst | Micrococcus luteus |
| 4.2.1.1 | environmental protection | the enzyme can be useful in biomimetic sequestration of CO2 into CaCO3 as a biological catalyst | Pseudomonas fragi |
| 4.2.1.1 | environmental protection | the enzyme can be useful in biomimetic sequestration of CO2 into CaCO3 as a biological catalyst | Micrococcus lylae |
Inhibitors
| EC Number | Inhibitors | Comment | Organism | Structure |
|---|---|---|---|---|
| 4.2.1.1 | As3+ | - |
Bos taurus |  |
| 4.2.1.1 | As3+ | - |
Micrococcus luteus | |
| 4.2.1.1 | As3+ | - |
Micrococcus lylae | |
| 4.2.1.1 | As3+ | - |
Pseudomonas fragi | |
| 4.2.1.1 | bicarbonate | - |
Bos taurus | |
| 4.2.1.1 | bicarbonate | - |
Micrococcus luteus | |
| 4.2.1.1 | bicarbonate | - |
Micrococcus lylae | |
| 4.2.1.1 | bicarbonate | - |
Pseudomonas fragi | |
| 4.2.1.1 | bromide | - |
Micrococcus luteus | |
| 4.2.1.1 | bromide | - |
Micrococcus lylae | |
| 4.2.1.1 | bromide | - |
Pseudomonas fragi | |
| 4.2.1.1 | Ca2+ | 25% inhibition at 0.2 mM | Bos taurus | |
| 4.2.1.1 | Ca2+ | 25% inhibition at 0.2 mM | Micrococcus luteus | |
| 4.2.1.1 | Ca2+ | 25% inhibition at 0.2 mM | Micrococcus lylae | |
| 4.2.1.1 | Ca2+ | 25% inhibition at 0.2 mM | Pseudomonas fragi | |
| 4.2.1.1 | chloride | - |
Bos taurus | |
| 4.2.1.1 | chloride | - |
Micrococcus luteus | |
| 4.2.1.1 | chloride | - |
Micrococcus lylae | |
| 4.2.1.1 | chloride | - |
Pseudomonas fragi | |
| 4.2.1.1 | Hg2+ | - |
Bos taurus | |
| 4.2.1.1 | Hg2+ | - |
Micrococcus luteus | |
| 4.2.1.1 | Hg2+ | - |
Micrococcus lylae | |
| 4.2.1.1 | Hg2+ | - |
Pseudomonas fragi | |
| 4.2.1.1 | Iodide | - |
Micrococcus luteus | |
| 4.2.1.1 | Iodide | - |
Micrococcus lylae | |
| 4.2.1.1 | Iodide | - |
Pseudomonas fragi | |
| 4.2.1.1 | K+ | 25% inhibition at 0.2 mM | Bos taurus | |
| 4.2.1.1 | K+ | 25% inhibition at 0.2 mM | Micrococcus luteus | |
| 4.2.1.1 | K+ | 25% inhibition at 0.2 mM | Micrococcus lylae | |
| 4.2.1.1 | K+ | 25% inhibition at 0.2 mM | Pseudomonas fragi | |
| 4.2.1.1 | Mg2+ | 25% inhibition at 0.2 mM | Bos taurus | |
| 4.2.1.1 | Mg2+ | 25% inhibition at 0.2 mM | Micrococcus luteus | |
| 4.2.1.1 | Mg2+ | 25% inhibition at 0.2 mM | Micrococcus lylae | |
| 4.2.1.1 | Mg2+ | 25% inhibition at 0.2 mM | Pseudomonas fragi | |
| 4.2.1.1 | Na+ | 25% inhibition at 0.2 mM | Bos taurus | |
| 4.2.1.1 | Na+ | 25% inhibition at 0.2 mM | Micrococcus luteus | |
| 4.2.1.1 | Na+ | 25% inhibition at 0.2 mM | Micrococcus lylae | |
| 4.2.1.1 | Na+ | 25% inhibition at 0.2 mM | Pseudomonas fragi | |
| 4.2.1.1 | nitrate | - |
Bos taurus | |
| 4.2.1.1 | nitrate | - |
Micrococcus luteus | |
| 4.2.1.1 | nitrate | - |
Micrococcus lylae | |
| 4.2.1.1 | nitrate | - |
Pseudomonas fragi | |
| 4.2.1.1 | Pb2+ | - |
Bos taurus | |
| 4.2.1.1 | Pb2+ | - |
Micrococcus luteus | |
| 4.2.1.1 | Pb2+ | - |
Micrococcus lylae | |
| 4.2.1.1 | Pb2+ | - |
Pseudomonas fragi | |
| 4.2.1.1 | sulfate | - |
Bos taurus | |
| 4.2.1.1 | sulfate | - |
Micrococcus luteus | |
| 4.2.1.1 | sulfate | - |
Micrococcus lylae | |
| 4.2.1.1 | sulfate | - |
Pseudomonas fragi | |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 4.2.1.1 | Bos taurus | - |
- |
- |
| 4.2.1.1 | Micrococcus luteus | - |
- |
- |
| 4.2.1.1 | Micrococcus luteus 2 | - |
- |
- |
| 4.2.1.1 | Micrococcus lylae | - |
- |
- |
| 4.2.1.1 | Pseudomonas fragi | - |
- |
- |
Source Tissue
| EC Number | Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|---|
| 4.2.1.1 | commercial preparation | - |
Bos taurus | - |
Specific Activity [micromol/min/mg]
| EC Number | Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
|---|---|---|---|---|
| 4.2.1.1 | 61 | - |
purified enzyme, pH 8.3, 4°C | Micrococcus luteus |
| 4.2.1.1 | 66.5 | - |
purified enzyme, pH 8.3, 4°C | Micrococcus lylae |
| 4.2.1.1 | 70.6 | - |
purified enzyme, pH 8.3, 4°C | Pseudomonas fragi |
| 4.2.1.1 | 74.6 | - |
purified enzyme, pH 8.3, 4°C | Bos taurus |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 4.2.1.1 | carbonic anhydrase | - |
Bos taurus |
| 4.2.1.1 | carbonic anhydrase | - |
Micrococcus luteus |
| 4.2.1.1 | carbonic anhydrase | - |
Pseudomonas fragi |
| 4.2.1.1 | carbonic anhydrase | - |
Micrococcus lylae |
Temperature Optimum [°C]
| EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 4.2.1.1 | 4 | - |
assay at | Bos taurus |
| 4.2.1.1 | 4 | - |
assay at | Micrococcus luteus |
| 4.2.1.1 | 4 | - |
assay at | Pseudomonas fragi |
| 4.2.1.1 | 4 | - |
assay at | Micrococcus lylae |
Temperature Stability [°C]
| EC Number | Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 4.2.1.1 | additional information | - |
effect of pH and temperature as function of time on stability of carbonic anhydrases from different species, overview | Bos taurus |
| 4.2.1.1 | additional information | - |
effect of pH and temperature as function of time on stability of carbonic anhydrases from different species, overview | Micrococcus luteus |
| 4.2.1.1 | additional information | - |
effect of pH and temperature as function of time on stability of CAs from different species, overview | Pseudomonas fragi |
| 4.2.1.1 | additional information | - |
the enzyme exhibits more than 80% stability between pH 7.0 and pH 8.0, while 68% and 57% are retained at pH 8.5 and pH 9.0 after 3 h of incubation. The enzyme retains 63%, 54% and 45% residual activity at pH 8.0, pH 8.5, and pH 9.0, respectively, following 6 h of incubation. Effect of pH and temperature as function of time on stability of CAs from different species, overview | Micrococcus lylae |
| 4.2.1.1 | 35 | 45 | the purifed enzyme retains 38-54% after 6 h | Bos taurus |
| 4.2.1.1 | 35 | 45 | the purifed enzyme retains 40-51% after 6 h | Micrococcus lylae |
| 4.2.1.1 | 35 | 45 | the purifed enzyme retains 65-50% after 6 h | Pseudomonas fragi |
| 4.2.1.1 | 35 | 45 | the purifed enzyme retains 71-83% after 6 h | Micrococcus luteus |
pH Optimum
| EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|---|
| 4.2.1.1 | 8.3 | - |
assay at | Bos taurus |
| 4.2.1.1 | 8.3 | - |
assay at | Micrococcus luteus |
| 4.2.1.1 | 8.3 | - |
assay at | Pseudomonas fragi |
| 4.2.1.1 | 8.3 | - |
assay at | Micrococcus lylae |
pH Stability
| EC Number | pH Stability | pH Stability Maximum | Comment | Organism |
|---|---|---|---|---|
| 4.2.1.1 | additional information | - |
42%, 39% and 36% stability is observed at pH 8.0, pH 8.5, and pH 9.0, respectively for commercial bovine carbonic anhydrase following 6 h of incubation. After 3 h incubation at pH 7.0 and pH 7.5, bovin retains 81% and 75% residual activity, while 79%, 69%, 61%, stability is observed at pH 8.0, pH 8.5, and pH 9.0, respectively. Effect of pH and temperature as function of time on stability of carbonic anhydrases from different species, overview | Bos taurus |
| 4.2.1.1 | additional information | - |
effect of pH and temperature as function of time on stability of CAs from different species, overview | Micrococcus lylae |
| 4.2.1.1 | additional information | - |
the enzyme shows 78% stability along with 71% and 73% residual activity at pH 8.0 and pH 9.0, respectively, following 6 h of incubation, after 3 h of incubation 80% stability is observed between pH 7.5-9.0, effect of pH and temperature as function of time on stability of CAs from different species, overview | Micrococcus luteus |
| 4.2.1.1 | 7 | 9 | the enzyme retains 88% residual activity at pH 8.0, 72% residual activity at pH 8.5, and 66% residual activity at pH 9.0 following 6 h of incubation, stable at 80% of maximal activity in the pH range pH 7.0-9.0 following 3 h of incubation, effect of pH and temperature as function of time on stability of carbonic anhydrases from different species, overview | Pseudomonas fragi |
General Information
| EC Number | General Information | Comment | Organism |
|---|---|---|---|
| 4.2.1.1 | additional information | evaluation of efficiency of enzymes from Pseudomonas fragi, Micrococcus lylae, and Micrococcus luteus 2 compared to commercial Bos taurus carbonic anhydrase as biocatalysts in biomimetic sequestration of CO2 into CaCO3, the compared parameters are stability, inhibition rates by toxic metals, and pH dependency, overview. Indigenous carbonic anhydrases and their consortia exhibit enhanced CO2 sequestration competence compared to commercial bovine carbonic anhydrase | Bos taurus |
| 4.2.1.1 | additional information | evaluation of efficiency of enzymes from Pseudomonas fragi, Micrococcus lylae, and Micrococcus luteus 2 compared to commercial Bos taurus carbonic anhydrase as biocatalysts in biomimetic sequestration of CO2 into CaCO3, the compared parameters are stability, inhibition rates by toxic metals, and pH dependency, overview. Indigenous carbonic anhydrases and their consortia exhibit enhanced CO2 sequestration competence compared to commercial bovine carbonic anhydrase | Micrococcus luteus |
| 4.2.1.1 | additional information | Pseudomonas fragi, Micrococcus lylae and Micrococcus luteus 2 along with a comparative evaluation of their efficiency compared to commercial Bis taurus carbonic anhydrase as biocatalysts in biomimetic sequestration of CO2 into CaCO3, aparameters are stability, inhibition rates by toxic metals, and pH dependency, overview. Indigenous CAs and their consortia exhibit enhanced CO2 sequestration competence compared to commercial bovine CA | Pseudomonas fragi |
| 4.2.1.1 | additional information | Pseudomonas fragi, Micrococcus lylae and Micrococcus luteus 2 along with a comparative evaluation of their efficiency compared to commercial Bis taurus carbonic anhydrase as biocatalysts in biomimetic sequestration of CO2 into CaCO3, aparameters are stability, inhibition rates by toxic metals, and pH dependency, overview. Indigenous CAs and their consortia exhibit enhanced CO2 sequestration competence compared to commercial bovine CA | Micrococcus lylae |
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