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Literature summary extracted from
- Novel alkalistable alpha-carbonic anhydrase from the polyextremophilic bacterium Bacillus halodurans characteristics and applicability in flue gas CO2 sequestration (2016), Environ. Sci. Pollut. Res. Int., 23, 15236-15249 .
Cloned(Commentary)
| EC Number | Cloned (Comment) | Organism |
|---|---|---|
| 4.2.1.1 | BhCA, recombinant constitutive extracellular expression of the enzyme in Pichia pastoris strain GS115 under methanol inducible (AOX1) as well as constitutive (GAP) promoters, the recombinant enzyme is secreted. The double transformant of the strain GS115 harboring BhCA under both AOX1 and GAP promoters possessed two copies of the gene | Halalkalibacterium halodurans |
Protein Variants
| EC Number | Protein Variants | Comment | Organism |
|---|---|---|---|
| 4.2.1.1 | additional information | the recombinant enzyme expressed from Pichia pastoris has a higher thermostability, a higher molecular weight and is glycosylated, as compared the unglycosylated recombinant enzyme expressed from Escherichia coli, overview | Halalkalibacterium halodurans |
Inhibitors
| EC Number | Inhibitors | Comment | Organism | Structure |
|---|---|---|---|---|
| 4.2.1.1 | Co2+ | inhibitits by 80-100% at 5 mM | Halalkalibacterium halodurans |  |
| 4.2.1.1 | Cu2+ | inhibitits by 80-100% at 5 mM | Halalkalibacterium halodurans | |
| 4.2.1.1 | Fe2+ | inhibitits by 80-100% at 5 mM | Halalkalibacterium halodurans | |
| 4.2.1.1 | Hg2+ | inhibitits by 80-100% at 5 mM | Halalkalibacterium halodurans | |
| 4.2.1.1 | Ni2+ | inhibitits by 80-100% at 5 mM | Halalkalibacterium halodurans | |
Metals/Ions
| EC Number | Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|---|
| 4.2.1.1 | additional information | rBhCA activity is unaffected by Na+ and Cl- up to 1.0 M or by Pb2+ at 1 mM. rBhCA is able to tolerate high concentration of NO32- and SO32- up to 1 M without losing activity | Halalkalibacterium halodurans | |
| 4.2.1.1 | Sn2+ | stimulates at 5 mM | Halalkalibacterium halodurans | |
| 4.2.1.1 | SO42- | the recombinant enzyme displays the unique property of stimulation in presence of SO42- | Halalkalibacterium halodurans | |
Molecular Weight [Da]
| EC Number | Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|---|
| 4.2.1.1 | 79500 | - |
about, recombinant enzyme, gel filtration and native PAGE | Halalkalibacterium halodurans |
Natural Substrates/ Products (Substrates)
| EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 4.2.1.1 | H2CO3 | Halalkalibacterium halodurans | - |
CO2 + H2O | - |
r | |
| 4.2.1.1 | H2CO3 | Halalkalibacterium halodurans TSLV1 / MTCC 10961 | - |
CO2 + H2O | - |
r | |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 4.2.1.1 | Halalkalibacterium halodurans | A0A0N9WRG3 | - |
- |
| 4.2.1.1 | Halalkalibacterium halodurans TSLV1 / MTCC 10961 | A0A0N9WRG3 | - |
- |
Posttranslational Modification
| EC Number | Posttranslational Modification | Comment | Organism |
|---|---|---|---|
| 4.2.1.1 | glycoprotein | the recombinant enzyme BhCA expressed in Pichia pastoris strain GS115 is a glycosylated protein. rBhCA possesses two potential N-glycosylation sites and many O-glycosylation sites. Enzyme deglycosylation by endoglycosylase H | Halalkalibacterium halodurans |
Purification (Commentary)
| EC Number | Purification (Comment) | Organism |
|---|---|---|
| 4.2.1.1 | recombinant extracellular enzyme from Pichia pastoris strain GS115 culture supernatant by ultrafiltration, acetone precipitation, and pAMBS affinity chromatography | Halalkalibacterium halodurans |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 4.2.1.1 | H2CO3 | - |
Halalkalibacterium halodurans | CO2 + H2O | - |
r | |
| 4.2.1.1 | H2CO3 | - |
Halalkalibacterium halodurans TSLV1 / MTCC 10961 | CO2 + H2O | - |
r | |
| 4.2.1.1 | additional information | the enzyme effectively sequesters CO2 into calcite form of CaCO3 | Halalkalibacterium halodurans | ? | - |
? | |
| 4.2.1.1 | additional information | the enzyme effectively sequesters CO2 into calcite form of CaCO3 | Halalkalibacterium halodurans TSLV1 / MTCC 10961 | ? | - |
? | |
Subunits
| EC Number | Subunits | Comment | Organism |
|---|---|---|---|
| 4.2.1.1 | homodimer | 2 * 39500, recombinant glycosylated enzyme, SDS-PAGE, 2 * 37500, recombinant deglycosylated enzyme, SDS-PAGE | Halalkalibacterium halodurans |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 4.2.1.1 | alkalistable alpha-carbonic anhydrase | - |
Halalkalibacterium halodurans |
| 4.2.1.1 | alpha-carbonic anhydrase | - |
Halalkalibacterium halodurans |
| 4.2.1.1 | BhCA | - |
Halalkalibacterium halodurans |
Temperature Optimum [°C]
| EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 4.2.1.1 | 4 | - |
assay at | Halalkalibacterium halodurans |
Temperature Stability [°C]
| EC Number | Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 4.2.1.1 | additional information | - |
the thermal unfolding of recombinant BhCA is studied by using circular dichroism | Halalkalibacterium halodurans |
| 4.2.1.1 | 40 | - |
purified recombinant enzyme, stable at | Halalkalibacterium halodurans |
| 4.2.1.1 | 50 | 80 | the T1/2 values at 50°C, 60°C, 70°C, and 80 °C are 72, 32, 7.0, and 2.0 min | Halalkalibacterium halodurans |
| 4.2.1.1 | 75 | - |
purified recombinant enzyme, Tm value | Halalkalibacterium halodurans |
pH Optimum
| EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|---|
| 4.2.1.1 | 8.3 | - |
assay at, initial pH value, the value drops to pH 7.3 during the reaction | Halalkalibacterium halodurans |
pH Range
| EC Number | pH Minimum | pH Maximum | Comment | Organism |
|---|---|---|---|---|
| 4.2.1.1 | 6 | 11 | activity range | Halalkalibacterium halodurans |
pH Stability
| EC Number | pH Stability | pH Stability Maximum | Comment | Organism |
|---|---|---|---|---|
| 4.2.1.1 | 1 | 2 | purified recombinant enzyme, stable for 2 h, complete loss of activity after 12 h | Halalkalibacterium halodurans |
| 4.2.1.1 | 6 | 11 | purified recombinant enzyme, 100% activity remaining after 48 h | Halalkalibacterium halodurans |
General Information
| EC Number | General Information | Comment | Organism |
|---|---|---|---|
| 4.2.1.1 | physiological function | the carbonic anhydrase catalyzed hydration of CO2 is fundamental to many vital physiological functions in living organisms such as pH homeostasis, ion transport, carbon concentrating mechanism (plants and many microorganisms), and in biosynthesis of physiologically important metabolites | Halalkalibacterium halodurans |
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Release 2023.1 (January 2023)
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