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evolution
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carbonic anhydrase represents one of the most ancient proteins
evolution
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carbonic anhydrase represents one of the most ancient proteins
evolution
evolutionary tree of some bacterial beta-CAs among which the two Brucella suis isozymes bsCA I and bsCA II, phylogenetic analysis, overview
evolution
HICA is a type II member of the beta-carbonic anhydrase family
evolution
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phylogenetic analysis of beta-class carbonic anhydrases in invertebrates, overview
evolution
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carbonic anhydrase is a member of zinc-containing metalloenzyme family
evolution
A0A2D1CFJ9
comparisons of putative active site residues between CA II and CA VI from humans and several fishes
evolution
evolutionary relationship analysis, phylogenetic tree, the enzyme belongs to the beta class of carbonic anhydrases, subgroup of type II beta-CAs. The enzyme B13-CA has all the features of a catalytically effective beta-CA: (i) the putative Zn(II) ligands, Cys42, Asp44, His 98 and Cys101, (ii) the catalytic dyad involved in activation of the zinc-coordinated water molecule/hydroxide ion for catalysis, represented by the Asp44-Arg46 residues, which resembles in a way the activation of the water molecule in aspartic proteases
evolution
phylogenetic analysis indicates that Pl-CAN is evolutionarily closer to humans among chordates than to other species
evolution
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phylogenetic tree of gamma-CAs
evolution
several genetically distinct classes of carbonic anhydrase (CAs) exist, e.g. alpha-, beta-, gamma-, delta- and zeta-, and all of them are metalloenzymes. delta-CAs are closer to the alpha-CAs than to the other classes of the enzymes, phylogenetic analysis
evolution
the dimeric arrangement is a peculiar feature of all bacterial alpha-CAs so far structurally characterized
evolution
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the dimeric arrangement is a peculiar feature of all bacterial alpha-CAs so far structurally characterized
evolution
the dimeric arrangement is a peculiar feature of all bacterial alpha-CAs so far structurally characterized
evolution
the dimeric arrangement is a peculiar feature of all bacterial alpha-CAs so far structurally characterized
evolution
the dimeric arrangement is a peculiar feature of all bacterial alpha-CAs so far structurally characterized
evolution
the dimeric arrangement is a peculiar feature of all bacterial alpha-CAs so far structurally characterized
evolution
the enzyme belongs to the eta-CA class. Six genetically distinct CA families are known to date, the alpha-, beta-, gamma-, delta-, zeta- and eta-CAs. The alpha-, beta-, delta- and probably eta-CAs use Zn(II) ions at the active site, the gamma-CAs are probably Fe(II) enzymes, but they are active also with bound Zn(II) or Co(II) ions, whereas the zeta-class are cambialistic enzymes, active both with Cd(II) or Zn(II) bound within the active site
evolution
the enzyme belongs to the superfamily of metalloenzymes
evolution
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evolutionary tree of some bacterial beta-CAs among which the two Brucella suis isozymes bsCA I and bsCA II, phylogenetic analysis, overview
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evolution
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the dimeric arrangement is a peculiar feature of all bacterial alpha-CAs so far structurally characterized
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evolution
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the dimeric arrangement is a peculiar feature of all bacterial alpha-CAs so far structurally characterized
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malfunction
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isozyme CAIX expression and activity is associated with metabolic dysfunction in MDA-MB-231 cells
malfunction
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CA IV-/- mice show a 32.13% reduction in total carbonic anhydrase activity and reduced beat frequency compared to the wild-type
malfunction
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analyses of a cpb deletion mutant shows that Cpb is strictly required for growth when cultured in semi-defined medium and an atmosphere without CO2. Growth of the mutant is the same as that of the parent wild-type strain when cultured in nutrient-rich media with or without CO2 in the atmosphere, although elimination of glucose results in decreased production of acetate, propionate, and butyrate
malfunction
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at very low CO2 concentrations eCA inhibition reduces photosynthesis
malfunction
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at very low CO2 concentrations enzyme inhibition reduces photosynthesis
malfunction
enzyme complements Saccharomyces cerevisiae deletion mutant Nce103
malfunction
a CrCIA3 deletion mutant shows 50% reduction of the O2 evolution rate
malfunction
Arabidopsis thaliana mutants defective in two CA subunits show an altered photorespiratory phenotype. Mutants grown in ambient air show growth retardation compared to wild-type plants, a feature that is reversed by cultivating plants in a high-CO2 atmosphere. Under photorespiratory conditions, carbon assimilation is diminished and glycine accumulates, suggesting an imbalance with respect to photorespiration. Additionally, transcript levels of specific CA subunits are reduced in plants grown under non-photorespiratory conditions, leaves of ca2cal1 and ca2cal2 double mutants exhibited increased ROS levels. Mutants ca2cal1 and ca2cal2 show growth retardation in normal air. Mutant phenotypes, overview
malfunction
Arabidopsis thaliana mutants defective in two CA subunits show an altered photorespiratory phenotype. Mutants grown in ambient air show growth retardation compared to wild-type plants, a feature that is reversed by cultivating plants in a high-CO2 atmosphere. Under photorespiratory conditions, carbon assimilation is diminished and glycine accumulates, suggesting an imbalance with respect to photorespiration. Additionally, transcript levels of specific CA subunits are reduced in plants grown under non-photorespiratory conditions. Mutant phenotypes, overview
malfunction
loss of CAIII in soleus and tibialanterior (TA) muscles in Car3-KO mice does not change muscle mass, sarcomere protein isoform contents, mitochondrial function, and the baseline twitch and tetanic contractility as compared with age-matched wild-type controls. Car3-KO TA muscle shows faster force reduction at the beginning but higher resistance at the end during a fatigue test, followed by slower postfatigue recovery than that of wild-type TA muscle. Superfused Car3-KO soleus muscle also have faster total force reduction during fatigue test than that of wild-type soleus. It shows less elevation of resting tension followed by a better postfatigue recovery under acidotic stress. Car3-KO increases the resistance of soleus muscle to acidosis
malfunction
swimming pattern analysis of ca6 morphant and wild-type zebrafish, mutant phenotype of ca6 knockout fish, overview
malfunction
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CA IV-/- mice show a 32.13% reduction in total carbonic anhydrase activity and reduced beat frequency compared to the wild-type
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malfunction
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loss of CAIII in soleus and tibialanterior (TA) muscles in Car3-KO mice does not change muscle mass, sarcomere protein isoform contents, mitochondrial function, and the baseline twitch and tetanic contractility as compared with age-matched wild-type controls. Car3-KO TA muscle shows faster force reduction at the beginning but higher resistance at the end during a fatigue test, followed by slower postfatigue recovery than that of wild-type TA muscle. Superfused Car3-KO soleus muscle also have faster total force reduction during fatigue test than that of wild-type soleus. It shows less elevation of resting tension followed by a better postfatigue recovery under acidotic stress. Car3-KO increases the resistance of soleus muscle to acidosis
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physiological function
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beta carbonic anhydrase is required for scavenging CO2 from the ambient air
physiological function
CA IX is involved in solid tumor acidification
physiological function
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isoform CA IX is involved in tumorigenesis through many pathways, such as pH regulation and cell adhesion control
physiological function
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CAIX is a zinc metalloenzyme that catalyzes the reversible hydration of CO2. CAIX expression is strongly induced by hypoxia and is significantly associated with tumor grade and poor survival
physiological function
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isoyzme CAII is associated with the acute mountain sickness, a common disease at high altitude
physiological function
isozyme LjCAA1 is involved in nitrogen ficxation/assimilation, but may also be involved in biochemical and physiological processes not directly linked to nitrogen fixation/assimilation
physiological function
isozyme LjCAA2 is involved in nitrogen fixation/assimilation, but may also be involved in biochemical and physiological processes not directly linked to nitrogen fixation/assimilation
physiological function
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role of isozyme carbonic anhydrase IV in the bicarbonate-mediated activation of sperm, overview. Sperm respond to CO2 with an increase in beat frequency, an effect that can be inhibited by ethoxyzolamide. CA IV supplies sperm with HCO3-, which is necessary for stimulation of atypical sperm adenylyl cyclase and hence early activation of spermatozoa
physiological function
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role of isozyme carbonic anhydrase IV in the bicarbonate-mediated activation of sperm, overview. Sperm respond to CO2 with an increase in beat frequency, an effect that can be inhibited by ethoxyzolamide. CA IV supplies sperm with HCO3-, which is necessary for stimulation of atypical sperm adenylyl cyclase and hence early activation of spermatozoa
physiological function
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the enzyme from chicken has an important role in eggshell formation
physiological function
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a theoretical model predicts that homogeneous cytoplasmic distribution of CAII is more favourable for cellular transport of HCO3- and CO2 than is association of CAII with the cytoplasmic surface of the plasma membrane. Physiological interference with anion exchanger AE1 could not be demonstrated
physiological function
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carbonic anhydrase which displays significant catalytic activity in intact oocytes, also reduces the SNAT3-associated membrane conductance, when glutamine, but not when asparagine is the substrate
physiological function
CA2-like can probably take part in the increased supply of inorganic carbon (Ci) from the host clam to the symbiotic zooxanthellae when the latter conduct photosynthesis to fix Ci during light exposure
physiological function
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carbonic anhydrase (CA) is a ubiquitously expressed metalloenzyme that catalyses the hydration and dehydration reactions of carbon dioxide and bicarbonate, respectively. This basic reaction has innumerable physiological and biochemical associations and consequently CA isoforms are found in virtually all living organisms
physiological function
carbonic anhydrase (CA) plays a key role in neuronal signaling, providing bicarbonate and proton ions for GABAergic and glutamatergic neuronal function. Activation of CA isoforms expressed in neurons have been shown to have implications in the prognosis of Alzheimer's disease and dementia, while inhibitors of CAs are clinically used in the treatment of epilepsy, emphasizing the importance of this family of enzymes in both disease and normal neuronal function
physiological function
Halalkalibacterium halodurans
carbonic anhydrase is a biocatalyst that catalyzes the hydration of CO2to bicarbonate and protons, and an alkalistable and moderately thermostable alpha-carbonic anhydrase
physiological function
carbonic anhydrase VA (CAVA) is a mitochondrial enzyme that catalyzes the reversible hydration of CO2 to produce HCO3- and proton. CAVA is primarily involved in several biosynthetic processes such as ureagenesis, gluconeogenesis and lipogenesis by providing bicarbonate ion
physiological function
carbonic anhydrases are key enzymes involved in the acquisition of inorganic carbon for photosynthesis in phytoplankton, as they catalyze efficiently the interconversion between carbon dioxide and bicarbonate
physiological function
CcaA is a beta-carbonic anhydrase that is a component of the carboxysomes of a subset of beta-cyanobacteria. It has a characteristic C-terminal extension and is recruited to the carboxysome via interactions with CcmM, UniProt ID P72758, which is itself a gamma-CA homologue with enzymatic activity in many, but not all cyanobacteria. Enzyme CcaA forms a complex with CcmM with sub-picomolar affinity, with contributions from residues in CcmM's alphaA helix and CcaA's C-terminal tail. Enzyme Cca shows low activity compared to other CAs, the C-terminal tail appears to partly inhibit activity, possibly indicating a role in minimizing the activity of unencapsulated enzyme. The need for the HCO3- entering the carboxysome to be efficiently converted into CO2 requires that carbonic anhydrase is co-encapsulated within the carboxysome. On the other hand, the presence of CA activity in the cytosol is highly deleterious as it converts the accumulated HCO3- into its membrane-permeable CO2 counterpart outside of the protective barrier afforded by the shell. Intracellular CAs in cyanobacteria are required to possess interaction determinants that target them to the carboxysome, as well as mechanisms that minimize CA activity prior to the completion of the shell. CcmM is the second potential beta-carboxysomal CA and is universally present in beta-carboxysomes as it functions as a central nexus for organizing the carboxysome's interior. Formation of the CcaA/CcmM complex probably requires significant backbone movements in at least one of the binding partners. CcaA is among the least active beta-CAs characterized to date, with activity comparable with the gamma-CA, CcmM
physiological function
CcmM is itself a gamma-carbonic anhydrase homologue with enzymatic activity. It has a characteristic C-terminal extension and is recruited to the carboxysome via interactions with CcmM, which is itself a gamma-CA homologue with enzymatic activity in many, but not all cyanobacteria. Enzyme CcaA forms a complex with CcmM with sub-picomolar affinity, with contributions from residues in CcmM's alphaA helix and CcaA's C-terminal tail. CcaA is recruited to the beta-carboxysome by binding the N-terminal domain of CcmM. Enzyme Cca shows low activity compared to other CAs, the C-terminal tail appears to partly inhibit activity, possibly indicating a role in minimizing the activity of unencapsulated enzyme. The need for the HCO3- entering the carboxysome to be efficiently converted into CO2 requires that carbonic anhydrase is co-encapsulated within the carboxysome. On the other hand, the presence of CA activity in the cytosol is highly deleterious as it converts the accumulated HCO3- into its membrane-permeable CO2 counterpart outside of the protective barrier afforded by the shell. Intracellular CAs in cyanobacteria are required to possess interaction determinants that target them to the carboxysome, as well as mechanisms that minimize CA activity prior to the completion of the shell. CcmM is the second potential beta-carboxysomal CA and is universally present in beta-carboxysomes as it functions as a central nexus for organizing the carboxysome's interior. Formation of the CcaA/CcmM complex probably requires significant backbone movements in at least one of the binding partners. CcaA is among the least active beta-CAs characterized to date, with activity comparable with the gamma-CA, CcmM. CcmM is the second potential beta-carboxysomal CA and is universally present in beta-carboxysomes as it functions as a central nexus for organizing the carboxysome's interior. CcmM is built as two distinct regions, the C-terminal region of CcmM consists of three to five repeats of a RubisCO small subunit-like domain, separated by flexible linker regions, this region binds RubisCO. The N-terminal domain is clearly homologous to gamma-CAs, but in Synechocystis sp. PCC 6803, this domain lacks measurable CA activity
physiological function
expressing similar fast type of myofilament proteins, CAIII-positive tibial anterior muscle exhibits higher tolerance to fatigue than that of CAIII-negative fast twitch extensor digitorum longus muscle in in situ contractility studies
physiological function
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gamma-CAs are present in carboxysomes, being involved in photosynthesis
physiological function
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gamma-CAs are widely distributed in all three phylogenetic domains of life, playing important roles in the global carbon cycle
physiological function
gamma-CAs are widely distributed in all three phylogenetic domains of life, playing important roles in the global carbon cycle
physiological function
human carbonic anhydrase IX (hCA IX) is a tumour-associated enzyme. The observed conformational flexibility of the enzyme's extrcellular PG domain may have several important roles in tumour progression, facilitating interactions of hCA IX with partner proteins assisting tumour spreading and progression
physiological function
Hyriopsis cumingii isozyme HcCA3 play a role in the formation of shell and pearl sac formation. The mantle epithelial cell of acceptor mussels sharply divide and proliferate after being stimulated and wrap the stimulus to form pearl sac gradually. Pearl sac gradually secretes pearl essence layer by layer around stimulus and form pearl ultimately. HcCA3 expression in different parts of the mantle shows different trends during pearl formation, which suggests that it plays different roles in the process
physiological function
in metazoans, the alpha-CA family is largely represented and plays a pivotal role in the deposition of calcium carbonate biominerals
physiological function
in the green alga Chlamydomonas reinhardtii, a luminal carbonic anhydrase, CrCAH3 improves proton removal from phorosystem PSII, possibly by rapid reformation of HCO3- from CO2. It plays a direct role of CrCAH3 in the turnover efficiency of PSII, and a stimulating effect of CrCAH3 and CO2/HCO3- on PSII activity. Possible redox regulation of the enzyme, overview. Redox regulation in the chloroplast thylakoid lumen is a common way to regulate lumenal and photosynthetic proteins
physiological function
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polyhemoglobin-superoxide dismutase-catalase-carbonic anhydrase (poly-[Hb-SOD-CAT-CA]) contains all three major functions of red blood cells (RBCs) at an enhanced level. The crosslinked poly-[SFHb-SOD-CAT-CA] enzyme complex does not activate the complement pathway in rat plasma
physiological function
A0A2D1CFJ9
pufferfish CA VI is an extracellular secretory protein
physiological function
Halalkalibacterium halodurans
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
physiological function
the ctenidial DDCA is positioned to dehydrate HCO3- to CO2 in seawater, and to hydrate the CO2 that has permeated the apical membrane back to HCO3- in the cytoplasm. During insolation, the host clam needs to increase the uptake of inorganic carbon from the ambient seawater to benefit the symbiotic zooxanthellae. Only then can the symbionts conduct photosynthesis and share the photosynthates with the host. Enzyme DDCA might participate in the light-enhanced uptake and assimilation of exogenous inorganic carbon
physiological function
the Mytilus galloprovincialis alpha-CA is involved in pH regulation and/or in the delivery of bicarbonate helping the mussel during the formation of the shell
physiological function
the NADH-ubiquinone oxidoreductase complex (complex I, EC 1.6.5.3) is the main entrance site of electrons into the respiratory chain. In a variety of eukaryotic organisms, except animals and fungi (Opisthokonta), it contains an extra domain comprising trimers of putative gamma-carbonic anhydrases, named the CA domain, which has been proposed to be essential for assembly of complex I. The CA domain of plant complex I contributes to sustaining efficient photosynthesis under ambient (photorespiratory) conditions. The CA protein domain contains at least two different gamma-CA proteins, CA1 (At1g19580) and CA2 (At1g47260), which show conserved active-site regions, and two less well-conserved gamma-CA-like proteins, CAL1 (At5g63510) and CAL2 (At3g48680), containing non-conservative replacements of putatively important amino acids
physiological function
Halalkalibacterium halodurans TSLV1
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carbonic anhydrase is a biocatalyst that catalyzes the hydration of CO2to bicarbonate and protons, and an alkalistable and moderately thermostable alpha-carbonic anhydrase
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physiological function
Halalkalibacterium halodurans TSLV1 / MTCC 10961
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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
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physiological function
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role of isozyme carbonic anhydrase IV in the bicarbonate-mediated activation of sperm, overview. Sperm respond to CO2 with an increase in beat frequency, an effect that can be inhibited by ethoxyzolamide. CA IV supplies sperm with HCO3-, which is necessary for stimulation of atypical sperm adenylyl cyclase and hence early activation of spermatozoa
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physiological function
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expressing similar fast type of myofilament proteins, CAIII-positive tibial anterior muscle exhibits higher tolerance to fatigue than that of CAIII-negative fast twitch extensor digitorum longus muscle in in situ contractility studies
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physiological function
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beta carbonic anhydrase is required for scavenging CO2 from the ambient air
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physiological function
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the enzyme from chicken has an important role in eggshell formation
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physiological function
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isozyme LjCAA1 is involved in nitrogen ficxation/assimilation, but may also be involved in biochemical and physiological processes not directly linked to nitrogen fixation/assimilation
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physiological function
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isozyme LjCAA2 is involved in nitrogen fixation/assimilation, but may also be involved in biochemical and physiological processes not directly linked to nitrogen fixation/assimilation
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additional information
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EGF induces CAIX translocation to lipid rafts but not its phosphorylation
additional information
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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
additional information
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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
additional information
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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
additional information
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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
additional information
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the wide use of dithiocarbamate pesticides may be one of the factors enhancing the vulnerability of this sturgeon species to pollutants, since they act as effective carbonate dehydratase inhibitors
additional information
a disulfide bond between Cys90 and Cys258 is essential for CrCAH3 activity
additional information
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a disulfide bond between Cys90 and Cys258 is essential for CrCAH3 activity
additional information
a key role for sodium ions in increasing halotolerant enzyme stability largely through interactions with the highly ordered first Na+ hydration shell, molecular dynamics calculations, overview
additional information
CcaA is crystallized at pH 4.5 but remains in the active, type I conformation, which is typified by a salt bridge between Asp41 and Arg43 that allows the zinc ion to remain free for substrate binding. In addition, CcaA does not show the co-operative inactivation at low pH characteristic of the type II bacterial enzymes (see below), and the residues that form the non-catalytic (regulatory) bicarbonate-binding site (Arg-Trp-Tyr) are absent. CcaA is a structurally characterized bacterial beta-CA that displays type I active sites
additional information
enzyme structure, catalytic mechanism, and molecular dynamics simulations
additional information
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enzyme structure, catalytic mechanism, and molecular dynamics simulations
additional information
homology modeling of isozyme CA VI including PTX domain (residues 317-530) using the structure of human isozyme CA IV as template, PDB ID 3FE4. Structure comparisons
additional information
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homology modeling of isozyme CA VI including PTX domain (residues 317-530) using the structure of human isozyme CA IV as template, PDB ID 3FE4. Structure comparisons
additional information
A0A2D1CFJ9
homology modeling of puffer CA VI is performed using the crystal structure of human carbonic anhydrase XIV as a template structure
additional information
homology modeling of Synechocystis CcmM
additional information
identification of the structural features responsible for the high catalytic activity of the enzyme from Sulfurihydrogenibium azorense, structure comparison with the enzyme from Sulfurihydrogenibium yellowstonensis. The active site of each monomer within the dimer is completely accessible to the solvent and, as observed for other alpha-CAs, is located in a cavity which extends from the surface to the center of the protein. On the bottom of this cavity, the catalytic zinc ion is tetrahedrally coordinated by the three histidine residues (His89, His91 and His108). Enzyme SazCA active site structure and environment, important for catalytic activity, overview
additional information
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identification of the structural features responsible for the high catalytic activity of the enzyme from Sulfurihydrogenibium azorense, structure comparison with the enzyme from Sulfurihydrogenibium yellowstonensis. The active site of each monomer within the dimer is completely accessible to the solvent and, as observed for other alpha-CAs, is located in a cavity which extends from the surface to the center of the protein. On the bottom of this cavity, the catalytic zinc ion is tetrahedrally coordinated by the three histidine residues (His89, His91 and His108). Enzyme SazCA active site structure and environment, important for catalytic activity, overview
additional information
isozyme modelling and molecular dynamics studies, overview
additional information
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isozyme modelling and molecular dynamics studies, overview
additional information
residue Thr477 in PfCAdom is crucial for its catalysis
additional information
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residue Thr477 in PfCAdom is crucial for its catalysis
additional information
Halalkalibacterium halodurans
residues H137, H139, H156, and H110 present in the active site play an important role in catalysis, the active site of recombinant BhCA is also composed of conserved Glu and Asp acid residues
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
additional information
structure comparisons
additional information
structure comparisons
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
additional information
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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
additional information
the 69 amino acid residues insertion present in the active site of eta-CA PfCAdom seem to be crucial for the active site architecture
additional information
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the 69 amino acid residues insertion present in the active site of eta-CA PfCAdom seem to be crucial for the active site architecture
additional information
the CA domain of the enzyme includes 7 active site residues: His93, Gln128, His130, His132, Glu142, His155 and Thr248. Residues His130, His132, and His155 are zinc iron binding sites
additional information
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the CA domain of the enzyme includes 7 active site residues: His93, Gln128, His130, His132, Glu142, His155 and Thr248. Residues His130, His132, and His155 are zinc iron binding sites
additional information
the deduced enzyme DDCA sequence contains two distinct alpha-CA domains, each with a specific catalytic site. Each alpha-CA domain of the DDCA has its own set of catalytic and active sites. The first alpha-CA domain comprised the three histidine residues (His116, His118, His141) which coordinate the Zn2+-containing catalytic site, the hydrophobic residues (Val143, Val164, Leu224, Val233, Trp235) that form the CO2 binding pocket, and the gatekeeper residues (Glu128, Thr226). In the first alpha-CA domain, the active binding site for HCO3- and H+ constitutes five hydrophilic residues (Asn85, His87, Gln114, Thr225, and Thr226), of which His87 acts as a proton shuttle for CO2 hydration. Similarly, the Zn2+-containing catalytic site (His391, His393, His416), the hydrophobic residues that form the CO2 binding pocket (Val418, Val439, Leu504, Val513, Trp515), and the gatekeeper residues (Glu403, Thr506) are conserved in the second alpha-CA domain. Unlike the first alpha-CA domain, six hydrophilic residues (Asn361, His363, Gln366, Gln389, Thr505, and Thr506) are found in the second alpha-CA domain, and His363 serves as a proton shuttle for CO2 hydration
additional information
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the deduced enzyme DDCA sequence contains two distinct alpha-CA domains, each with a specific catalytic site. Each alpha-CA domain of the DDCA has its own set of catalytic and active sites. The first alpha-CA domain comprised the three histidine residues (His116, His118, His141) which coordinate the Zn2+-containing catalytic site, the hydrophobic residues (Val143, Val164, Leu224, Val233, Trp235) that form the CO2 binding pocket, and the gatekeeper residues (Glu128, Thr226). In the first alpha-CA domain, the active binding site for HCO3- and H+ constitutes five hydrophilic residues (Asn85, His87, Gln114, Thr225, and Thr226), of which His87 acts as a proton shuttle for CO2 hydration. Similarly, the Zn2+-containing catalytic site (His391, His393, His416), the hydrophobic residues that form the CO2 binding pocket (Val418, Val439, Leu504, Val513, Trp515), and the gatekeeper residues (Glu403, Thr506) are conserved in the second alpha-CA domain. Unlike the first alpha-CA domain, six hydrophilic residues (Asn361, His363, Gln366, Gln389, Thr505, and Thr506) are found in the second alpha-CA domain, and His363 serves as a proton shuttle for CO2 hydration
additional information
the full nucleotide sequence encoding for the native MgaCA shows an open reading frame of 255 amino acid residues containing the conserved three histidines, His94, His96, and His119 (hCA I numbering system), which coordinate the Zn(II) ion crucial for catalysis, and the two gate-keeper residues, the Glu106 and Thr199. The mussel enzyme has a residue of lysine as substituent of the proton shuttle residue His64, explaining the relatively low catalytic activity of the native MgaCA, with the following kinetic parameters for the CO2 hydration reaction
additional information
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the full nucleotide sequence encoding for the native MgaCA shows an open reading frame of 255 amino acid residues containing the conserved three histidines, His94, His96, and His119 (hCA I numbering system), which coordinate the Zn(II) ion crucial for catalysis, and the two gate-keeper residues, the Glu106 and Thr199. The mussel enzyme has a residue of lysine as substituent of the proton shuttle residue His64, explaining the relatively low catalytic activity of the native MgaCA, with the following kinetic parameters for the CO2 hydration reaction
additional information
the Mytilus galloprovincialis alpha-CA sequence contains the three His residues (His94, His96, and His119) acting as zinc ligands and the gate-keeper residues present in all alpha-CAs (Glu106 and Thr199), but has a Lys in position 64 and not a His as proton shuttling residue
additional information
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the Mytilus galloprovincialis alpha-CA sequence contains the three His residues (His94, His96, and His119) acting as zinc ligands and the gate-keeper residues present in all alpha-CAs (Glu106 and Thr199), but has a Lys in position 64 and not a His as proton shuttling residue
additional information
the polypeptide segment Val131-Asp136 in CA IV arranges in an extended loop conformation rich of charged residues extending to the outside
additional information
the polypeptide segment Val131-Asp136 in CA IV arranges in an extended loop conformation rich of charged residues extending to the outside
additional information
the polypeptide segment Val131-Asp136 in CA IV arranges in an extended loop conformation rich of charged residues extending to the outside
additional information
the polypeptide segment Val131-Asp136 in CA IV arranges in an extended loop conformation rich of charged residues extending to the outside
additional information
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the polypeptide segment Val131-Asp136 in CA IV arranges in an extended loop conformation rich of charged residues extending to the outside
additional information
the residues essential for CA2 catalytic activity are highly conserved, and also the hydrophobic portion of the CA2 active site (Val129, Val150, Leu209, Val218 and Trp220) and responsible for binding the substrate CO2 are fully conserved, active site structure
additional information
the TcruCA monomer has the signature secondary structure typical of an alpha-CA fold, with helical and loop structures present towards the surface and a conical active-site cavity comprised of mostly beta-structure, structure comparisons, especially with human carbonic anhydrase 2, CA2, overview
additional information
three histidine residues predicted to form the Zn2+ coordination center, H233, H235, and H258, are conserved in Pl-CAN, together with four additional sites, H206, Q231, E245, and T340
additional information
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three histidine residues predicted to form the Zn2+ coordination center, H233, H235, and H258, are conserved in Pl-CAN, together with four additional sites, H206, Q231, E245, and T340
additional information
Halalkalibacterium halodurans TSLV1
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residues H137, H139, H156, and H110 present in the active site play an important role in catalysis, the active site of recombinant BhCA is also composed of conserved Glu and Asp acid residues
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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
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the TcruCA monomer has the signature secondary structure typical of an alpha-CA fold, with helical and loop structures present towards the surface and a conical active-site cavity comprised of mostly beta-structure, structure comparisons, especially with human carbonic anhydrase 2, CA2, overview
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identification of the structural features responsible for the high catalytic activity of the enzyme from Sulfurihydrogenibium azorense, structure comparison with the enzyme from Sulfurihydrogenibium yellowstonensis. The active site of each monomer within the dimer is completely accessible to the solvent and, as observed for other alpha-CAs, is located in a cavity which extends from the surface to the center of the protein. On the bottom of this cavity, the catalytic zinc ion is tetrahedrally coordinated by the three histidine residues (His89, His91 and His108). Enzyme SazCA active site structure and environment, important for catalytic activity, overview
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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
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