Carbonic anhydrase - a universal enzyme of the carbon-based life

Kupriyanova, Elena V.; Пронина, Н. А.; Los, Dmitry A.

doi:10.1007/s11099-017-0685-4

Cited by 41 publications

(31 citation statements)

References 116 publications

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“…Carbonic anhydrase (CA, E.C. 4.2.1.1), a zinc metalloenzyme, can efficiently catalyze the reversible hydration of CO 2 to bicarbonate ion [1,2]. In nature, chemical fixation of CO 2 usually requires high temperatures, high pressure and long reaction times, while carbonic anhydrase can fix carbon dioxide and have a high reaction rate under low pressure conditions [3].…”

Section: Introductionmentioning

confidence: 99%

Fast Immobilization of Human Carbonic Anhydrase II on Ni-Based Metal-Organic Framework Nanorods with High Catalytic Performance

Jiao

Sun

et al. 2020

Catalysts

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Carbonic anhydrase (CA) has received considerable attention for its ability to capture carbon dioxide efficiently. This study reports a simple strategy for immobilizing recombinant carbonic anhydrase II from human (hCA II) on Ni-based MOFs (Ni-BTC) nanorods, which was readily achieved in a one-pot immobilization of His-tagged hCA II (His-hCA II). Consequently, His-hCA II from cell lysate could obtain an activity recovery of 99% under optimal conditions. After storing for 10 days, the immobilized His-hCA II maintained 40% activity while the free enzyme lost 91% activity. Furthermore, during the hydrolysis of p-nitrophenyl acetic acid, immobilized His-hCA II exhibited excellent reusability and still retained more than 65% of the original activity after eight cycles. In addition, we also found that Ni-BTC had no fixation effect on proteins without histidine-tag. These results show that the Ni-BTC MOFs have a great potential with high efficiency for and specific binding of immobilized enzymes.

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Section: Introductionmentioning

confidence: 99%

Fast Immobilization of Human Carbonic Anhydrase II on Ni-Based Metal-Organic Framework Nanorods with High Catalytic Performance

Jiao

Sun

et al. 2020

Catalysts

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“…The interconversion between CO 2 and HCO 3 − is fundamental for the successful flow of biochemical processes in all living cells [ 1 ]. Metabolic conversion is ensured by the hydration of carbonic anhydride which leads to the corresponding soluble ion, bicarbonate, and the release of a proton [ 2 , 3 ].…”

Section: Introductionmentioning

confidence: 99%

“…Due to the high number of physiological process in which these chemical species are essential, the optimal balance between them is vital for all life forms [ 2 , 4 , 5 , 6 , 7 ]. This equilibrium is regulated by a superfamily of metalloenzyme, the carbonic anhydrases (CAs, EC 4.2.1.1) [ 1 ]. By accelerating this normally slow reaction [ 8 ], CAs fulfil the metabolic needs connected to CO 2 /bicarbonate and protons [ 2 , 4 , 6 ].…”

Section: Introductionmentioning

confidence: 99%

Amino Acids as Building Blocks for Carbonic Anhydrase Inhibitors

et al. 2018

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Carbonic anhydrases (CAs) are a superfamily of metalloenzymes widespread in all life, classified into seven genetically different families (α–θ). These enzymes catalyse the reversible hydration of carbonic anhydride (CO2), generating bicarbonate (HCO3−) and protons (H+). Fifteen isoforms of human CA (hCA I–XV) have been isolated, their presence being fundamental for the regulation of many physiological processes. In addition, overexpression of some isoforms has been associated with the outbreak or progression of several diseases. For this reason, for a long time CA inhibitors (CAIs) have been used in the control of glaucoma and as diuretics. Furthermore, the search for new potential CAIs for other pharmacological applications is a very active field. Amino acids constitute the smallest fundamental monomers of protein and, due to their useful bivalent chemical properties, are widely used in organic chemistry. Both proteinogenic and non-proteinogenic amino acids have been extensively used to synthesize CAIs. This article provides an overview of the different strategies that have been used to design new CAIs containing amino acids, and how these bivalent molecules influence the properties of the inhibitors.

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“…In addition, most chloroplast-located proteins are synthesized in the ER and then transported to the chloroplast through the secretory pathway. CAH1, alpha-type carbonic anhydrase (EC 4.2.1.1), is one of the few plant proteins known to be targeted to the chloroplast, and which is essential for efficient photosynthesis (Samuelsson and Karlsson 2001, Burén et al 2011, Kupriyanova et al 2017. The mature CAH1 harboring multiple glycoforms of N-glycans (Burén et al 2011) might be a good substrate to study the relation between N-glycosylation and photosynthesis.…”

Section: Introductionmentioning

confidence: 99%

N-glycosylation regulates photosynthetic efficiency of Arabidopsis thaliana

Jiao¹,

Niu²,

Wang³

et al. 2020

Photosynt.

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N-glycosylation is one of the most important protein modifications in eukaryotes. It has been well established that N-glycosylation plays multiple roles in regulating stress tolerance of plants. However, the effects and mechanism of N-glycosylation on photosynthesis have not been well understood. In the present study, an obvious decrease in photosynthetic capacity and dry mass were detected in alg3-3 and cgl1-1, two typical mutants in N-glycosylation process. The maximal photochemical efficiency of PSII decreased significantly in cgl1-1. The values of effective quantum yield of PSII photochemistry, rate of photosynthetic electron transport through PSII, and photochemical quenching coefficient, which reflected the photochemical efficiency of plants, decreased as well, while the values of quantum yield of nonregulated energy dissipation of PSII showed obvious enhancement, the similar tendency was also observed in alg3-3. Furthermore, we found that N-glycosylation was also required to maintain the stability of a chloroplast-located protein CAH1, which was closely related to photosynthesis. These results suggest that N-glycosylation plays crucial roles in maintaining photosynthetic efficiency.

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Carbonic anhydrase - a universal enzyme of the carbon-based life

Cited by 41 publications

References 116 publications

Fast Immobilization of Human Carbonic Anhydrase II on Ni-Based Metal-Organic Framework Nanorods with High Catalytic Performance

Fast Immobilization of Human Carbonic Anhydrase II on Ni-Based Metal-Organic Framework Nanorods with High Catalytic Performance

Amino Acids as Building Blocks for Carbonic Anhydrase Inhibitors

N-glycosylation regulates photosynthetic efficiency of Arabidopsis thaliana

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