Molecular evolution and selection pressure in alpha-class carbonic anhydrase family members

McDevitt, Meghan E.; Lambert, Lisa A.

doi:10.1016/j.bbapap.2011.07.007

Cited by 7 publications

(7 citation statements)

References 73 publications

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“…According to evolutionary studies, CA‐II appeared first than CA‐VI, which possibly emerged due to an initial duplication that occurred around the origin of the animal kingdom . The active site of CA‐II shows some degree of conservation, although positive selection was detected in some histidine residues . In CA‐VI there is also conservation of those segments and the small variability noticed seems to have no effect on its catalytic activity .…”

Section: Discussionmentioning

confidence: 99%

“…The active site of CA‐II shows some degree of conservation, although positive selection was detected in some histidine residues . In CA‐VI there is also conservation of those segments and the small variability noticed seems to have no effect on its catalytic activity . Furthermore, in CA‐VI there are other conserved segments that were pointed as possible candidates for protein interfaces as, for example, a binding site to the enamel surface .…”

Section: Discussionmentioning

confidence: 99%

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Cross-species comparison of mammalian saliva using an LC-MALDI based proteomic approach

Sousa-Pereira

Cova

Abrantes³

et al. 2015

Proteomics

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Despite the importance of saliva in the regulation of oral cavity homeostasis, few studies have been conducted to quantitatively compare the saliva of different mammal species. Aiming to define a proteome signature of mammals' saliva, an in-depth SDS-PAGE-LC coupled to MS/MS (GeLC-MS/MS) approach was used to characterize the saliva from primates (human), carnivores (dog), glires (rat and rabbit), and ungulates (sheep, cattle, horse). Despite the high variability in the number of distinct proteins identified per species, most protein families were shared by the mammals studied with the exception of cattle and horse. Alpha-amylase is an example that seems to reflect the natural selection related to digestion efficacy and food recognition. Casein protein family was identified in all species but human, suggesting an alternative to statherin in the protection of hard tissues. Overall, data suggest that different proteins might assure a similar role in the regulation of oral cavity homeostasis, potentially explaining the specific mammals' salivary proteome signature. Moreover, some protein families were identified for the first time in the saliva of some species, the presence of proline-rich proteins in rabbit's saliva being a good example.

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Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

Cross-species comparison of mammalian saliva using an LC-MALDI based proteomic approach

Sousa-Pereira

Cova

Abrantes³

et al. 2015

Proteomics

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“…Carbonic anhydrases (CAs) form a superfamily of mostly zinc-binding metalloenzymes that catalyze, by approximately one million fold [ 1 ], the interconversion of carbon dioxide and bicarbonate: . These enzymes are a critical component of the acid-base balance and play roles in numerous biological functions [ 2 ].…”

Section: Introductionmentioning

confidence: 99%

Carbonic Anhydrases in Cnidarians: Novel Perspectives from the Octocorallian Corallium rubrum

et al. 2016

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Although the ability to elaborate calcium carbonate biominerals was apparently gained independently during animal evolution, members of the alpha carbonic anhydrases (α-CAs) family, which catalyze the interconversion of CO2 into HCO3-, are involved in the biomineralization process across metazoans. In the Mediterranean red coral Corallium rubrum, inhibition studies suggest an essential role of CAs in the synthesis of two biominerals produced in this octocoral, the axial skeleton and the sclerites. Hitherto no molecular characterization of these enzymes was available. In the present study we determined the complete set of α-CAs in C. rubrum by data mining the genome and transcriptome, and measured their differential gene expression between calcifying and non-calcifying tissues. We identified six isozymes (CruCA1-6), one cytosolic and five secreted/membrane-bound among which one lacked two of the three zinc-binding histidines and was so referred to as a carbonic anhydrase related protein (CARP). One secreted isozyme (CruCA4) showed specific expression both by qPCR and western-blot in the calcifying tissues, suggesting its involvement in biomineralization. Moreover, phylogenetic analyses of α-CAs, identified in six representative cnidarians with complete genome, support an independent recruitment of α-CAs for biomineralization within anthozoans. Finally, characterization of cnidarian CARPs highlighted two families: the monophyletic cytosolic CARPs, and the polyphyletic secreted CARPs harboring a cnidarian specific cysteine disulfide bridge. Alignment of the cytosolic CARPs revealed an evolutionary conserved R-H-Q motif in place of the characteristic zinc-binding H-H-H necessary for the catalytic function of α-CAs.

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“…The spontaneous reaction of CO 2 with water can produce bicarbonate HCO − 3 + H + , but that reaction is too slow to support respiration [93,94] and other biological processes catalyzed by different CAs. Eight unrelated families of carbonic anhydrase (CA) enzymes represent different ways nature performed the feat of fast catalytic interconversion between carbon dioxide and carbonic oxide [95], reaching the catalytic turnover of 1 µs −1 or even higher [96]. There is little or no sequence homology among the CA families α, β, γ, δ, ζ, η, θ, and ι [91,97].…”

Section: Ca I Ca Ii and Ca Ii-t200h (Also Four-state Enzymes)mentioning

confidence: 99%

“…There is little or no sequence homology among the CA families α, β, γ, δ, ζ, η, θ, and ι [91,97]. Molecular biologists concluded that convergent biological evolution performed the spectacular function-enhancing feat at least seven times, because different CAs evolved to perform an identical function [95,98,99].…”

Section: Ca I Ca Ii and Ca Ii-t200h (Also Four-state Enzymes)mentioning

confidence: 99%

Theoretical Improvements in Enzyme Efficiency Associated with Noisy Rate Constants and Increased Dissipation

Juretić,

Bonačić Lošić

2024

Entropy

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Previous studies have revealed the extraordinarily large catalytic efficiency of some enzymes. High catalytic proficiency is an essential accomplishment of biological evolution. Natural selection led to the increased turnover number, kcat, and enzyme efficiency, kcat/KM, of uni–uni enzymes, which convert a single substrate into a single product. We added or multiplied random noise with chosen rate constants to explore the correlation between dissipation and catalytic efficiency for ten enzymes: beta-galactosidase, glucose isomerase, β-lactamases from three bacterial strains, ketosteroid isomerase, triosephosphate isomerase, and carbonic anhydrase I, II, and T200H. Our results highlight the role of biological evolution in accelerating thermodynamic evolution. The catalytic performance of these enzymes is proportional to overall entropy production—the main parameter from irreversible thermodynamics. That parameter is also proportional to the evolutionary distance of β-lactamases PC1, RTEM, and Lac-1 when natural or artificial evolution produces the optimal or maximal possible catalytic efficiency. De novo enzyme design and attempts to speed up the rate-limiting catalytic steps may profit from the described connection between kinetics and thermodynamics.

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Molecular evolution and selection pressure in alpha-class carbonic anhydrase family members

Cited by 7 publications

References 73 publications

Cross-species comparison of mammalian saliva using an LC-MALDI based proteomic approach

Cross-species comparison of mammalian saliva using an LC-MALDI based proteomic approach

Carbonic Anhydrases in Cnidarians: Novel Perspectives from the Octocorallian Corallium rubrum

Theoretical Improvements in Enzyme Efficiency Associated with Noisy Rate Constants and Increased Dissipation

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