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231225s2021 xx |||||o 00| ||eng c |
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|a 10.1016/j.jplph.2020.153337
|2 doi
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|a pubmed25n1066.xml
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|a (DE-627)NLM319853586
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|a (NLM)33421837
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|a (PII)S0176-1617(20)30227-3
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|a DE-627
|b ger
|c DE-627
|e rakwb
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|a eng
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| 100 |
1 |
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|a Ślesak, Ireneusz
|e verfasserin
|4 aut
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|a The activity of RubisCO and energy demands for its biosynthesis. Comparative studies with CO2-reductases
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|c 2021
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|a Text
|b txt
|2 rdacontent
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|a ƒaComputermedien
|b c
|2 rdamedia
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|a ƒa Online-Ressource
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|2 rdacarrier
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|a Date Completed 27.05.2021
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|a Date Revised 27.05.2021
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|a published: Print-Electronic
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|a Citation Status MEDLINE
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|a Copyright © 2020 Elsevier GmbH. All rights reserved.
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|a Most CO2 on Earth is fixed into organic matter via reactions catalysed by enzymes called carboxylases. CO2-fixation via carboxylases occurs in the Calvin-Benson-Bassham (CBB) cycle, and the crucial role in this cycle is played by RubisCO (D-ribulose 1,5-bisphosphate carboxylase/oxygenase). CO2 can also be fixed by pathways, where a reduction of CO2 to formate or carbon monoxide (CO) occurs. The latter reactions are performed by so-called CO2-reductases e.g. formate dehydrogenase (FDH), carbon-monooxide (CO) dehydrogenase (CODH), and crotonyl-CoA reductase/carboxylase (CCR). In general, a simple model of enzymatic activity based only on a turnover rate of an enzyme for an appropriate substrate (kcat) is insufficient. Based on estimated metabolic costs of each amino acid, the average energetic costs of amino acid biosynthesis (Eaa), and the total costs (ET) for selected CO2-fixing enzymes were analyzed concerning 1) kcat for CO2 (kC), and 2) specificity factor (Srel) for RubisCO. A comparison of Eaa and ET to their kC showed that CODH and FDHs do not need to be more efficient enzymes in CO2 capturing pathways than some forms of RubisCO. CCR was the only both low-cost and highly active CO2-fixing enzyme. The obtained results showed also that there exists an evolutionarily conserved trade-off between Srel of RubisCOs and the energetic demands needed for their biosynthesis. Phylogenetic analysis demonstrated that RubisCO, CODH, FDH, and CCR are enzymes formed as a result of parallel evolution. Moreover, the kinetic parameters (kC) of CO2-fixing enzymes were plausibly optimized already at the early stages of life evolution on Earth
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|a Comparative Study
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|a Journal Article
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|a 16S rRNA phylogeny
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|a Convergent evolution
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|a Crotonyl-CoA carboxylases/reductases
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|a Ethylmalonyl-CoA pathway
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| 650 |
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|a Pareto optimization
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|a Photosynthesis
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|a Carbon Dioxide
|2 NLM
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|a 142M471B3J
|2 NLM
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|a Oxidoreductases
|2 NLM
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|a EC 1.-
|2 NLM
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| 650 |
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|a Ribulose-Bisphosphate Carboxylase
|2 NLM
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| 650 |
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|a EC 4.1.1.39
|2 NLM
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| 700 |
1 |
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|a Ślesak, Halina
|e verfasserin
|4 aut
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| 773 |
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|i Enthalten in
|t Journal of plant physiology
|d 1979
|g 257(2021) vom: 15. Feb., Seite 153337
|w (DE-627)NLM098174622
|x 1618-1328
|7 nnas
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| 773 |
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|g volume:257
|g year:2021
|g day:15
|g month:02
|g pages:153337
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|u http://dx.doi.org/10.1016/j.jplph.2020.153337
|3 Volltext
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|d 257
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|h 153337
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