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231225s2021 xx |||||o 00| ||eng c |
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|a 10.1016/j.plaphy.2021.09.041
|2 doi
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|a pubmed24n1106.xml
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|a (DE-627)NLM331897512
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|a (NLM)34649025
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|a (PII)S0981-9428(21)00506-4
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|a DE-627
|b ger
|c DE-627
|e rakwb
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|a eng
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|a Kumar, Sachin
|e verfasserin
|4 aut
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|a Site-directed mutagenesis (P61G) of copper, zinc superoxide dismutase enhances its kinetic properties and tolerance to inactivation by H2O2
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|c 2021
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|a Text
|b txt
|2 rdacontent
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|a ƒaComputermedien
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|2 rdamedia
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|a ƒa Online-Ressource
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|2 rdacarrier
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|a Date Completed 10.12.2021
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|a Date Revised 14.12.2021
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|a published: Print-Electronic
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|a Citation Status MEDLINE
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|a Copyright © 2021 Elsevier Masson SAS. All rights reserved.
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|a Superoxide dismutases (SODs) protect the cells by catalyzing the dismutation of harmful superoxide radicals (O2•-) into molecular oxygen (O2) and hydrogen peroxide (H2O2). Here, a Cu, Zn SOD (WT) from a high altitude plant (Potentilla atrosanguinea) was engineered by substituting a conserved residue proline to glycine at position 61 (P61G). The computational analysis showed higher structural flexibility and clusters in P61G than WT. The P61G exhibited moderately higher catalytic efficiency (Km = 0.029 μM, Vmax = 1488) than WT protein (Km = 0.038 μM, Vmax = 1290.11). P61G showed higher thermostability as revealed from residual activity (72.25% for P61G than 59.31% for WT after heating at 80 °C for 60 min), differential calorimetry scanning and CD-spectroscopic analysis. Interestingly, the P61G mutation also resulted in enhanced tolerance to H2O2 inactivation than WT protein. The finding on enhancing the biophysico-chemical properties by mutating conserved residue could stand as an example to engineer other enzymes. Also, the reported mutant can be exploited in food and pharmaceutical industries
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|a Journal Article
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|a And H(2)O(2) tolerance
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|a Molecular docking
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|a Molecular dynamics simulations
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|a Site-directed mutagenesis
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|a Superoxide dismutase
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|a Copper
|2 NLM
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|a 789U1901C5
|2 NLM
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|a Hydrogen Peroxide
|2 NLM
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|a BBX060AN9V
|2 NLM
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| 650 |
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|a Superoxide Dismutase
|2 NLM
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| 650 |
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|a EC 1.15.1.1
|2 NLM
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| 650 |
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|a Zinc
|2 NLM
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| 650 |
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|a J41CSQ7QDS
|2 NLM
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| 700 |
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|a Bhardwaj, Vijay Kumar
|e verfasserin
|4 aut
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|a Kaachra, Anish
|e verfasserin
|4 aut
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|a Guleria, Shweta
|e verfasserin
|4 aut
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|a Kumar, Arun
|e verfasserin
|4 aut
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|a Purohit, Rituraj
|e verfasserin
|4 aut
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|a Kumar, Sanjay
|e verfasserin
|4 aut
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| 773 |
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|i Enthalten in
|t Plant physiology and biochemistry : PPB
|d 1991
|g 168(2021) vom: 15. Nov., Seite 221-229
|w (DE-627)NLM098178261
|x 1873-2690
|7 nnns
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| 773 |
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|g volume:168
|g year:2021
|g day:15
|g month:11
|g pages:221-229
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|u http://dx.doi.org/10.1016/j.plaphy.2021.09.041
|3 Volltext
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|d 168
|j 2021
|b 15
|c 11
|h 221-229
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