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E12Q
superoxide dismutase activity shows a 29% increase in activity relative to activity of the wild-type enzyme
E12V
superoxide dismutase activity shows a 47% increase in activity relative to activity of the wild-type enzyme
A16V
naturally occuring ala16val polymorphism genotyping, overview
A4V
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mutation causing familial amyotrophic lateral scerosis, 30% of wild-type activity, 1.06 atoms of copper and 1.43 atoms of zinc per subunit
C111S
site-directed mutagenesis, the mutant has 1.07 copper and 1.18 zinc per subunit
C140S
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catalytic efficiency similar to wild-type, product inhibition is less than in wild-type
C140S/Q143A
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catalysis does not follow Michaelis-Menten kinetics, substrate inhibition with KI-value of 0.06 mM
D124N
site-directed mutagenesis, the mutant has 0.93 copper and 0.03 zinc per subunit
D124N/C111S
site-directed mutagenesis, the mutant has 0.93 copper and 0.03 zinc per subunit
D83S
site-directed mutagenesis, the mutant has 0.93 copper and 0.08 zinc per subunit
D83S/C111S
site-directed mutagenesis, the mutant has 0.93 copper and 0.08 zinc per subunit
E100G
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an amyotrophic lateral sclerosis-associated naturally occuring SOD mutant, misfolding/aggregation mechanism with folding and unfolding kinetics, overview
E93A
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construction of transgenic mice overexpressing wild-type and mutant SOD1, biochemical changes occur in the hindlimb muscle of young, presymptomatic G93A hSOD1 transgenic mice, cdk5 activity is reduced in hindlimb muscle of 27-day-old G93A hSOD1 transgenic mice by suppression through the mutant E93A enzyme, phenotype, overview, mutant G93A SOD1 also suppresses muscle cdk5 activity in vitro
F50E/G51E
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about 20% of wild-type activity, monomeric
F66A
site-directed mutagenesis, alteration of the active site surrounding, the mutant is 3fold less sensitive to product inhibition compared to the wild-type enzyme
F66L
site-directed mutagenesis, alteration of the active site surrounding, the mutant shows residual product inhibition with formation of a peroxide-inhibited enzyme and increased catalytic activity
G41N
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Cu,Zn-SOD, site-directed mutagenesis, analogous to mutant found in familial amyotrophic lateral sclerosis, 47% activity compared to the wild-type
G93R
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an amyotrophic lateral sclerosis-associated naturally occuring SOD mutant, misfolding/aggregation mechanism with folding and unfolding kinetics, overview
H46R
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an amyotrophic lateral sclerosis-associated naturally occuring SOD mutant, misfolding/aggregation mechanism with folding and unfolding kinetics, overview
H63C
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Cu,Zn-SOD, mutant with exchange of metal-bridging proton-donor His63 for Cys, binds Cu2+, but not Zn2+, 1% remaining activity compared to wild-type
H80S/D83S
site-directed mutagenesis, the mutant has 0.93 copper and 0.08 zinc per subunit
H80S/D83S/C6A/C111S
site-directed mutagenesis, the mutant has 1.07 copper and 1.18 zinc per subunit
N73S
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ratio kcat/Km about twofold smaller than in wild-type, product inhibition similar to wild-type
N73S/C140S/Q143A
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catalytic efficiency much smaller than wild-type, no appreciable product inhibition
N73S/Q143A
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catalytic efficiency much smaller than wild-type, no appreciable product inhibition
Q143A
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dramatically reduced product inhibition, reduced catalytic activity and efficiency
Y34F
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about 12fold decrease in kcat value
D90A
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Cu,Zn-SOD, mutant found in familial amyotrophic lateral sclerosis, activity similar compared to native and recombinant wild-type, but enhanced OH- generating activity, mutant is more sensitive to inhibition by copper-chelators
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G41N
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Cu,Zn-SOD, site-directed mutagenesis, analogous to mutant found in familial amyotrophic lateral sclerosis, 47% activity compared to the wild-type
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G85R
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Cu,Zn-SOD, site-directed mutagenesis, analogous to mutant found in familial amyotrophic lateral sclerosis, 99% activity compared to the wild-type
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H43R
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Cu,Zn-SOD, site-directed mutagenesis, analogous to mutant found in familial amyotrophic lateral sclerosis, 66% activity compared to the wild-type
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H63C
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Cu,Zn-SOD, mutant with exchange of metal-bridging proton-donor His63 for Cys, binds Cu2+, but not Zn2+, 1% remaining activity compared to wild-type
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G93A
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site-directed mutagenesis
H155Q
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site-directed mutagenesis, the mutant shows a a slightly lower iron content, reduced heat stability, and a 2fold reduced activity compared to the wild-type enzyme
Y41F
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site-directed mutagenesis, the mutant shows a a slightly lower iron content and a 17fold reduced activity compared to the wild-type enzyme, the mutant shows an uninterrupted hydrogen bond network
Y88F
site-directed mutagenesis, substitution of Tyr88 to Phe does not affect the metal specificity of the enzyme
H30A
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active site mutant, site-directed mutagenesis, activity, sensitivity to heat and inhibitors unchanged compared to wild-type
K170R
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active site mutant, site-directed mutagenesis, unchanged activity, decreased thermal stability, more stable to 2,4,6-trinotrobenzenesulfonate than the wild-type, completely inactivated by phenylglyoxal
H30A
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active site mutant, site-directed mutagenesis, activity, sensitivity to heat and inhibitors unchanged compared to wild-type
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K170R
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active site mutant, site-directed mutagenesis, unchanged activity, decreased thermal stability, more stable to 2,4,6-trinotrobenzenesulfonate than the wild-type, completely inactivated by phenylglyoxal
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H171A
site-directed mutagenesis, the mutation changes the metal-binding specificity of the mutant enzyme from Mn to Fe. The alpha-helix content of mutant His171Ala is 59% suggesting that the mutant folds with a reasonable secondary structure. Mutant His171Ala exhibits a 39.6% higher activity than the wild-type. Mutant His171Ala is a Fe-SOD with Zn, Ni,and Fe contents of 180, 77, and 530 ng/mg, respectively. Mutant His171Ala exhibits a specific activity 39.6% higher than that of the wild type enzyme
H29A
site-directed mutagenesis, the mutation changes the metal-binding specificity of the mutant enzyme from Mn to Fe. The alpha-helix content of mutant His29Ala is 66% , suggesting that the mutant folds with a reasonable secondary structure. Mutant His29Ala shows an activity comparable to that of the wild-type. Zn, Ni, and Fe contents of the His29Ala enzyme mutant are 180, 76, and 300 ng/mg, respectively, and the amount of Fe is almost twice that of Zn and fourtimes that of Ni, suggesting that His29Ala mainly is a Fe-SOD. The mutant exhibits a specific activity comparable to that of the wild-type enzyme
H84A
site-directed mutagenesis, the mutant exhibits a specific activity comparable to that of the wild-type enzyme
P143S/P145L
site-directed mutagenesis, gain-of-function, the mutant shows increased activirty compared to the wild-type SOD1
P143S/P145L
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site-directed mutagenesis, gain-of-function, the mutant shows increased activirty compared to the wild-type SOD1
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Y34F
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the mutant shows metalcofactor kinetics similar to the human not the Deinococcus radiodurans Mn-SOD, formation of human-like Mn3+SOD and human-like Mn3+SOD-O2 - adduct, overview
Y34F
unlike wild-type, F- binding is retained at high pH-values. N3- inhibitis Y34F with a 20fold lower KI-value than for wild-type
D90A
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Cu,Zn-SOD, mutant found in familial amyotrophic lateral sclerosis, activity similar compared to native and recombinant wild-type, but enhanced OH- generating activity, mutant is more sensitive to inhibition by copper-chelators
D90A
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mutant related to amyothrophic lateral sclerosis, improvement of expression by coexpression with yeast copper chaperone
G85R
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Cu,Zn-SOD, site-directed mutagenesis, analogous to mutant found in familial amyotrophic lateral sclerosis, 99% activity compared to the wild-type
G85R
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an amyotrophic lateral sclerosis-associated naturally occuring SOD mutant, misfolding/aggregation mechanism with folding and unfolding kinetics, overview
G93A
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mutant related to amyothrophic lateral sclerosis, improvement of expression by coexpression with yeast copper chaperone
G93A
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an amyotrophic lateral sclerosis-associated naturally occuring SOD mutant, misfolding/aggregation mechanism with folding and unfolding kinetics, overview
G93A
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naturally occuring mutation, mutant SOD1-induced cytotoxicity protection
H43R
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Cu,Zn-SOD, site-directed mutagenesis, analogous to mutant found in familial amyotrophic lateral sclerosis, 66% activity compared to the wild-type
H43R
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mutation causing familial amyotrophic lateral scerosis, 59% of wild-type activity, 1.4 atoms of copper and 1.11 atoms of zinc per subunit
R213G
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site-directed mutagenesis, mutant mice with R213G knock-in mutation, a human single nucleotide polymorphism leading to reduced binding EcSOD in peripheral organs, exacerbate the organ damages. Phenotype, overview
R213G
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site-directed mutagenesis, mutant mice with R213G knock-in mutation, a human single nucleotide polymorphism leading to reduced binding EcSOD in peripheral organs, exacerbate the organ damages. Phenotype, overview
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additional information
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generation of a highly thermostable and stress tolerant superoxide dismutase by N-terminal modification and metal incorporation engineering. Recombinant wild-type enzyme SODAp and NTD-fused N-terminal domain ntdSODAp are incorporated with metal cofactors by two ways: the Fe2+- and Mn2+-contained SODs are obtained by in vivo modification (Mn-med SODAp and ntdSODAp) and in vitro reconstitution (Mn-rec SODAp and ntdSODAp), respectively
additional information
construction of two mutant strains KO1 and KOS, lacking either sodA-1 or both sodA-1 and sodA-2, through homologous recombination
additional information
construction of two mutant strains KO1 and KOS, lacking either sodA-1 or both sodA-1 and sodA-2, through homologous recombination
additional information
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construction of two mutant strains KO1 and KOS, lacking either sodA-1 or both sodA-1 and sodA-2, through homologous recombination
additional information
construction of two mutant strains KO2 and KOS, lacking either sodA-2 or both sodA-1 and sodA-2, through homologous recombination
additional information
construction of two mutant strains KO2 and KOS, lacking either sodA-2 or both sodA-1 and sodA-2, through homologous recombination
additional information
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construction of two mutant strains KO2 and KOS, lacking either sodA-2 or both sodA-1 and sodA-2, through homologous recombination
additional information
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construction of two mutant strains KO2 and KOS, lacking either sodA-2 or both sodA-1 and sodA-2, through homologous recombination
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additional information
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construction of two mutant strains KO1 and KOS, lacking either sodA-1 or both sodA-1 and sodA-2, through homologous recombination
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additional information
construction of a chimeric SOD1 mutant fused to Saccharomyces cerevisiae superoxide dismutase 1 copper chaperone-fusion enzyme, Lys7, the chimeric mutant SOD1-Lys7 shows increased activirty compared to the wild-type SOD1 and SOD1 mutant P143S/P145L
additional information
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construction of a chimeric SOD1 mutant fused to Saccharomyces cerevisiae superoxide dismutase 1 copper chaperone-fusion enzyme, Lys7, the chimeric mutant SOD1-Lys7 shows increased activirty compared to the wild-type SOD1 and SOD1 mutant P143S/P145L
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additional information
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chemical modification of the enzyme with linoleic and alpha-linolenic acids using two different methods leads to higher retained enzymatic activity compared with SOD modified by macromolecular substances. Enhanced heat stability, acid and alkali resistance, and anti-pepsin/trypsin ability of the modified SOD are observed and compared to those of the natural enzyme, the apparent oil-water partition coefficient of the modified enzyme is especially increased, overview
additional information
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enzyme null mutant cell is not sensitive to H2O2, 3-morpholinosydnonimine, or paraquat challenge, but is killed by exogenous superoxide generated by the xanthine/xanthine oxidase method
additional information
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construction of a sodC null mutant strain KEK1, which is not sensitive to a H2O2, 3-morpholinosydnonimine, or paraquat challenge, but is killed by exogenous superoxide generated by the xanthine/xanthine oxidase method. The sodC mutant also exhibits a growth defect in liquid medium compared to the parental strain, which can be complemented in trans. The mutant organism is killed more rapidly than the parental strain in murine macrophage-like cell line RAW 264.7, but killing is eliminated when macrophages are treated with an NADPH oxidase inhibitor, overview
additional information
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enzyme null mutant cell is not sensitive to H2O2, 3-morpholinosydnonimine, or paraquat challenge, but is killed by exogenous superoxide generated by the xanthine/xanthine oxidase method
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additional information
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construction of a sodC null mutant strain KEK1, which is not sensitive to a H2O2, 3-morpholinosydnonimine, or paraquat challenge, but is killed by exogenous superoxide generated by the xanthine/xanthine oxidase method. The sodC mutant also exhibits a growth defect in liquid medium compared to the parental strain, which can be complemented in trans. The mutant organism is killed more rapidly than the parental strain in murine macrophage-like cell line RAW 264.7, but killing is eliminated when macrophages are treated with an NADPH oxidase inhibitor, overview
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additional information
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Cu,Zn-enzyme disruption mutant, no Cu,Zn-dependent activity, increase in Fe-dependent activity by 30-40%. Under illuminated conditions, 60% reduction of cell survival rate compared to wild type
additional information
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strains with mutations in the enzyme gene SOD2 exhibit increased susceptibility to oxidative stress as well as poor growth at elevated temperature
additional information
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naturally occuring hybrids between Fe-SOD and Mn-SOD, altered metal content
additional information
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naturally occuring hybrids between Fe-SOD and Mn-SOD, altered metal content
additional information
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naturally occuring hybrids between Fe-SOD and Mn-SOD, altered metal content
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additional information
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naturally occuring hybrids between Fe-SOD and Mn-SOD, altered metal content
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additional information
construction of a fusion protein between the N-terminal domain of superoxide dismutase from Geobacillus thermodenitrificans NG80-2 and superoxide dismutase from Sulfolobus solfataricus. The recombinant protein exhibits improved thermophilicity, higher working temperature, improved thermostability, broader pH stability, and enhanced tolerance to inhibitors and organic media without any alterations in its oligomerization state. The N-terminal domain is a good candidate for improving stability of both mesophilic and thermophilic superoxide dismutase from either bacteria or archaea via simple genetic manipulation
additional information
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construction of a fusion protein between the N-terminal domain of superoxide dismutase from Geobacillus thermodenitrificans NG80-2 and superoxide dismutase from Sulfolobus solfataricus. The recombinant protein exhibits improved thermophilicity, higher working temperature, improved thermostability, broader pH stability, and enhanced tolerance to inhibitors and organic media without any alterations in its oligomerization state. The N-terminal domain is a good candidate for improving stability of both mesophilic and thermophilic superoxide dismutase from either bacteria or archaea via simple genetic manipulation
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additional information
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replacement of all of the nine tyosine residues in each of the four enzyme subunits by 3-fluorotyrosine. Crystal structures of unfluorinated and fluorinated enzyme are nearly superimposable. Ratio kcat/Km decreases from 0.8 per mM and s for wild-type to 0.03 per mM and s for the fluorinated mutant which is in significant part due to 3-fluorotyrosine residues distant from the active-site metal
additional information
construction of a zinc-deficient enzyme, structure analysis, the loss of zinc from SOD is potentially important for both the aggregation and zinc-deficient Cu,Zn-SOD hypotheses, and leads to an altered dimer, phenotypes, overview
additional information
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construction of a zinc-deficient enzyme, structure analysis, the loss of zinc from SOD is potentially important for both the aggregation and zinc-deficient Cu,Zn-SOD hypotheses, and leads to an altered dimer, phenotypes, overview
additional information
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the recombinant SOD is cvalently linked to lecithin, which increases its half-life after administration to humans
additional information
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deletion analysis of the key DNA binding elements in the SOD-1 gene promoter identifies the distal hypoxia response element, but not the peroxisome proliferator response element or nuclear factor-kappaB element, as essential for the suppressive effects of docosahexaenoic acid
additional information
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engineering of a novel chimera of human Mn-SOD and Vitreoscilla hemoglobin, i.e. MnSOD-VHb, for rapid detoxification of reactive oxygen species, the recombinant bifunctional enzyme possesses MnSOD and peroxidase-like activities. The greater antioxidant capability is possibly due to the close proximity between the active site of MnSOD and the heme moiety of VHb, synergistic functions of SOD and peroxidase, overview
additional information
generation of a catalytically active truncated (residues 19-240) mutant form of human EC-SOD (hEC-SOD)
additional information
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generation of a catalytically active truncated (residues 19-240) mutant form of human EC-SOD (hEC-SOD)
additional information
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the mutant enzymes lacking the glutamate and lysine residues close to the active site can be a competent superoxide reductase
additional information
overexpression of recombinant Cu/Zn-SOD1 in strain L3 does not significantly increase the SOD specific activity, and in some cases, a net reduction of the enzymatic activity occurs, cell phenotypes, overview
additional information
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overexpression of recombinant Cu/Zn-SOD1 in strain L3 does not significantly increase the SOD specific activity, and in some cases, a net reduction of the enzymatic activity occurs, cell phenotypes, overview
additional information
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overexpression of recombinant Cu/Zn-SOD1 in strain L3 does not significantly increase the SOD specific activity, and in some cases, a net reduction of the enzymatic activity occurs, cell phenotypes, overview
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additional information
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hyaluronan levels are increased in the bronchoalveolar lavage fluid after asbestos-induced pulmonary injury, and this response is markedly enhanced in EC-SOD knock-out mice, overview
additional information
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phenotype of homozygous LDL-receptor-knockout mice, heterozygous ob/+, and wild-type C57BL6 mice, overview
additional information
the recombinant pea chloroplastic SOD possesses nearly 6fold higher superoxide dismutase activity and 5fold higher peroxidase activity as compared to commercially available CuZn-superoxide dismutase from Bos taurus. The recombinant protein harbors all the characteristics features of this class of enzyme. The recombinant enzyme is exceptionally stable concerning pH and temperature and maintains its activity upon prolonged storage
additional information
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the recombinant pea chloroplastic SOD possesses nearly 6fold higher superoxide dismutase activity and 5fold higher peroxidase activity as compared to commercially available CuZn-superoxide dismutase from Bos taurus. The recombinant protein harbors all the characteristics features of this class of enzyme. The recombinant enzyme is exceptionally stable concerning pH and temperature and maintains its activity upon prolonged storage
additional information
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construction of an enzyme-deletion mutant, the mutant strain is less virulent in mice than the wild-type strain or the complemented strain, overview
additional information
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construction of mutants of strain PAO1 lacking manganese-SOD, iron-SOD, or both, the mutants are injected into the hemocoel of Bombyx mori, the virulence decreases in the order: wild-type PAO1, manganese-SOD deficient PAO1, iron-SOD deficient PAO1, and double mutant PAO1, which is avirulent at a dose of 105 cells or less, the virulence of the double mutant can be partially restored by expression of a wild-type enzyme variant, overview
additional information
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construction of mutants of Pseudomonas putida lacking manganese-superoxide dismutase MnSOD, iron-superoxide dismutase FeSOD, or both, phenotypes, overview, the sodA sodB mutant does not grow on components washed from bean root surfaces or glucose in minimal medium, the sodB and sodA sodB mutants are more sensitive than wild-type to oxidative stress generated within the cell by paraquat treatment
additional information
construction of a fusion protein with the N-terminal domain of superoxide dismutase from Geobacillus thermodenitrificans NG80-2. The recombinant protein exhibits improved thermophilicity, higher working temperature, improved thermostability, broader pH stability, and enhanced tolerance to inhibitors and organic media without any alterations in its oligomerization state
additional information
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construction of a fusion protein with the N-terminal domain of superoxide dismutase from Geobacillus thermodenitrificans NG80-2. The recombinant protein exhibits improved thermophilicity, higher working temperature, improved thermostability, broader pH stability, and enhanced tolerance to inhibitors and organic media without any alterations in its oligomerization state
additional information
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construction of a fusion protein with the N-terminal domain of superoxide dismutase from Geobacillus thermodenitrificans NG80-2. The recombinant protein exhibits improved thermophilicity, higher working temperature, improved thermostability, broader pH stability, and enhanced tolerance to inhibitors and organic media without any alterations in its oligomerization state
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additional information
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naturally occuring exchange of Arg-189 for Lys in the active site of Mn-SOD, sensitivity to lysine-modifying agents
additional information
the enzyme is not significantly modified in light mitochondrial (LMF) fractions by any treatment
additional information
the enzyme is not significantly modified in light mitochondrial (LMF) fractions by any treatment
additional information
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polysialylation of SOD, method development and optimization, overview. Optimal conditions for the cross-linking reaction are the ratio of polysialic acid and SOD of 40:1 with a reaction time of 24 h. Under this condition, the average cross-linking ratio is 3.9 and average molecular weight was 95 kDa derived from the molecular weight of polysialic acid with 16.2 kDa and CuZn-SOD with 32 kDa. The molecular size of the polysialylated enzyme was about 90-100 kDa, enhancement of hydratability of SOD through polysialylation, analysis by atomic force microscopy, overview
additional information
structure models of three enzyme mutants His29Ala, His84Ala, and His171Ala, overview