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1.15.1.1: superoxide dismutase

This is an abbreviated version!
For detailed information about superoxide dismutase, go to the full flat file.

Word Map on EC 1.15.1.1

Reaction

2 superoxide + 2 H+ =

O2
+
H2O2

Synonyms

AhSOD, alr2938, AmSOD, APE0743, ApMn-SOD1, ApMn-SOD2, ASAC_0498, Ca-Cu,Zn SOD, cambialistic superoxide dismutase, Cg-EcSOD, chloroplastic Fe-SOD, Cj-Cu, Zn SOD, cMn-SOD, cMnSOD, cold-active superoxide dismutase, copper, zinc superoxide dismutase, copper-zinc superoxide dismutase, copper/zinc superoxide dismutase, copper/zinc-superoxide dismutase, CpSOD, CSD1, CSD2, CtSOD, Cu, Zn SOD, Cu, Zn superoxide dismutase, Cu, Zn-superoxide dismutase, Cu, ZnSOD, Cu,Zn superoxide dismutase, Cu,Zn-SOD, Cu,Zn-superoxide dismutase, Cu,ZnSOD, Cu-Zn SOD, Cu-Zn superoxide dismutase, Cu-Zn-SOD, Cu/Zn SOD, Cu/Zn superoxide dismutase, Cu/Zn superoxide dismutase 1, Cu/Zn-SOD, Cu/Zn-SODI, Cu/Zn-SODII, Cu/Zn-superoxide dismutase, Cu/ZnSOD, cuprein, CuZn superoxide dismutase, CuZn superoxide dismutase 1, CuZn-SOD, CuZn-superoxide dismutase, CuZnSOD, cytMnSOD, cytocuprein, cytoplasmic manganese SOD, cytosolic Cu/Zn superoxide dismutase, cytosolic Cu/Zn-SOD, cytosolic manganese superoxide dismutase, DaSOD, dhsod-1, dismutase, superoxide, EC-SOD, ecCuZnSOD, ECSOD, ElFe-SOD, ElSOD, erythrocuprein, erythrocyte superoxide dismutase, eSOD, extracellular copper-zinc superoxide dismutase, extracellular CuZnSOD, extracellular SOD, extracellular superoxide dismutase, Fe-SOD, Fe-SODe, Fe-SOD_ASAC, Fe-superoxide dismutase, Fe-type SOD, Fe/Mn-SOD, Fe/Mn-type SOD, Fe/MnSOD, ferrisuperoxide dismutase, FeSOD, GTNG_2884, hEC-SOD, hemocuprein, hepatocuprein, high isoelectric point superoxide dismutase, intracellular Cu-Zn superoxide dismutase, iron SOD, iron SOD type, iron superoxide dismutase, iron-containing superoxide dismutase, iron-dependent superoxide dismutase, iron-superoxide dismutase, KmSod1p, LSOD, manganese superoxide dismutase, manganese-containing SOD, manganese-containing superoxide dismutase, MgMnSOD1, MgMnSOD2, mitMn-SOD, mitochondrial manganese superoxide dismutase, mMnSOD, Mn-containing superoxide dismutase, Mn-SOD, Mn-type SOD, Mn/Fe superoxide dismutase, MnSOD, MnSOD-2, MnSOD-3, MnSOD1, MnSOD47, More, mtMnSOD, mtSOD, nectarin I, neelaredoxin, Nlr, Of-cCu/ZnSOD, PASOD, perMn-SOD, pfSOD, PschSOD, PsSOD, PthipI-SODC, PthipI-SODC1, PthipI-SODC2, RmFeSOD, RsrSOD, SaCSD1, SaFe-SOD, sdB, SOD, SOD 1, SOD I, SOD-1, SOD-2, SOD-3, SOD-4, SOD1, SOD2, SOD3, SODA, SodB, SODB1, SODB2, SodC, SODF, SODI, SODII, SODIII, SODIV, SODS, SSO0316, superoxide dismutase, superoxide dismutase 1, superoxide dismutase I, superoxide dismutase II, superoxide dismutase [Cu-Zn]

ECTree

     1 Oxidoreductases
         1.15 Acting on superoxide as acceptor
             1.15.1 Acting on superoxide as acceptor (only sub-subclass identified to date)
                1.15.1.1 superoxide dismutase

Engineering

Engineering on EC 1.15.1.1 - superoxide dismutase

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
P143S/P145L
A16V
naturally occuring ala16val polymorphism genotyping, overview
A4V
-
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
-
catalytic efficiency similar to wild-type, product inhibition is less than in wild-type
C140S/Q143A
-
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
-
an amyotrophic lateral sclerosis-associated naturally occuring SOD mutant, misfolding/aggregation mechanism with folding and unfolding kinetics, overview
E93A
-
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
-
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
-
Cu,Zn-SOD, site-directed mutagenesis, analogous to mutant found in familial amyotrophic lateral sclerosis, 47% activity compared to the wild-type
G93R
-
an amyotrophic lateral sclerosis-associated naturally occuring SOD mutant, misfolding/aggregation mechanism with folding and unfolding kinetics, overview
H46R
-
an amyotrophic lateral sclerosis-associated naturally occuring SOD mutant, misfolding/aggregation mechanism with folding and unfolding kinetics, overview
H63C
-
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
-
ratio kcat/Km about twofold smaller than in wild-type, product inhibition similar to wild-type
N73S/C140S/Q143A
-
catalytic efficiency much smaller than wild-type, no appreciable product inhibition
N73S/Q143A
-
catalytic efficiency much smaller than wild-type, no appreciable product inhibition
Q143A
-
dramatically reduced product inhibition, reduced catalytic activity and efficiency
Y34F
-
about 12fold decrease in kcat value
D90A
-
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
-
G41N
-
Cu,Zn-SOD, site-directed mutagenesis, analogous to mutant found in familial amyotrophic lateral sclerosis, 47% activity compared to the wild-type
-
G85R
-
Cu,Zn-SOD, site-directed mutagenesis, analogous to mutant found in familial amyotrophic lateral sclerosis, 99% activity compared to the wild-type
-
H43R
-
Cu,Zn-SOD, site-directed mutagenesis, analogous to mutant found in familial amyotrophic lateral sclerosis, 66% activity compared to the wild-type
-
H63C
-
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
-
G93A
-
site-directed mutagenesis
R213G
H155Q
-
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
-
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
-
active site mutant, site-directed mutagenesis, activity, sensitivity to heat and inhibitors unchanged compared to wild-type
K170R
-
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
-
active site mutant, site-directed mutagenesis, activity, sensitivity to heat and inhibitors unchanged compared to wild-type
-
K170R
-
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
-
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
additional information