Literature summary for 1.15.1.1 extracted from

Zheng, J.; Domsic, J.F.; Cabelli, D.; McKenna, R.; Silverman, D.N.
Structural and kinetic study of differences between human and Escherichia coli manganese superoxide dismutases (2007), Biochemistry, 46, 14830-14837.

Cloned(Commentary)

Cloned (Comment)	Organism
gene sod, expression of wild-type and mutant soluble enzymes in Escherichia coli strain QC774, that lacks the genes encoding endogeneous FeSOD, SodB-, and MnSOD, SodA-	Homo sapiens

Crystallization (Commentary)

Crystallization (Comment)	Organism
mutant enzymes F66A and F66L, hanging drop vapor diffusion method, 0.005 ml of enzyme solution are mixed with 0.005 ml of precipitant solution containing 2.5 M ammonium sulfate, 100 mM imidazole, and 100 mM malic acid, pH 8.5, equilibration against 1 ml of precipitant solution, 1 week, room temperature, X-ray diffraction structure determination and analysis at 2.2 A and 2.3 A resolution, respectively	Homo sapiens

Crystallization (Comment)

Organism

mutant enzymes F66A and F66L, hanging drop vapor diffusion method, 0.005 ml of enzyme solution are mixed with 0.005 ml of precipitant solution containing 2.5 M ammonium sulfate, 100 mM imidazole, and 100 mM malic acid, pH 8.5, equilibration against 1 ml of precipitant solution, 1 week, room temperature, X-ray diffraction structure determination and analysis at 2.2 A and 2.3 A resolution, respectively

Homo sapiens

Protein Variants

Protein Variants	Comment	Organism
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	Homo sapiens
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	Homo sapiens

Inhibitors

Inhibitors	Comment	Organism	Structure
additional information	the conserved, active-site residue Tyr34 mediates product inhibition	Homo sapiens

KM Value [mM]

KM Value [mM]	KM Value Maximum [mM]	Substrate	Comment	Organism	Structure
additional information	-	additional information	kinetics of recombinant wild-type and mutant enzymes	Homo sapiens

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Mn2+	a Mn-SOD	Homo sapiens

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
O2.- + H+	Homo sapiens	-	O2 + H2O2	-	?

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	P04179	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
O2.- + H+	-	Homo sapiens	O2 + H2O2	-	?
O2.- + H+	the conserved, active-site residue Tyr34 mediates product inhibition	Homo sapiens	O2 + H2O2	-	?

Subunits

Subunits	Comment	Organism
tetramer	-	Homo sapiens

Synonyms

Synonyms	Comment	Organism
manganese superoxide dismutase	-	Homo sapiens
MnSOD	-	Homo sapiens

Temperature Optimum [°C]

Temperature Optimum [°C]	Temperature Optimum Maximum [°C]	Comment	Organism
25	-	assay at	Homo sapiens

pH Optimum

pH Optimum Minimum	pH Optimum Maximum	Comment	Organism
7.8	-	assay at	Homo sapiens

pH Range

pH Minimum	pH Maximum	Comment	Organism
6.4	10.9	-	Homo sapiens