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Literature summary extracted from

  • Azadmanesh, J.; Trickel, S.R.; Borgstahl, G.E.O.
    Substrate-analog binding and electrostatic surfaces of human manganese superoxide dismutase (2017), J. Struct. Biol., 199, 68-75 .
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.15.1.1 gene SOD2, recombinant expression in Escherichia coli Homo sapiens

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
1.15.1.1 purified enzyme MnSOD in complex with azide, hanging-drop vapor diffusion, mixing of 0.001 ml of 21 mg/ml protein solution with 0.001 ml of reservoir solution 1.8 M potassium phosphate, pH 7.8, at room temperature for1 day, to obtain the azide complex, 0.002 ml of reservoir containing 200 mM sodium azide are added to drops of 6 day crystals, X-ray diffraction structure determination and analysis at 1.77-1.82 A resolution Homo sapiens

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.15.1.1 azide the azide ion acts as a strong competitive inhibitor for SOD by binding directly to the active site metal. Azide is bound end-on at the sixth coordinate position of the manganese ion. Tetrameric electrostatic surfaces are calculated incorporating accurate partial charges for the active site in three states, including a state with superoxide coordinated to the metal using the position of azide as a model Homo sapiens

Metals/Ions

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

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.15.1.1 2 superoxide + 2 H+ Homo sapiens
-
 O2 + H2O2
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.15.1.1 Homo sapiens P04179
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.15.1.1 soluble recombinant enzyme SOD2 from Escherichia coli cell-free extract by dialysis, anion exchange chromatography, again dialysis, and ultrafiltration Homo sapiens

Reaction

EC Number Reaction Comment Organism Reaction ID
1.15.1.1 2 superoxide + 2 H+ = O2 + H2O2 electrostatic guidance of anionic substrate to the active site, detailed overview. Generation of a model for electrostatic-mediated diffusion, and efficient binding of superoxide for catalysis Homo sapiens
a

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.15.1.1 2 superoxide + 2 H+
-
 Homo sapiens O2 + H2O2
-
 ?

Subunits

EC Number Subunits Comment Organism
1.15.1.1 tetramer
-
 Homo sapiens

Synonyms

EC Number Synonyms Comment Organism
1.15.1.1 manganese superoxide dismutase
-
 Homo sapiens
1.15.1.1 MnSOD
-
 Homo sapiens
1.15.1.1 SOD2
-
 Homo sapiens

General Information

EC Number General Information Comment Organism
1.15.1.1 additional information the putative binding position of superoxide is determined from the crystal structure of the enzyme in complex with azide, providing a model for binding to the active site. Facilitation of the anionic ligand to the active site pit via a valley of positively-charged surface patches. Surrounding ridges of negative charge help guide the superoxide anion. Within the active site pit, Arg173 and Glu162 further guide and align superoxide for efficient catalysis. Superoxide coordination at the sixth position causes the electrostatic surface of the active site pit to become nearly neutral. Generation of a model for electrostatic-mediated diffusion, and efficient binding of superoxide for catalysis. The active site manganese ion is coordinated by His26, His74, Asp159, His163, and a single oxygen, typically thought to be a water or hydroxide ion. These ligands are referred to as the inner-sphere residues. Outer-sphereresidues surround the inner-sphere and include His30, Tyr34, Phe77, Trp78, Trp123, Gln143, Trp161 and, from across the dimer interface, Glu162. Distorted five-coordinate trigonal bipyramidal active site geometry of native human MnSOD, overview Homo sapiens