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Literature summary extracted from

  • Miller, A.F.; Sorkin, D.L.; Padmakumar, K.
    Anion binding properties of reduced and oxidized iron-containing superoxide dismutase reveal no requirement for tyrosine 34 (2005), Biochemistry, 44, 5969-5981.
    View publication on PubMed

Protein Variants

EC Number Protein Variants Comment Organism
1.15.1.1 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 Escherichia coli

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.15.1.1 HS- substrate analogue, formation of a green complex upon binding Escherichia coli
1.15.1.1 N3-
-
 Escherichia coli

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.15.1.1 additional information
-
 additional information pH-dependence of KM-value reflects the inhibition of anion binding by ionized Y34 Escherichia coli

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.15.1.1 Iron spectroscopic analysis of reduced and oxidized state of iron. In oxidized state, formation of a six-coordinate complex occurs. Two substrate analogues F- can bind to the oxidized enzyme’s active site Escherichia coli

Organism

EC Number Organism UniProt Comment Textmining
1.15.1.1 Escherichia coli P0AGD3 FeSOD
-