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Literature summary for 1.11.1.6 extracted from

  • Kamat, S.S.; Holmes-Hampton, G.P.; Bagaria, A.; Kumaran, D.; Tichy, S.E.; Gheyi, T.; Zheng, X.; Bain, K.; Groshong, C.; Emtage, S.; Sauder, J.M.; Burley, S.K.; Swaminathan, S.; Lindahl, P.A.; Raushel, F.M.
    The catalase activity of diiron adenine deaminase (2011), Protein Sci., 20, 2080-2094.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 1.11.1.6

Crystallization (Commentary)

Crystallization (Comment) Organism
metal-bound [FeII/FeII]-ADEec and [FeII/MnII]-ADEec enzyme, sitting drop vapor diffusion, room temperature, X-ray diffraction struccture determination and analysis at 2.63-2.8 A resolution Escherichia coli

Protein Variants

Protein Variants Comment Organism
D474N site-directed mutagenesis, catalase inactive mutant Escherichia coli
H473N site-directed mutagenesis, catalase inactive mutant Escherichia coli

General Stability

General Stability Organism
iron-bound [FeII/FeII]-ADE undergoes more than 100 turnovers with H2O2 before the enzyme is inactivated due to oxygenation of histidine residues critical for metal binding Escherichia coli

Inhibitors

Inhibitors Comment Organism Structure
6-Chloropurine
-
 Escherichia coli
H2O2 excess H2O2 inhibits the enzyme. In the presence of excess H2O2, [FeII/FeII]-ADEec rapidly loses its ability to deaminate adenine Escherichia coli
additional information oxygenation of active site residues, inhibiting catalase activity, occurs via release of hydroxyl radicals Escherichia coli

Metals/Ions

Metals/Ions Comment Organism Structure
Fe2+ enzyme-bound, [FeII/FeII]-enzyme, required for activity. Disproportionation of H2O2 by the iron-bound enzyme involves the cycling of the binuclear metal center between the di-ferric and di-ferrous oxidation states Escherichia coli
additional information no acatalase acivit with Zn2+ or Mn2+-substituted enzyme Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Escherichia coli adenine deaminase, EC 3.5.4.2, from the amidohydrolase superfamily of enzymes catalyzes the conversion of adenine to hypoxanthine and ammonia. But it also catalyzes the catalase reaction converting H2O2 to H2O and O2. [MnII/MnII]-ADEec is active as a deaminase but not as a catalase. In contrast, [FeII/FeII]-ADEec catalyzes both reactions ?
-
 ?

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2 H2O2
-
 Escherichia coli O2 + 2 H2O
-
 ?
additional information adenine deaminase, EC 3.5.4.2, from the amidohydrolase superfamily of enzymes catalyzes the conversion of adenine to hypoxanthine and ammonia. But it also catalyzes the catalase reaction converting H2O2 to H2O and O2. [MnII/MnII]-ADEec is active as a deaminase but not as a catalase. In contrast, [FeII/FeII]-ADEec catalyzes both reactions Escherichia coli ?
-
 ?

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
200
-
 H2O2 pH 7.5, 30°C Escherichia coli

General Information

General Information Comment Organism
additional information reaction mechanism of catalase activity, overview. The iron in the active site is in an uncoupled high-spin ferric oxidation state. The metal ions can be reduced back to the di-ferrous state with dithionite but the deaminase activity is not recovered. Therefore, addition of an excess of H2O2 to [FeII/FeII]-ADEec irreversibly modifies the protein and stabilizes the [FeIII/FeIII] state Escherichia coli

kcat/KM [mM/s]

kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
24
-
 H2O2 pH 7.5, 30°C Escherichia coli