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Literature summary extracted from

  • Vetting, M.W.; D'Argenio, D.A.; Ornston, L.N.; Ohlendorf, D.H.
    Structure of Acinetobacter strain ADP1 protocatechuate 3,4-dioxygenase at 2.2 A resolution: implications for the mechanism of an intradiol dioxygenase (2000), Biochemistry, 39, 7943-7955.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.13.11.3
-
 Acinetobacter sp.

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
1.13.11.3 recombinant enzyme, hanging drop method with 1.8 M ammonium sulfate, 50 mM Tris-HCl pH 7.0 in the reservoir and 10 mg/ml enzyme in the drop at 18°C, crystals grow as perfect dodecahedrons, crystal structure with 2.2 A resolution Acinetobacter sp.

Organism

EC Number Organism UniProt Comment Textmining
1.13.11.3 Acinetobacter sp.
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.13.11.3 recombinant enzyme Acinetobacter sp.

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.13.11.3 3,4-dihydroxybenzoate + O2
-
 Acinetobacter sp. 3-carboxy-cis,cis-muconate
-
 ?

Subunits

EC Number Subunits Comment Organism
1.13.11.3 More crystal structure, dodecameric enzyme Acinetobacter sp.