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Literature summary extracted from

  • Briganti, F.; Pessione, E.; Giunta, C.; Mazzoli, R.; Scozzafava, A.
    Purification and catalytic properties of two catechol 1,2-dioxygenase isozymes from benzoate-grown cells of Acinetobacter radioresistens (2000), J. Protein Chem., 19, 709-716.
    View publication on PubMed

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.13.11.1 Ag+
-
 Acinetobacter radioresistens
1.13.11.1 iodoacetamide
-
 Acinetobacter radioresistens
1.13.11.1 o-phenanthroline
-
 Acinetobacter radioresistens
1.13.11.1 Tiron
-
 Acinetobacter radioresistens

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.13.11.1 0.001
-
 catechol IsoB Acinetobacter radioresistens
1.13.11.1 0.0028
-
 catechol IsoA Acinetobacter radioresistens

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.13.11.1 Iron isoenzyme A: 0.96 mol per mol enzyme, isoenzyme B: 0.89 mol per mol enzyme Acinetobacter radioresistens

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.13.11.1 37700
-
 2 * 37700, isoenzyme B, SDS-PAGE Acinetobacter radioresistens
1.13.11.1 38600
-
 2 * 38600, isoenzyme A, SDS-PAGE Acinetobacter radioresistens
1.13.11.1 38600
-
 3 * 38600, isoenzyme A, low ionic strength, SDS-PAGE Acinetobacter radioresistens
1.13.11.1 76200
-
 isoenzyme B, gel filtration, high ionic strength Acinetobacter radioresistens
1.13.11.1 76800
-
 isoenzyme B, gel filtration, low ionic strength Acinetobacter radioresistens
1.13.11.1 77600
-
 isoenzyme A, gel filtration, high ionic strength Acinetobacter radioresistens
1.13.11.1 112400
-
 isoenzyme A, gel filtration, low ionic strength Acinetobacter radioresistens

Organism

EC Number Organism UniProt Comment Textmining
1.13.11.1 Acinetobacter radioresistens
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.13.11.1 isoenzymes A and B Acinetobacter radioresistens

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
1.13.11.1 additional information
-
-
 Acinetobacter radioresistens

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.13.11.1 3-methylcatechol + O2
-
 Acinetobacter radioresistens (2Z,4Z)-2-methylhexa-2,4-dienedioate
-
 ?
1.13.11.1 4-methylcatechol + O2
-
 Acinetobacter radioresistens (2Z,4Z)-3-methylhexa-2,4-dienedioate
-
 ?
1.13.11.1 catechol + O2
-
 Acinetobacter radioresistens cis,cis-muconate
-
 ?
1.13.11.1 additional information extradiol cleavage of 3-methylcatechol, no substrate: 3-chlorocatechol, protocatechuic acid Acinetobacter radioresistens ?
-
 ?

Subunits

EC Number Subunits Comment Organism
1.13.11.1 homodimer 2 * 37700, isoenzyme B, SDS-PAGE Acinetobacter radioresistens
1.13.11.1 homodimer 2 * 38600, isoenzyme A, SDS-PAGE Acinetobacter radioresistens
1.13.11.1 trimer 3 * 38600, isoenzyme A, low ionic strength, SDS-PAGE Acinetobacter radioresistens

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
1.13.11.1 30 45 IsoA Acinetobacter radioresistens
1.13.11.1 40
-
 IsoB Acinetobacter radioresistens

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.13.11.1 31.3
-
 catechol isoenzyme B Acinetobacter radioresistens
1.13.11.1 48.7
-
 catechol isoenzyme A Acinetobacter radioresistens

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.13.11.1 6.6 8.5 isoenzyme A Acinetobacter radioresistens
1.13.11.1 6.6 8.5 isoenzyme B Acinetobacter radioresistens