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Literature summary extracted from

  • Caglio, R.; Pessione, E.; Valetti, F.; Giunta, C.; Ghibaudi, E.
    An EPR, thermostability and pH-dependence study of wild-type and mutant forms of catechol 1,2-dioxygenase from Acinetobacter radioresistens S13 (2013), Biometals, 26, 75-84.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.13.11.1 expression of wild-type and mutant enzymes in Escherichia coli Acinetobacter radioresistens

Protein Variants

EC Number Protein Variants Comment Organism
1.13.11.1 A72D site-directed mutagenesis, the mutant shows a low level of iron incorporation compared to the wild-type enzyme and altered thermal stability values, pH and temperature dependence Acinetobacter radioresistens
1.13.11.1 A72G site-directed mutagenesis, the mutant shows altered thermal stability values, pH and temperature dependence Acinetobacter radioresistens
1.13.11.1 A72N site-directed mutagenesis, the mutant shows a disturbed iron binding and altered thermal stability values, pH and temperature dependence Acinetobacter radioresistens
1.13.11.1 A72P site-directed mutagenesis, the mutant shows altered thermal stability values, pH and temperature dependence Acinetobacter radioresistens
1.13.11.1 A72S site-directed mutagenesis, the mutant shows altered thermal stability values, pH and temperature dependence Acinetobacter radioresistens
1.13.11.1 L69A site-directed mutagenesis, the mutant shows altered thermal stability values, pH and temperature dependence Acinetobacter radioresistens
1.13.11.1 L69G/A72G site-directed mutagenesis, the mutant shows altered thermal stability values, pH and temperature dependence Acinetobacter radioresistens

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.13.11.1 Fe3+ bound at the active site Acinetobacter radioresistens

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.13.11.1 catechol + O2 Acinetobacter radioresistens
-
 cis,cis-muconate
-
 ?
1.13.11.1 catechol + O2 Acinetobacter radioresistens S13
-
 cis,cis-muconate
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.13.11.1 Acinetobacter radioresistens
-
-
-
1.13.11.1 Acinetobacter radioresistens S13
-
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.13.11.1 catechol + O2
-
 Acinetobacter radioresistens cis,cis-muconate
-
 ?
1.13.11.1 catechol + O2
-
 Acinetobacter radioresistens S13 cis,cis-muconate
-
 ?

Synonyms

EC Number Synonyms Comment Organism
1.13.11.1 1,2-CTD
-
 Acinetobacter radioresistens

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
1.13.11.1 23 27 mutant L69G/A72G Acinetobacter radioresistens
1.13.11.1 27
-
 mutant L69A Acinetobacter radioresistens
1.13.11.1 30
-
 wild-type enzyme and mutants Aa72G and A72P Acinetobacter radioresistens
1.13.11.1 37
-
 mutant A72S 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 2.04
-
 catechol pH 8.0, 35°C, mutant A72G/L69G Acinetobacter radioresistens
1.13.11.1 4.81
-
 catechol pH 8.0, 35°C, mutant L69A Acinetobacter radioresistens
1.13.11.1 13.56
-
 catechol pH 8.0, 35°C, mutant A72G Acinetobacter radioresistens
1.13.11.1 14.72
-
 catechol pH 8.0, 35°C, mutant A72P Acinetobacter radioresistens
1.13.11.1 15.48
-
 catechol pH 8.0, 35°C, mutant A72S Acinetobacter radioresistens
1.13.11.1 30.03
-
 catechol pH 8.0, 35°C, wild-type enzyme Acinetobacter radioresistens

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.13.11.1 8
-
 mutant L69G/A72G Acinetobacter radioresistens
1.13.11.1 8 8.5 wild-type enzyme Acinetobacter radioresistens
1.13.11.1 8 9 mutants L69A and A72S Acinetobacter radioresistens
1.13.11.1 8.5 9 mutant A72P Acinetobacter radioresistens
1.13.11.1 9
-
 mutant A72G Acinetobacter radioresistens

General Information

EC Number General Information Comment Organism
1.13.11.1 evolution the enzyme is a non-heme Fe dioxygenase Acinetobacter radioresistens
1.13.11.1 additional information structure-function relationships of wild-type and mutant enzymes, overview Acinetobacter radioresistens