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Literature summary for 1.13.11.1 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)

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

Protein Variants

Protein Variants Comment Organism
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
A72G site-directed mutagenesis, the mutant shows altered thermal stability values, pH and temperature dependence Acinetobacter radioresistens
A72N site-directed mutagenesis, the mutant shows a disturbed iron binding and altered thermal stability values, pH and temperature dependence Acinetobacter radioresistens
A72P site-directed mutagenesis, the mutant shows altered thermal stability values, pH and temperature dependence Acinetobacter radioresistens
A72S site-directed mutagenesis, the mutant shows altered thermal stability values, pH and temperature dependence Acinetobacter radioresistens
L69A site-directed mutagenesis, the mutant shows altered thermal stability values, pH and temperature dependence Acinetobacter radioresistens
L69G/A72G site-directed mutagenesis, the mutant shows altered thermal stability values, pH and temperature dependence Acinetobacter radioresistens

Metals/Ions

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

Natural Substrates/ Products (Substrates)

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

Organism

Organism UniProt Comment Textmining
Acinetobacter radioresistens
-
-
-
Acinetobacter radioresistens S13
-
-
-

Substrates and Products (Substrate)

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

Synonyms

Synonyms Comment Organism
1,2-CTD
-
Acinetobacter radioresistens

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
23 27 mutant L69G/A72G Acinetobacter radioresistens
27
-
mutant L69A Acinetobacter radioresistens
30
-
wild-type enzyme and mutants Aa72G and A72P Acinetobacter radioresistens
37
-
mutant A72S Acinetobacter radioresistens

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
2.04
-
catechol pH 8.0, 35°C, mutant A72G/L69G Acinetobacter radioresistens
4.81
-
catechol pH 8.0, 35°C, mutant L69A Acinetobacter radioresistens
13.56
-
catechol pH 8.0, 35°C, mutant A72G Acinetobacter radioresistens
14.72
-
catechol pH 8.0, 35°C, mutant A72P Acinetobacter radioresistens
15.48
-
catechol pH 8.0, 35°C, mutant A72S Acinetobacter radioresistens
30.03
-
catechol pH 8.0, 35°C, wild-type enzyme Acinetobacter radioresistens

pH Optimum

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

General Information

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