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Literature summary for 1.13.11.1 extracted from

  • Han, L.; Chen, S.; Zhou, J.
    Expression and cloning of catA encoding a catechol 1,2-dioxygenase from the 2,4-D-degrading strain Cupriavidus campinensis BJ71 (2020), Prep. Biochem. Biotechnol., 50, 486-493 .
    View publication on PubMed
Search for more literature for 1.13.11.1

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Escherichia coli Cupriavidus campinensis

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.03997
-
 catechol pH 8.0, 35°C Cupriavidus campinensis

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
34000
-
 calculated from sequence Cupriavidus campinensis

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
catechol + O2 Cupriavidus campinensis
-
 cis,cis-muconate
-
 ?
catechol + O2 Cupriavidus campinensis BJ71
-
 cis,cis-muconate
-
 ?

Organism

Organism UniProt Comment Textmining
Cupriavidus campinensis A0A481S4R2
-
-
Cupriavidus campinensis BJ71 A0A481S4R2
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Cupriavidus campinensis

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4-chlorocatechol + O2 28.05% of the activity compared to catechol Cupriavidus campinensis 4-chloro-cis,cis-muconate
-
 ?
4-chlorocatechol + O2 28.05% of the activity compared to catechol Cupriavidus campinensis BJ71 4-chloro-cis,cis-muconate
-
 ?
4-methylcatechol + O2 90.12% of the activity compared to catechol Cupriavidus campinensis 4-methyl-cis,cis-muconate
-
 ?
4-methylcatechol + O2 90.12% of the activity compared to catechol Cupriavidus campinensis BJ71 4-methyl-cis,cis-muconate
-
 ?
catechol + O2
-
 Cupriavidus campinensis cis,cis-muconate
-
 ?
catechol + O2
-
 Cupriavidus campinensis BJ71 cis,cis-muconate
-
 ?

Synonyms

Synonyms Comment Organism
CatA
-
 Cupriavidus campinensis
catechol 1,2-dioxygenase
-
 Cupriavidus campinensis

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
35
-
-
 Cupriavidus campinensis

Temperature Range [°C]

Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
25 50 25°C: more than 90% of maximal activity, 45°C: more than 90% of maximal activity, 50°C: 72.8% of maximal activity, 55°C: 37.5% of maximal activity Cupriavidus campinensis

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
40
-
 10 min, stable Cupriavidus campinensis
45
-
 10 min, activity dropps to 37.12% of the maximum Cupriavidus campinensis

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
3.65
-
 catechol pH 8.0, 35°C Cupriavidus campinensis

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8
-
-
 Cupriavidus campinensis

pH Range

pH Minimum pH Maximum Comment Organism
6 9 the enzyme retains at least 68.45% of its peak activity in the pH range of 6.0-9.0 Cupriavidus campinensis

pH Stability

pH Stability pH Stability Maximum Comment Organism
6 9 stable Cupriavidus campinensis

pI Value

Organism Comment pI Value Maximum pI Value
Cupriavidus campinensis calculated from sequence
-
 5.39

General Information

General Information Comment Organism
physiological function the enzyme catalyzes catechol ring-opening, a critical step in the degradation of aromatic compounds Cupriavidus campinensis