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Literature summary extracted from

  • Cerdan, P.; Wasserfallen, A.; Rekik, M.; Timmis, K.N.; Harayama, S.
    Substrate specificity of catechol 2,3-dioxygenase encoded by TOL plasmid pWW0 of Pseudomonas putida and its relationship to cell growth (1994), J. Bacteriol., 176, 6074-6081.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.13.11.2 expression in Escherichia coli Pseudomonas putida

Protein Variants

EC Number Protein Variants Comment Organism
1.13.11.2 A177V increased sensitivity to 3-methylcatechol Pseudomonas putida
1.13.11.2 L226S increased activity with 4-ethylcatechol, reduced binding of the ferrous ion cofactor, modified the catalytic activity toward 3-methylcatechol Pseudomonas putida
1.13.11.2 T196I increased sensitivity to 3-methylcatechol Pseudomonas putida
1.13.11.2 T253I increased activity with 4-ethylcatechol, reduced binding of the ferrous ion cofactor Pseudomonas putida

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.13.11.2 additional information
-
 additional information Km of wild-type and mutant enzymes Pseudomonas putida

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.13.11.2 Fe2+ one atom of iron per monomer of the wild-type enzyme Pseudomonas putida

Organism

EC Number Organism UniProt Comment Textmining
1.13.11.2 Pseudomonas putida
-
 KT 2440
-
1.13.11.2 Pseudomonas putida
-
 PaW94
-
1.13.11.2 Pseudomonas putida KT 2440
-
 KT 2440
-
1.13.11.2 Pseudomonas putida PaW94
-
 PaW94
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.13.11.2 wild-type and mutant enzymes Pseudomonas putida

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
1.13.11.2 additional information
-
 comparison of wild-type and mutant enzymes Pseudomonas putida
1.13.11.2 400
-
 wild-type enzyme Pseudomonas putida

Storage Stability

EC Number Storage Stability Organism
1.13.11.2 -80°C, did not prevent the initial loss of activity Pseudomonas putida
1.13.11.2 4°C, 10 h, the mutant enzymes lost 95% of activity Pseudomonas putida
1.13.11.2 4°C, 3 days, 20% loss of activity of wild-type enzyme Pseudomonas putida

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.13.11.2 3-methylcatechol + O2
-
 Pseudomonas putida 2-hydroxy-6-oxohepta-2,4-dienoate
-
 ?
1.13.11.2 3-methylcatechol + O2
-
 Pseudomonas putida KT 2440 2-hydroxy-6-oxohepta-2,4-dienoate
-
 ?
1.13.11.2 3-methylcatechol + O2
-
 Pseudomonas putida PaW94 2-hydroxy-6-oxohepta-2,4-dienoate
-
 ?
1.13.11.2 4-methylcatechol + O2
-
 Pseudomonas putida 2-hydroxy-3-methyl-6-oxohexa-2,4-dienoate
-
 ?
1.13.11.2 4-methylcatechol + O2
-
 Pseudomonas putida KT 2440 2-hydroxy-3-methyl-6-oxohexa-2,4-dienoate
-
 ?
1.13.11.2 4-methylcatechol + O2
-
 Pseudomonas putida PaW94 2-hydroxy-3-methyl-6-oxohexa-2,4-dienoate
-
 ?
1.13.11.2 catechol + O2
-
 Pseudomonas putida 2-hydroxymuconate semialdehyde
-
 ?
1.13.11.2 catechol + O2
-
 Pseudomonas putida KT 2440 2-hydroxymuconate semialdehyde
-
 ?
1.13.11.2 catechol + O2
-
 Pseudomonas putida PaW94 2-hydroxymuconate semialdehyde
-
 ?

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.13.11.2 additional information
-
 additional information comparison of kcat values of wild-type and mutant enzymes for catechol, 3-methylcatechol and 4-ethylcatechol Pseudomonas putida