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Literature summary for 1.13.11.2 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
Search for more literature for 1.13.11.2

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli Pseudomonas putida

Protein Variants

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

KM Value [mM]

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

Metals/Ions

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

Organism

Organism UniProt Comment Textmining
Pseudomonas putida
-
 KT 2440
-
Pseudomonas putida
-
 PaW94
-
Pseudomonas putida KT 2440
-
 KT 2440
-
Pseudomonas putida PaW94
-
 PaW94
-

Purification (Commentary)

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

Specific Activity [micromol/min/mg]

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

Storage Stability

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

Substrates and Products (Substrate)

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

Turnover Number [1/s]

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