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Literature summary for 1.13.11.1 extracted from

  • Di Nardo, G.; Roggero, C.; Campolongo, S.; Valetti, F.; Trotta, F.; Gilardi, G.
    Catalytic properties of catechol 1,2-dioxygenase from Acinetobacter radioresistens S13 immobilized on nanosponges (2009), Dalton Trans., 33, 6507-6512.
    View publication on PubMed
Search for more literature for 1.13.11.1

Application

Application Comment Organism
biotechnology product is precursor of the industrially important compound adipic acid Acinetobacter radioresistens

Cloned(Commentary)

Cloned (Comment) Organism
-
 Acinetobacter radioresistens

Protein Variants

Protein Variants Comment Organism
additional information immobilized enzyme on nanosponges Acinetobacter radioresistens

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.002
-
 catechol free protein Acinetobacter radioresistens
0.0166
-
 catechol immobilized protein Acinetobacter radioresistens

Metals/Ions

Metals/Ions Comment Organism Structure
Iron contains iron Acinetobacter radioresistens

Organism

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

Purification (Commentary)

Purification (Comment) Organism
-
 Acinetobacter radioresistens

Storage Stability

Storage Stability Organism
25°C, 11 days, complete inactivation for the immobilized protein Acinetobacter radioresistens
25°C, 4 days, residual activity 50% for the immobilized protein and 10% for the free form Acinetobacter radioresistens
25°C, 5 days, complete inactivation for the free enzyme Acinetobacter radioresistens
4°C, 10 days, 50% residual acitivity for the immobilized protein and only 10% residual activity of the free form protein Acinetobacter radioresistens

Substrates and Products (Substrate)

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

Synonyms

Synonyms Comment Organism
catechol 1,2-dioxygenase
-
 Acinetobacter radioresistens

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
30
-
 free protein Acinetobacter radioresistens
50
-
 immobilized protein Acinetobacter radioresistens

Temperature Range [°C]

Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
10 60 at 60°C still 70% residual activity of the immobilized enzyme form Acinetobacter radioresistens
30 40 complete loss of enzyme activity of the free form at 60°C Acinetobacter radioresistens

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
40
-
 90 min, 60% residual activity for the immobilized protein versus 20% residual activity for the free enzyme Acinetobacter radioresistens
60
-
 15 min, 75% residual activity for the immobilized protein versus total inactivation of the free enzyme Acinetobacter radioresistens

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8.5
-
 free protein Acinetobacter radioresistens
9.5
-
 immobilized protein Acinetobacter radioresistens

pH Range

pH Minimum pH Maximum Comment Organism
6.5 10 below no enzyme activity, at pH 8.5 40% residual enzyme activity of the immobilized enzyme compared to inactive free form enzyme Acinetobacter radioresistens