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Literature summary extracted from

  • Pessione, E.; Divari, S.; Griva, E.; Cavaletto, M.; Rossi, G.L.; Gilardi, G.; Giunta, C.
    Phenol hydroxylase from Acinetobacter radioresistens is a multicomponent enzyme. Purification and characterization of the reductase moiety (1999), Eur. J. Biochem., 265, 549-555.
    View publication on PubMed

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.14.13.7 additional information
-
 additional information Km values with various electron acceptors Acinetobacter radioresistens

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.14.13.7 Fe2+ iron-sulfur cluster of the type 2Fe-2S Acinetobacter radioresistens

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.14.13.7 38800
-
 gel filtration Acinetobacter radioresistens
1.14.13.7 41000
-
 SDS-PAGE Acinetobacter radioresistens

Organism

EC Number Organism UniProt Comment Textmining
1.14.13.7 Acinetobacter radioresistens
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.14.13.7
-
 Acinetobacter radioresistens

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
1.14.13.7 429.5
-
-
 Acinetobacter radioresistens

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.14.13.7 phenol + NADPH + O2 cytochrome c, 2,6-dichlorophenolindophenol, potassium ferricyanide and nitro blue tetrazolium can act as electron acceptors in vitro Acinetobacter radioresistens catechol + NADP+ + H2O
-
 ?

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.14.13.7 additional information
-
 additional information with various electron acceptors Acinetobacter radioresistens