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Literature summary for 1.14.12.12 extracted from

  • Ensley, B.D.; Gibson, D.T.
    Naphthalene dioxygenase: purification and properties of a terminal oxygenase component (1983), J. Bacteriol., 155, 505-511.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 1.14.12.12

General Stability

General Stability Organism
10% ethanol and 10% glycerol are required for stability Pseudomonas sp.
DTT stabilizes Pseudomonas sp.

Localization

Localization Comment Organism GeneOntology No. Textmining
cytoplasm
-
 Pseudomonas sp. 5737
-

Metals/Ions

Metals/Ions Comment Organism Structure
Fe2+ component B, the terminal oxygenase ISPNAP is an iron-sulfur protein, oxidized ISPNAP binds naphthalene without conformational changes that affect its FeS-chromophores, ISPNAP contains 6 g-atom Fe2+ and 4 g-atom acid-labile sulfur per mol enzyme, the enzyme complex is not stimulated by exogenous Fe2+ Pseudomonas sp.

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
additional information
-
 three component enzyme system consisting of: component A, i.e. ferredoxinNAP reductase, component B, i.e. terminal oxygenase ISPNAP, and component C, i.e. ferredoxinNAP Pseudomonas sp.
20000
-
 alpha2beta2 2 * 55000 + 2 * 20000, terminal oxygenase ISPNAP, SDS-PAGE Pseudomonas sp.
55000
-
 alpha2beta2 2 * 55000 + 2 * 20000, terminal oxygenase ISPNAP, SDS-PAGE Pseudomonas sp.
158000
-
 component B, i.e. oxygenase ISPNAP, gel filtration Pseudomonas sp.

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
naphthalene + NADH + O2 Pseudomonas sp.
-
 (1R,2S)-1,2-dihydronaphthalene-1,2-diol + NAD+
-
 ?
naphthalene + NADH + O2 Pseudomonas sp. NCIB 9816
-
 (1R,2S)-1,2-dihydronaphthalene-1,2-diol + NAD+
-
 ?

Organism

Organism UniProt Comment Textmining
Pseudomonas sp.
-
-
-
Pseudomonas sp. NCIB 9816
-
-
-

Purification (Commentary)

Purification (Comment) Organism
component B i.e. the terminal oxygenase ISPNAP, DEAE-Sephadex, DEAE-cellulose, octyl-Sepharose, presence of 10% ethanol and 10% glycerol is required to maintain stability Pseudomonas sp.

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
1.37
-
 in the presence of partially purified components A and C of the 3 component enzyme system plus FAD Pseudomonas sp.

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
naphthalene + NADH + O2
-
 Pseudomonas sp. cis-(1R,2S)-1,2-dihydronaphthalene-1,2-diol + NAD+
-
 ?
naphthalene + NADH + O2
-
 Pseudomonas sp. NCIB 9816 cis-(1R,2S)-1,2-dihydronaphthalene-1,2-diol + NAD+
-
 ?
naphthalene + NADH + O2
-
 Pseudomonas sp. (1R,2S)-1,2-dihydronaphthalene-1,2-diol + NAD+
-
 ?
naphthalene + NADH + O2
-
 Pseudomonas sp. NCIB 9816 (1R,2S)-1,2-dihydronaphthalene-1,2-diol + NAD+
-
 ?

Subunits

Subunits Comment Organism
tetramer alpha2beta2 2 * 55000 + 2 * 20000, terminal oxygenase ISPNAP, SDS-PAGE Pseudomonas sp.

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.5
-
 assay at Pseudomonas sp.

Cofactor

Cofactor Comment Organism Structure
FAD component A, ferredoxinNAP reductase is a flavoprotein, enzyme can use both FAD and FMN but exhibits slightly higher affinity for FAD Pseudomonas sp.
NADH requirement, the oxygenase accepts two electrons from NADH, the reduction requires component A and C as mediators Pseudomonas sp.