EC 1.14.12.12 - Naphthalene 1,2-dioxygenase

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IntEnz Enzyme Nomenclature
EC 1.14.12.12

Names

Accepted name:
naphthalene 1,2-dioxygenase
Other names:
naphthalene dioxygenase
naphthalene oxygenase
NDO
Systematic name:
naphthalene,NADH:oxygen oxidoreductase (1,2-hydroxylating)

Reaction

Cofactor

Comments:

This enzyme is a member of the ring-hydroxylating dioxygenase (RHD) family of bacterial enzymes that play a critical role in the degradation of aromatic compounds, such as polycyclic aromatic hydrocarbons [5]. This enzyme comprises a multicomponent system, containing a reductase that is an iron-sulfur flavoprotein (FAD; EC 1.18.1.3, ferredoxin—NAD+ reductase), an iron-sulfur oxygenase, and ferredoxin. Requires Fe2+.

Links to other databases

Enzymes and pathways: NC-IUBMB , BRENDA , DIAGRAM , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , UM-BBD , UniPathway
Protein domains and families: PROSITE:PDOC00493
Structural data: CSA , EC2PDB
Gene Ontology: GO:0018625
CAS Registry Number: 9074-04-8
UniProtKB/Swiss-Prot:

References

  1. Ensley, B.D. and Gibson, D.T.
    Naphthalene dioxygenase: purification and properties of a terminal oxygenase component.
    J. Bacteriol. 155: 505-511 (1983). [PMID: 6874638]
  2. Jeffrey, A.M., Yeh, H.J.C., Jerina, D.M., Patel, T.R., Davey, J.F. and Gibson, D.T.
    Initial reactions in the oxidation of naphthalene by Pseudomonas putida.
    Biochemistry 14: 575-584 (1975). [PMID: 234247]
  3. Kauppi, B., Lee, K., Carredano, E., Parales, R.E., Gibson, D.T., Eklund, H. and Ramaswamy, S.
    Structure of an aromatic-ring-hydroxylating dioxygenase-naphthalene 1,2-dioxygenase.
    Structure 6: 571-586 (1998). [PMID: 9634695]
  4. Parales, R.E., Lee, K., Resnick, S.M., Jiang, H., Lessner, D.J. and Gibson, D.T.
    Substrate specificity of naphthalene dioxygenase: effect of specific amino acids at the active site of the enzyme.
    J. Bacteriol. 182: 1641-1649 (2000). [PMID: 10692370]
  5. Jouanneau, Y., Meyer, C., Jakoncic, J., Stojanoff, V. and Gaillard, J.
    Characterization of a naphthalene dioxygenase endowed with an exceptionally broad substrate specificity toward polycyclic aromatic hydrocarbons.
    Biochemistry 45: 12380-12391 (2006). [PMID: 17014090]

[EC 1.14.12.12 created 1992]