IUBMB Enzyme Nomenclature

EC 1.14.12.12

Accepted name: naphthalene 1,2-dioxygenase

Reaction: naphthalene + NADH + H+ + O2 = (1R,2S)-1,2-dihydronaphthalene-1,2-diol + NAD+

For diagram of reaction click here and related reactions click here.

Other name(s): naphthalene dioxygenase; naphthalene oxygenase

Systematic name: naphthalene,NADH:oxygen oxidoreductase (1,2-hydroxylating)

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: BRENDA, EXPASY, KEGG, Metacyc, PDB, UM-BBD, CAS registry number: 9074-04-8

References:

1. Ensley, B.D. and Gibson, D.T. Naphthalene dioxygenase: purification and properties of a terminal oxygenase component. J. Bacteriol. 155 (1983) 505-511. [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 (1975) 575-584. [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 (1998) 571-586. [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 (2000) 1641-1649. [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 (2006) 12380-12391. [PMID: 17014090]

[EC 1.14.12.12 created 1992]


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