ExplorEnz: EC 1.14.12.12

Your query returned 1 entry. Printable version

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

Other name(s):

naphthalene dioxygenase; naphthalene oxygenase; NDO

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, EAWAG-BBD, EXPASY, Gene, KEGG, MetaCyc, PDB, 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. [DOI] [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. [DOI] [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. [DOI] [PMID: 17014090]

[EC 1.14.12.12 created 1992]