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Naphthalene 1,2-dioxygenase

From Wikipedia, the free encyclopedia
naphthalene 1,2-dioxygenase
Identifiers
EC no.1.14.12.12
CAS no.9074-04-8
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO
Search
PMCarticles
PubMedarticles
NCBIproteins

In enzymology, a naphthalene 1,2-dioxygenase (EC 1.14.12.12) is an enzyme that catalyzes the chemical reaction

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

The 4 substrates of this enzyme are naphthalene, NADH, H+, and O2, whereas its two products are (1R,2S)-1,2-dihydronaphthalene-1,2-diol and NAD+.

This enzyme belongs to the family of oxidoreductases, specifically those acting on paired donors, with O2 as oxidant and incorporation or reduction of oxygen. The oxygen incorporated need not be derived from O2 with NADH or NADPH as one donor, and incorporation of two atoms o oxygen into the other donor. The systematic name of this enzyme class is naphthalene,NADH:oxygen oxidoreductase (1,2-hydroxylating). Other names in common use include naphthalene dioxygenase, and naphthalene oxygenase. This enzyme participates in 4 metabolic pathways: 1- and 2-methylnaphthalene degradation, naphthalene and anthracene degradation, fluorene degradation, and ethylbenzene degradation. It employs one cofactor, iron.

Structural studies

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As of late 2007, 18 structures have been solved for this class of enzymes, with PDB accession codes 1EG9, 1NDO, 1O7G, 1O7H, 1O7M, 1O7N, 1O7P, 1O7W, 1UUV, 1UUW, 2B1X, 2B24, 2HMJ, 2HMK, 2HML, 2HMM, 2HMN, and 2HMO.

References

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  • Ensley BD, Gibson DT (1983). "Naphthalene dioxygenase: purification and properties of a terminal oxygenase component". J. Bacteriol. 155 (2): 505–11. doi:10.1128/JB.155.2.505-511.1983. PMC 217717. PMID 6874638.
  • Jeffrey AM, Yeh HJ, Jerina DM, Patel TR, Davey JF, Gibson DT (1975). "Initial reactions in the oxidation of naphthalene by Pseudomonas putida". Biochemistry. 14 (3): 575–84. doi:10.1021/bi00674a018. PMID 234247.