Naphthalene 1,2-dioxygenase

naphthalene 1,2-dioxygenase
Identifiers
EC no.	1.14.12.12
CAS no.	9074-04-8
Databases
IntEnz	IntEnz view
BRENDA	BRENDA entry
ExPASy	NiceZyme view
KEGG	KEGG entry
MetaCyc	metabolic pathway
PRIAM	profile
PDB structures	RCSB PDB PDBe PDBsum
Gene Ontology	AmiGO / QuickGO
Search PMC articles PubMed articles NCBI proteins

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

naphthalene + NADH + H⁺ + O₂${\displaystyle \rightleftharpoons }$ (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

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

• 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.