KEGG   ENZYME: 1.14.12.12Help
Entry
EC 1.14.12.12               Enzyme                                 

Name naphthalene 1,2-dioxygenase;
naphthalene dioxygenase;
naphthalene oxygenase;
NDO
Class Oxidoreductases;
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 of
oxygen into the other donor
BRITE hierarchy
Sysname naphthalene,NADH:oxygen oxidoreductase (1,2-hydroxylating)
Reaction(IUBMB) naphthalene + NADH + H+ + O2 =
(1R,2S)-1,2-dihydronaphthalene-1,2-diol + NAD+ [RN:R02968]
Reaction(KEGG) R02968;
(other) R05422 R05423 R05424 R05425 R05426 R05427 R06909 R06930
R06937 R07704
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Substrate naphthalene [CPD:C00829];
NADH [CPD:C00004];
H+ [CPD:C00080];
O2 [CPD:C00007]
Product (1R,2S)-1,2-dihydronaphthalene-1,2-diol [CPD:C04314];
NAD+ [CPD:C00003]
Cofactor Iron [CPD:C00023]
Comment 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+.
Pathway PATH: ec00624  1- and 2-Methylnaphthalene degradation
PATH: ec00626  Naphthalene and anthracene degradation
PATH: ec00628  Fluorene degradation
PATH: ec00642  Ethylbenzene degradation
PATH: ec01100  Metabolic pathways
Structures PDB: 1EG9  1NDO  1O7G  1O7H  1O7M  1O7N  1O7P  1O7W  1UUV  1UUW  
     2B1X  2B24  2HMJ  2HMK  2HML  2HMM  2HMN  2HMO  
Reference
  Authors
  Title

  Journal
  Organism
1  [PMID:6874638]
Ensley BD, Gibson DT.
Naphthalene dioxygenase: purification and properties of a terminal
oxygenase component.
J. Bacteriol. 155 (1983) 505-11.
Pseudomonas sp.
Reference
  Authors
  Title

  Journal
  Organism
2  [PMID:234247]
Jeffrey AM, Yeh HJ, Jerina DM, Patel TR, Davey JF, Gibson DT.
Initial reactions in the oxidation of naphthalene by Pseudomonas
putida.
Biochemistry. 14 (1975) 575-84.
Pseudomonas putida
Reference
  Authors

  Title

  Journal
  Organism
3  [PMID:9634695]
Kauppi B, Lee K, Carredano E, Parales RE, Gibson DT, Eklund H,
Ramaswamy S
Structure of an aromatic-ring-hydroxylating dioxygenase-naphthalene
1,2-dioxygenase.
Structure. 6 (1998) 571-86.
Pseudomonas sp.
Reference
  Authors
  Title

  Journal
  Organism
4  [PMID:10692370]
Parales RE, Lee K, Resnick SM, Jiang H, Lessner DJ, Gibson DT
Substrate specificity of naphthalene dioxygenase: effect of specific
amino acids at the active site of the enzyme.
J. Bacteriol. 182 (2000) 1641-9.
Pseudomonas sp.
Reference
  Authors
  Title


  Journal
  Organism
5  [PMID:17014090]
Jouanneau Y, Meyer C, Jakoncic J, Stojanoff V, Gaillard J
Characterization of a naphthalene dioxygenase endowed with an
exceptionally broad substrate specificity toward polycyclic aromatic
hydrocarbons.
Biochemistry. 45 (2006) 12380-91.
Pseudomonas putida
Other DBs ExplorEnz - The Enzyme Database: 1.14.12.12
IUBMB Enzyme Nomenclature: 1.14.12.12
ExPASy - ENZYME nomenclature database: 1.14.12.12
UM-BBD (Biocatalysis/Biodegradation Database): 1.14.12.12
BRENDA, the Enzyme Database: 1.14.12.12
CAS: 9074-04-8

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