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Information on EC 1.14.12.12 - naphthalene 1,2-dioxygenase
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1.14.12.12 naphthalene 1,2-dioxygenaseIUBMB 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 . 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+.
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Word Map
- 1.14.12.12
- putida
-
polycyclic
-
bioremediation
-
rieske
- toluene
- phenanthrene
-
dioxygenation
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naphthalene-degrading
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ring-hydroxylating
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dihydroxylation
- indigo
-
pah-degrading
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hydrocarbon-degrading
- dihydrodiols
- cis-dihydrodiols
-
rieske-type
-
oil-contaminated
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cis-dihydroxylation
-
parales
- 2-nitrotoluene
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pah-contaminated
- acenaphthene
-
cis-diols
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side-on
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alpha3beta3
- indene
- synthesis
The enzyme appears in viruses and cellular organisms
Synonyms
naphthalene dioxygenase, nahac, naphthalene 1,2-dioxygenase, naphthalene oxygenase, 
more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
nahAc
naphthalene 1,2-dioxygenase
naphthalene dioxygenase
naphthalene oxygenase
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NDO
oxygenase, naphthalene di-
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naphthalene dioxygenase
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naphthalene dioxygenase
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the enzyme is a three-component dioxygenase complex consisting of ht-PhnI (oxygenase component), ht-PhnA3 (ferredoxin component), and ht-PhnA4 (reductase component)
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
naphthalene + NADH + H+ + O2 = (1R,2S)-1,2-dihydronaphthalene-1,2-diol + NAD+
proposed mechanism
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naphthalene + NADH + H+ + O2 = (1R,2S)-1,2-dihydronaphthalene-1,2-diol + NAD+
proposed electron transport chain: NADH, ferredoxixinNAP reductase, ferredoxinNAP, terminal oxygenase ISPNAP
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naphthalene + NADH + H+ + O2 = (1R,2S)-1,2-dihydronaphthalene-1,2-diol + NAD+
proposed mechanism
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naphthalene + NADH + H+ + O2 = (1R,2S)-1,2-dihydronaphthalene-1,2-diol + NAD+
proposed electron transport chain: NADH, ferredoxixinNAP reductase, ferredoxinNAP, terminal oxygenase ISPNAP
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naphthalene + NADH + H+ + O2 = (1R,2S)-1,2-dihydronaphthalene-1,2-diol + NAD+
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
redox reaction
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reduction
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oxidation
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oxidation
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naphthalene dioxygenase has a relaxed substrate specificity and can oxidize almost 100 substrates, these include the enantiospecific cis-dihydroxylation of polycyclic aromatic hydrocarbons and the olefin groups of benzocycloalkenes, benzylic hydroxylation, N- and O-dealkylation, sulfoxidation and desaturation reactions
oxidation
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naphthalene dioxygenase has a relaxed substrate specificity and can oxidize almost 100 substrates, these include the enantiospecific cis-dihydroxylation of polycyclic aromatic hydrocarbons and the olefin groups of benzocycloalkenes, benzylic hydroxylation, N- and O-dealkylation, sulfoxidation and desaturation reactions
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PATHWAY SOURCE
PATHWAYS
KEGG
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SYSTEMATIC NAME
IUBMB Comments
naphthalene,NADH:oxygen oxidoreductase (1,2-hydroxylating)
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+.
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CAS REGISTRY NUMBER
COMMENTARY
9074-04-8
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(1S)-indanol + NADH + O2
(1S)-indanol + trans-1,3-indandiol
-
recombinant enzyme
85.5% indanol, 11.5% 1,3-indandiol, minor products: (1S)-indenol and 1-indanone
?
(R)-1-indanol + NADH + H+ + O2
cis-1,3-indandiol + (R)-3-hydroxy-1-indanone + cis-1,2,3-indantriol + NAD+
-
activity in E. coli cells expressing recombinant naphthalene dioxygenase
71% cis-1,3-indandiol, 18.2% (R)-3-hydroxy-1-indanone and 10.8% cis-1,2,3-indantriol
?
(S)-1-indanol + NADH + H+ + O2
trans-(1S,3S)-indan-1,3-diol + (R)-3-hydroxy-1-indanone + NAD+
-
activity in E. coli cells expressing recombinant naphthalene dioxygenase
95.5% trans-(1S,3S)-indan-1,3-diol
?
(S)-1-indenol + NADH + O2
syn-2,3-dihydroxy-1-indanol + anti-2,3-dihydroxy-1-indanol
-
recombinant enzyme system
-
?
1,2-dihydronaphthalene + NADH + O2
cis-(1R,2S)-dihydroxy-1,2,3,4-tetrahydronaphthalene + cis-(1R,2S)-dihydroxy-1,2-dihydronaphthalene + NAD+
-
naphthalene dioxygenase activity in cells induced by salicylate
-
?
1-chloronaphthalene + NADH + H+ + O2
(1R,2S)-5-chloro-1,2-dihydronaphthalene-1,2-diol + (1S,2R)-8-chloro-1,2-dihydronaphthalene-1,2-diol + NAD+
1-methylnaphthalene + NADH + H+ + O2
? + NAD+
-
-
generation of dioxygenated product, but mainly formation of side-chain monooxygenated product
-
?
2,3-dihydro-1,4-benzo[d]dithiine + NADH + O2
(S)-2,3-dihydrobenzo[d]dithiin-1-oxide + NAD+
2,3-dimethylnaphthalene + NADH + H+ + O2
? + NAD+
-
-
generation of mono- and mostly dioxygenated products
-
?
2,4,6-trimethylnaphthalene + NADH + H+ + O2
? + NAD+
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generation of mostly mono- and some dioxygenated products
-
?
2-methoxynaphthalene + NADH + O2
(1R,2S)-dihydroxy-7-methoxy-1,2-dihydronaphthalene + NAD+
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naphtalene dioxygenase activity in whole cells and activity in E. coli cells expressing naphtalene dioxygenase
minor product (1R,2S)-dihydroxy-6-methoxy-1,2-dihydronaphthalene
?
2-methyl-1,3-benzodithiole + NADH + O2
(1S,2R)-2-methyl-1,3-benzodithiole-1-oxide + (1S,2S)-2-methyl-1,3-benzodithiole-1-oxide + NAD+
2-methylnaphthalene + NADH + H+ + O2
? + NAD+
-
-
generation of two different dioxygenated products
-
?
2-methylquinoline + NADH + H+ + O2
(5R,6S)-2-methyl-5,6-dihydroquinoline-5,6-diol + 2-methylquinolin-8-ol + NAD+
3 benz[a]anthracene + 3 NADH + 3 O2 + 3 H+
benz[a]anthracene-10,11-cis-dihydrodiol + benz[a]anthracene-8,9-cis-dihydrodiol + benz[a]anthracene-1,2-cis-dihydrodiol + 3 NAD+
-
-
-
-
?
3,4-dihydro-2H-1lambda4,5-benzodithiepin + NADH + O2
(S)-1,2,3,4-tetrahydro-1lambda4,5-benzodithiepin-1-oxide + NAD+
3-methylisoquinoline + NADH + H+ + O2
cis-3-methyl-7,8-dihydroisoquinoline-7,8-diol + 3-methylisoquinolin-5-ol + NAD+
6,7-dihydro-5H-benzocycloheptene + NADH + O2
(1R,2S)-cis-dihydroxybenzocycloheptane + NAD+
-
naphthalene dioxygenase activity in cells induced by salicylate
enantiomeric excess greater than 98%
?
8-methylquinoline + NADH + H+ + O2
5,6-dihydroquinolin-8-ylmethanol + (5R,6S)-8-methyl-5,6-dihydroquinoline-5,6-diol + NAD+
9,10-dihydroanthracene + NADH + O2
cis-(1R,2S)-1,2-dihydroxy-1,2,9,10-tetrahydroanthracene + NAD+
-
naphthalene dioxygenase activity in cells induced by salicylate
more than 95% yield, enantiomeric excess greater than 95%, minor product: 9-hydroxy-9,10-dihydroanthracene
?
9,10-dihydrophenanthrene + NADH + O2
cis-(3S,4R)-3,4-dihydroxy-3,4,9,10-tetrahydrophenanthrene + (S)-9-hydroxy-9,10-dihydrophenanthrene
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naphthalene dioxygenase activity in cells induced by salicylate
70% cis-(3S,4R)-3,4-dihydroxy-3,4,9,10-tetrahydrophenanthrene, enantiomeric excess greater than 95%, 30% (S)-9-hydroxy-9,10-dihydrophenanthrene
?
anthracene + NADH + O2
(1R,2S)-1,2-dihydroanthracene-1,2-diol + (1S,2R)-1,2-dihydroanthracene-1,2-diol + NAD+
benzene + NADH + O2
H2O2 + cis-benzene-1,2-dihydrodiol + NAD+
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40-50% of O2 is reduced to H2O2 by an uncoupling reaction, only trace amounts of cis-benzene-1,2-dihydrodiol are formed
-
?
benzocyclobutene + NADH + O2
benzocyclobutene-1-ol + benzocyclobutene-1-one
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naphtalene dioxygenase activity in intact cells
-
?
benzo[a]pyrene + NADH + H+ + O2
cis-9,10-dihydroxy-9,10-dihydrobenzo[a]pyrene + NAD+
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-
-
?
benzo[rst]dinaphtho[defg,ijkl]pentaphene + NADH + H+ + O2
?
-
-
-
?
benzo[rst]phenanthro[1,10,9-cde]pentaphene + NADH + H+ + O2
?
-
-
-
?
benz[a]anthracene + NADH + H+ + O2
cis,cis-1,2,10,11-tetrahydroxy-1,2,10,11-tetrahydrobenz[a]anthracene + NAD+
-
-
-
-
?
benz[a]anthracene-1,2-cis-dihydrodiol + NADH + O2
benz[a]anthracene-1,2,10,11-bis-cis-dihydrodiol + NAD+
-
-
-
-
?
benz[a]anthracene-10,11-cis-dihydrodiol + NADH + O2
benz[a]anthracene-1,2,10,11-bis-cis-dihydrodiol + NAD+
-
-
-
-
?
chrysene + NADH + H+ + O2
cis-3,4-dihydroxy-3,4-dihydrochrysene + NAD+
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-
-
-
?
chrysene + NADH + O2
chrysene-3,4-cis-dihydrodiol + chrysene-3,4,9,10-bis-cis-dihydrodiol + NAD+
-
-
-
-
?
dibenzofuran + NADH + O2
(1R,2S)-cis-1,2-dihydroxy-1,2-dihydrodibenzofuran + (3S,4R)-cis-3,4-dihydroxy-3,4-dihydrodibenzofuran + NAD+
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naphthalene dioxygenase activity in cells induced by salicylate
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-
?
dibenzothiophene + NADH + H+ + O2
1,2-dihydroxydibenzothiophene + NAD+
-
-
-
-
?
dibenzothiophene + NADH + O2
(1R,2S)-cis-1,2-dihydroxy-dihydrodibenzothiophene + dibenzothiophene sulfoxide
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naphthalene dioxygenase activity in cells induced by salicylate
84-87% (1R,2S)-cis-1,2-dihydroxy-dihydrodibenzothiophene, enantiomeric excess greater than 95%, 15% dibenzothiophene sulfoxide
?
fluoranthene + NADH + H+ + O2
cis-7,8-dihydroxy-7,8-dihydrofluoranthene + cis-2,3-dihydroxy-2,3-dihydrofluoranthene + NAD+
-
-
-
-
?
fluorene + NADH + O2
(3S,4R)-cis-3,4dihydroxy-3,4-dihydrofluorene + 9-fluorenol + NAD+
-
naphthalene dioxygenase activity in cells induced by salicylate
-
-
?
indan + NADH + H+ + O2
(1S)-indenol + (1S)-indanol + NAD+
-
recombinant enzyme, enantiospecific monooxygenation
20% indenol, 67.1% indanol, minor products: indene, 1-indanone and (1R,2S)-indandiol
?
indene + NADH + O2
(1S)-indenol + (1R,2S)-indandiol + NAD+
-
recombinant enzyme
57.9% indenol, 29.6% indandiol
?
indole + NADH + H+ + O2
cis-indole-2,3-dihydrodiol + NAD+
-
-
-
?
phenanthrene + NADH + O2
(1R,2S)-1,2-dihydrophenanthrene-1,2-diol + (1S,2R)-1,2-dihydrophenanthrene-1,2-diol + (3R,4S)-3,4-dihydrophenanthrene-3,4-diol + (3S,4R)-3,4-dihydrophenanthrene-3,4-diol + NAD+
phenetole + NADH + H+ + O2
phenol + vinyloxybenzene + (S)-ethylphenyl sulfoxide + NAD+
-
-
-
?
quinoxaline + NADH + H+ + O2
(5R,6S)-5,6-dihydroquinoxaline-5,6-diol + NAD+
-
-
exclusive product
-
?
styrene + NADH + H+ + O2
(R)-1-phenylethane-1,2-diol + (S)-1-phenylethane-1,2-diol + NAD+
-
-
-
?
styrene + NADH + O2
(R)-1-phenyl-1,2-ethanediol + NAD+
-
recombinant enzyme system
78.6% enantiomeric excess
?
(2S)-flavanone + NADH + H+ + O2
8-hydroxy-(2S)-flavanone + NAD+ + ?
-
no substrate for wild-type, substrate for mutants F224C, F224K, F224Q, F224Y
product has an oxygen atom directly attached to the aromatic ring. Upon completion of the dihydroxylation, the oxygen atom on the C-ring is believed to expel the 7-OH group through donation of its lone pair electrons and the charged intermediate. Once formed this readily re-aromatizes to provide 8-hydroxyflavanones or 8-hydroxyisoflavanones
-
?
(2S)-flavanone + NADH + H+ + O2
8-hydroxy-(2S)-flavanone + NAD+ + ?
-
no substrate for wild-type, substrate for mutants F224C, F224K, F224Q, F224Y
product has an oxygen atom directly attached to the aromatic ring. Upon completion of the dihydroxylation, the oxygen atom on the C-ring is believed to expel the 7-OH group through donation of its lone pair electrons and the charged intermediate. Once formed this readily re-aromatizes to provide 8-hydroxyflavanones or 8-hydroxyisoflavanones
-
?
(3S)-isoflavanone + NADH + H+ + O2
8-hydroxy-(3S)-isoflavanone + NAD+ + ?
-
no substrate for wild-type, substrate for mutants F224K, F224Y
product has an oxygen atom directly attached to the aromatic ring. Upon completion of the dihydroxylation, the oxygen atom on the C-ring is believed to expel the 7-OH group through donation of its lone pair electrons and the charged intermediate. Once formed this readily re-aromatizes to provide 8-hydroxyflavanones or 8-hydroxyisoflavanones
-
?
(3S)-isoflavanone + NADH + H+ + O2
8-hydroxy-(3S)-isoflavanone + NAD+ + ?
-
no substrate for wild-type, substrate for mutants F224K, F224Y
product has an oxygen atom directly attached to the aromatic ring. Upon completion of the dihydroxylation, the oxygen atom on the C-ring is believed to expel the 7-OH group through donation of its lone pair electrons and the charged intermediate. Once formed this readily re-aromatizes to provide 8-hydroxyflavanones or 8-hydroxyisoflavanones
-
?
1,2,4-trimethylnaphthalene + NADH + H+ + O2
? + NAD+
-
-
generation of mono- and dioxygenated products
-
?
1,2,4-trimethylnaphthalene + NADH + H+ + O2
? + NAD+
-
-
generation of mono- and dioxygenated products
-
?
1,2,5-trimethylnaphthalene + NADH + H+ + O2
? + NAD+
-
-
generation of mostly mono- and some dioxygenated products
-
?
1,2,5-trimethylnaphthalene + NADH + H+ + O2
? + NAD+
-
-
generation of mostly mono- and some dioxygenated products
-
?
1,3-benzodithiole + NADH + O2
(R)-1,3-benzodithiole-1-oxide + NAD+
-
-
-
-
?
1,3-benzodithiole + NADH + O2
(R)-1,3-benzodithiole-1-oxide + NAD+
-
-
-
-
?
1,4-benzo[d]dithiine + NADH + O2
(S)-1,4-benzo[d]dithiin-1-oxide + NAD+
-
-
-
-
?
1,4-benzo[d]dithiine + NADH + O2
(S)-1,4-benzo[d]dithiin-1-oxide + NAD+
-
-
-
-
?
1,4-dimethylnaphthalene + NADH + H+ + O2
? + NAD+
-
-
generation of monooxygenated products
-
?
1,4-dimethylnaphthalene + NADH + H+ + O2
? + NAD+
-
-
generation of monooxygenated products
-
?
1,5-dimethylnaphthalene + NADH + H+ + O2
? + NAD+
-
-
generation of monooxygenated products
-
?
1,5-dimethylnaphthalene + NADH + H+ + O2
? + NAD+
-
-
generation of monooxygenated products
-
?
1-chloronaphthalene + NADH + H+ + O2
(1R,2S)-5-chloro-1,2-dihydronaphthalene-1,2-diol + (1S,2R)-8-chloro-1,2-dihydronaphthalene-1,2-diol + NAD+
-
-
-
?
1-chloronaphthalene + NADH + H+ + O2
(1R,2S)-5-chloro-1,2-dihydronaphthalene-1,2-diol + (1S,2R)-8-chloro-1,2-dihydronaphthalene-1,2-diol + NAD+
-
-
-
?
2,3-dihydro-1,4-benzo[d]dithiine + NADH + O2
(S)-2,3-dihydrobenzo[d]dithiin-1-oxide + NAD+
-
-
-
-
?
2,3-dihydro-1,4-benzo[d]dithiine + NADH + O2
(S)-2,3-dihydrobenzo[d]dithiin-1-oxide + NAD+
-
-
-
-
?
2-chlorobiphenyl + NADH + O2
2-chloro-2',3'-dihydrobiphenyl-2',3'-diol + NAD+
-
recombinant histidine-tagged terminal dioxygenase
-
?
2-chlorobiphenyl + NADH + O2
2-chloro-2',3'-dihydrobiphenyl-2',3'-diol + NAD+
-
recombinant histidine-tagged terminal dioxygenase
-
?
2-methyl-1,3-benzodithiole + NADH + O2
(1S,2R)-2-methyl-1,3-benzodithiole-1-oxide + (1S,2S)-2-methyl-1,3-benzodithiole-1-oxide + NAD+
-
-
cis and trans product
-
?
2-methyl-1,3-benzodithiole + NADH + O2
(1S,2R)-2-methyl-1,3-benzodithiole-1-oxide + (1S,2S)-2-methyl-1,3-benzodithiole-1-oxide + NAD+
-
-
cis and trans product
-
?
2-methylquinoline + NADH + H+ + O2
(5R,6S)-2-methyl-5,6-dihydroquinoline-5,6-diol + 2-methylquinolin-8-ol + NAD+
-
-
99% total conversion, giving 92% (5R,6S)-2-methyl-5,6-dihydroquinoline-5,6-diol and 8% 2-methylquinolin-8-ol
-
?
2-methylquinoline + NADH + H+ + O2
(5R,6S)-2-methyl-5,6-dihydroquinoline-5,6-diol + 2-methylquinolin-8-ol + NAD+
-
-
99% total conversion, giving 92% (5R,6S)-2-methyl-5,6-dihydroquinoline-5,6-diol and 8% 2-methylquinolin-8-ol
-
?
3,4-dihydro-2H-1lambda4,5-benzodithiepin + NADH + O2
(S)-1,2,3,4-tetrahydro-1lambda4,5-benzodithiepin-1-oxide + NAD+
-
-
-
-
?
3,4-dihydro-2H-1lambda4,5-benzodithiepin + NADH + O2
(S)-1,2,3,4-tetrahydro-1lambda4,5-benzodithiepin-1-oxide + NAD+
-
-
-
-
?
3-chlorobiphenyl + NADH + O2
3-chloro-2',3'-dihydrobiphenyl-2',3'-diol + NAD+
-
recombinant histidine-tagged terminal dioxygenase
-
?
3-chlorobiphenyl + NADH + O2
3-chloro-2',3'-dihydrobiphenyl-2',3'-diol + NAD+
-
recombinant histidine-tagged terminal dioxygenase
-
?
3-chlorophenol + NADH + O2
chlorohydroquinone + 4-chlorocatechol + NAD+
-
-
-
-
?
3-chlorophenol + NADH + O2
chlorohydroquinone + 4-chlorocatechol + NAD+
-
-
-
-
?
3-methylisoquinoline + NADH + H+ + O2
cis-3-methyl-7,8-dihydroisoquinoline-7,8-diol + 3-methylisoquinolin-5-ol + NAD+
-
-
99% total conversion, giving 73% cis-3-methyl-7,8-dihydroisoquinoline-7,8-diol + 27% 3-methylisoquinolin-5-ol
-
?
3-methylisoquinoline + NADH + H+ + O2
cis-3-methyl-7,8-dihydroisoquinoline-7,8-diol + 3-methylisoquinolin-5-ol + NAD+
-
-
99% total conversion, giving 73% cis-3-methyl-7,8-dihydroisoquinoline-7,8-diol + 27% 3-methylisoquinolin-5-ol
-
?
3-nitrotoluene + NADH + O2
4-nitrobenzyl alcohol + NAD+
-
-
-
-
?
4-chlorobiphenyl + NADH + O2
4-chloro-2',3'-dihydrobiphenyl-2',3'-diol + NAD+
-
recombinant histidine-tagged terminal dioxygenase
-
?
4-chlorobiphenyl + NADH + O2
4-chloro-2',3'-dihydrobiphenyl-2',3'-diol + NAD+
-
recombinant histidine-tagged terminal dioxygenase
-
?
8-methylquinoline + NADH + H+ + O2
5,6-dihydroquinolin-8-ylmethanol + (5R,6S)-8-methyl-5,6-dihydroquinoline-5,6-diol + NAD+
-
-
78% total conversion, giving 72% 5,6-dihydroquinolin-8-ylmethanol + 28% (5R,6S)-8-methyl-5,6-dihydroquinoline-5,6-diol
-
?
8-methylquinoline + NADH + H+ + O2
5,6-dihydroquinolin-8-ylmethanol + (5R,6S)-8-methyl-5,6-dihydroquinoline-5,6-diol + NAD+
-
-
78% total conversion, giving 72% 5,6-dihydroquinolin-8-ylmethanol + 28% (5R,6S)-8-methyl-5,6-dihydroquinoline-5,6-diol
-
?
anthracene + NADH + O2
(1R,2S)-1,2-dihydroanthracene-1,2-diol + (1S,2R)-1,2-dihydroanthracene-1,2-diol + NAD+
-
-
-
-
?
anthracene + NADH + O2
(1R,2S)-1,2-dihydroanthracene-1,2-diol + (1S,2R)-1,2-dihydroanthracene-1,2-diol + NAD+
-
-
-
-
?
ethylbenzene + NADH + H+ + O2
(S)-1-phenylethanol + (R)-1-phenylethanol + NAD+
-
-
-
?
ethylbenzene + NADH + H+ + O2
(S)-1-phenylethanol + (R)-1-phenylethanol + NAD+
-
-
-
?
ethylphenyl sulfide + NADH + H+ + O2
(R)-ethylphenyl sulfoxide + NAD+
-
-
-
?
ethylphenyl sulfide + NADH + H+ + O2
(R)-ethylphenyl sulfoxide + NAD+
-
-
-
?
indole + ? + O2
cis-indole-2,3-dihydrodiol
-
reaction of recombinant E. coli transformed with Pseudomonas sp. DNA
-
?
indole + ? + O2
cis-indole-2,3-dihydrodiol
-
reaction of recombinant E. coli transformed with Pseudomonas sp. DNA
-
?
indole + NADH + O2
(2S,3S)-2,3-dihydro-1H-indole-2,3-diol + NAD+
-
-
-
-
?
indole + NADH + O2
(2S,3S)-2,3-dihydro-1H-indole-2,3-diol + NAD+
-
-
-
-
?
m-cresol + NADH + O2
methylhydroquinone + 3-methylcatechol + 4-methylcatechol + NAD+
-
-
-
-
?
m-cresol + NADH + O2
methylhydroquinone + 3-methylcatechol + 4-methylcatechol + NAD+
-
-
-
-
?
naphthalene + NAD(P)H + O2
cis-(1R,2S)-1,2-dihydronaphthalene-1,2-diol + NAD(P)+
-
-
only cis-isomer by bacteria, product rapidly autooxidizes to 1,2-naphthoquinone
?
naphthalene + NAD(P)H + O2
cis-(1R,2S)-1,2-dihydronaphthalene-1,2-diol + NAD(P)+
-
-
only cis-isomer by bacteria, product rapidly autooxidizes to 1,2-naphthoquinone
?
naphthalene + NAD(P)H + O2
cis-(1R,2S)-1,2-dihydronaphthalene-1,2-diol + NAD(P)+
-
-
-
-
?
naphthalene + NAD(P)H + O2
cis-(1R,2S)-1,2-dihydronaphthalene-1,2-diol + NAD(P)+
-
50% activity with NADH compared to NADPH
-
-
?
naphthalene + NAD(P)H + O2
cis-(1R,2S)-1,2-dihydronaphthalene-1,2-diol + NAD(P)+
-
-
-
-
?
naphthalene + NAD(P)H + O2
cis-(1R,2S)-1,2-dihydronaphthalene-1,2-diol + NAD(P)+
-
-
-
?
naphthalene + NAD(P)H + O2
cis-(1R,2S)-1,2-dihydronaphthalene-1,2-diol + NAD(P)+
-
-
-
?
naphthalene + NADH + H+ + O2
(1R,2S)-1,2-dihydronaphthalene-1,2-diol + NAD+
-
-
-
-
?
naphthalene + NADH + H+ + O2
(1R,2S)-1,2-dihydronaphthalene-1,2-diol + NAD+
-
-
-
?
naphthalene + NADH + H+ + O2
(1R,2S)-1,2-dihydronaphthalene-1,2-diol + NAD+
-
-
-
-
?
naphthalene + NADH + H+ + O2
(1R,2S)-1,2-dihydronaphthalene-1,2-diol + NAD+
-
-
-
?
naphthalene + NADH + H+ + O2
(1R,2S)-1,2-dihydronaphthalene-1,2-diol + NAD+
-
-
-
?
naphthalene + NADH + H+ + O2
(1R,2S)-1,2-dihydronaphthalene-1,2-diol + NAD+
-
-
-
-
?
naphthalene + NADH + H+ + O2
(1R,2S)-1,2-dihydronaphthalene-1,2-diol + NAD+
-
-
-
-
?
naphthalene + NADH + H+ + O2
(1R,2S)-1,2-dihydronaphthalene-1,2-diol + NAD+
-
-
-
?
naphthalene + NADH + H+ + O2
(1R,2S)-1,2-dihydronaphthalene-1,2-diol + NAD+
-
the catalytic ferrous site is primed for the O2 reaction when substrate is bound in the active site in the presence of the reduced Rieske site. These structural changes ensure that two electrons and the substrate are present before the binding and activation of O2, which avoids the uncontrolled formation and release of reactive oxygen species
-
-
?
naphthalene + NADH + H+ + O2
(1R,2S)-1,2-dihydronaphthalene-1,2-diol + NAD+
-
-
-
?
naphthalene + NADH + H+ + O2
(1R,2S)-1,2-dihydronaphthalene-1,2-diol + NAD+
-
-
-
-
?
naphthalene + NADH + H+ + O2
(1R,2S)-1,2-dihydronaphthalene-1,2-diol + NAD+
-
-
exclusive product
-
?
naphthalene + NADH + H+ + O2
(1R,2S)-1,2-dihydronaphthalene-1,2-diol + NAD+
-
-
exclusive product
-
?
naphthalene + NADH + H+ + O2
(1R,2S)-1,2-dihydronaphthalene-1,2-diol + NAD+
-
-
-
-
?
naphthalene + NADH + H+ + O2
1,2-dihydronaphthalene-1,2-diol + NAD+
-
-
-
-
?
naphthalene + NADH + H+ + O2
1,2-dihydronaphthalene-1,2-diol + NAD+
-
-
-
-
?
naphthalene + NADH + O2
(1R,2S)-1,2-dihydronaphthalene-1,2-diol + NAD+
-
initial oxidative reaction in bacterial naphthalene catabolism
-
?
naphthalene + NADH + O2
(1R,2S)-1,2-dihydronaphthalene-1,2-diol + NAD+
-
initial oxidative reaction in bacterial naphthalene catabolism
-
?
naphthalene + NADH + O2
(1R,2S)-1,2-dihydronaphthalene-1,2-diol + NAD+
-
-
-
?
naphthalene + NADH + O2
(1R,2S)-1,2-dihydronaphthalene-1,2-diol + NAD+
-
-
-
?
naphthalene + NADH + O2
(1R,2S)-1,2-dihydronaphthalene-1,2-diol + NAD+
-
-
-
-
?
naphthalene + NADH + O2
(1R,2S)-1,2-dihydronaphthalene-1,2-diol + NAD+
-
initial oxidative reaction in bacterial naphthalene catabolism
-
?
naphthalene + NADH + O2
(1R,2S)-1,2-dihydronaphthalene-1,2-diol + NAD+
-
three-component dioxygenase, uses two proteins containing three redox centers to transfer electrons to the terminal oxygenase
-
?
naphthalene + NADH + O2
(1R,2S)-1,2-dihydronaphthalene-1,2-diol + NAD+
-
genes coding for naphthalene dioxygenase: ndoA, ndoB and ndoC
-
?
naphthalene + NADH + O2
(1R,2S)-1,2-dihydronaphthalene-1,2-diol + NAD+
-
-
-
?
naphthalene + NADH + O2
(1R,2S)-1,2-dihydronaphthalene-1,2-diol + NAD+
-
-
-
-
?
naphthalene + NADH + O2
(1R,2S)-1,2-dihydronaphthalene-1,2-diol + NAD+
-
-
-
-
?
naphthalene + NADH + O2
(1R,2S)-1,2-dihydronaphthalene-1,2-diol + NAD+
-
-
-
-
?
naphthalene + NADH + O2
(1R,2S)-1,2-dihydronaphthalene-1,2-diol + NAD+
-
-
-
-
?
naphthalene + NADH + O2
cis-(1R,2S)-1,2-dihydronaphthalene-1,2-diol + NAD+
-
-
-
?
naphthalene + NADH + O2
cis-(1R,2S)-1,2-dihydronaphthalene-1,2-diol + NAD+
-
-
-
?
naphthalene + NADH + O2
cis-(1R,2S)-1,2-dihydronaphthalene-1,2-diol + NAD+
-
-
-
?
naphthalene + NADH + O2
cis-(1R,2S)-1,2-dihydronaphthalene-1,2-diol + NAD+
-
-
-
?
naphthalene + NADH + O2
cis-(1R,2S)-1,2-dihydronaphthalene-1,2-diol + NAD+
-
-
-
?
naphthalene + NADH + O2
cis-(1R,2S)-1,2-dihydronaphthalene-1,2-diol + NAD+
-
-
-
?
naphthalene + NADH + O2
cis-(1R,2S)-1,2-dihydronaphthalene-1,2-diol + NAD+
-
3 component enzyme system consisting of ferredoxinNAP reductase, ferredoxinNAP and oxygenase ISPNAP, ferredoxinNAP reductase reduces: 2,6-dichlorophenolindophenol, ferricyanide, nitro blue tetrazolium and cytochrome c, in the presence of FAD ferredoxinNAP reductase transfers electrons to ferredoxin
-
?
naphthalene + NADH + O2
cis-(1R,2S)-1,2-dihydronaphthalene-1,2-diol + NAD+
-
-
-
?
phenanthrene + NADH + O2
(1R,2S)-1,2-dihydrophenanthrene-1,2-diol + (1S,2R)-1,2-dihydrophenanthrene-1,2-diol + (3R,4S)-3,4-dihydrophenanthrene-3,4-diol + (3S,4R)-3,4-dihydrophenanthrene-3,4-diol + NAD+
-
-
-
-
?
phenanthrene + NADH + O2
(1R,2S)-1,2-dihydrophenanthrene-1,2-diol + (1S,2R)-1,2-dihydrophenanthrene-1,2-diol + (3R,4S)-3,4-dihydrophenanthrene-3,4-diol + (3S,4R)-3,4-dihydrophenanthrene-3,4-diol + NAD+
-
-
-
-
?
pyrene + NADH + H+ + O2
pyrene cis-4,5-dihydrodiol + NAD+
-
poor substrate
-
-
?
quinazoline + NADH + H+ + O2
(5R,6S)-5,6-dihydroquinazoline-5,6-diol + quinazolin-8-ol
-
-
99% total conversion, givng 56% (5R,6S)-5,6-dihydroquinazoline-5,6-diol + 43% quinazolin-8-ol
-
?
quinazoline + NADH + H+ + O2
(5R,6S)-5,6-dihydroquinazoline-5,6-diol + quinazolin-8-ol
-
-
99% total conversion, givng 56% (5R,6S)-5,6-dihydroquinazoline-5,6-diol + 43% quinazolin-8-ol
-
?
quinoline + NADH + H+ + O2
(5R,6S)-5,6-dihydroquinoline-5,6-diol + quinolin-3-ol + NAD+
-
-
66% total conversion, giving 55% (5R,6S)-5,6-dihydroquinoline-5,6-diol and 35% quinolin-3-ol
-
?
quinoline + NADH + H+ + O2
(5R,6S)-5,6-dihydroquinoline-5,6-diol + quinolin-3-ol + NAD+
-
-
66% total conversion, giving 55% (5R,6S)-5,6-dihydroquinoline-5,6-diol and 35% quinolin-3-ol
-
?
additional information
?
-
-
the enzyme is responsible for the initial catabolic reactions onto naphthothiophenes and dibenzothiophene
-
-
?
additional information
?
-
-
biotransformation of 2-pyridone- and 2-quinolone-derived compounds by recombinant whole-cells of Escherichia coli JM109(DE3)(pDTG141) expressing the naphthalene-dioxygenase system from Pseudomonas sp. NCIB 9816-4, using a series of N- and C-substituted derivatives. Among them, only the N-methyl substituted compounds are good substrates for a regio- and stereoselective dihydroxylation reaction leading to cis-dihydroxydihydro pyridone derivatives
-
-
?
additional information
?
-
-
the enzyme is responsible for the initial catabolic reactions onto naphthothiophenes and dibenzothiophene
-
-
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
naphthalene + NADH + H+ + O2
(1R,2S)-1,2-dihydronaphthalene-1,2-diol + NAD+
-
-
-
-
?
naphthalene + NADH + H+ + O2
(1R,2S)-1,2-dihydronaphthalene-1,2-diol + NAD+
-
-
-
?
naphthalene + NADH + H+ + O2
(1R,2S)-1,2-dihydronaphthalene-1,2-diol + NAD+
-
-
-
-
?
naphthalene + NADH + H+ + O2
(1R,2S)-1,2-dihydronaphthalene-1,2-diol + NAD+
-
-
-
?
naphthalene + NADH + H+ + O2
(1R,2S)-1,2-dihydronaphthalene-1,2-diol + NAD+
-
-
-
?
naphthalene + NADH + H+ + O2
(1R,2S)-1,2-dihydronaphthalene-1,2-diol + NAD+
-
-
-
-
?
naphthalene + NADH + H+ + O2
(1R,2S)-1,2-dihydronaphthalene-1,2-diol + NAD+
-
-
-
-
?
naphthalene + NADH + H+ + O2
(1R,2S)-1,2-dihydronaphthalene-1,2-diol + NAD+
-
-
-
?
naphthalene + NADH + H+ + O2
(1R,2S)-1,2-dihydronaphthalene-1,2-diol + NAD+
-
-
-
?
naphthalene + NADH + H+ + O2
(1R,2S)-1,2-dihydronaphthalene-1,2-diol + NAD+
-
-
-
-
?
naphthalene + NADH + O2
(1R,2S)-1,2-dihydronaphthalene-1,2-diol + NAD+
-
initial oxidative reaction in bacterial naphthalene catabolism
-
?
naphthalene + NADH + O2
(1R,2S)-1,2-dihydronaphthalene-1,2-diol + NAD+
-
initial oxidative reaction in bacterial naphthalene catabolism
-
?
naphthalene + NADH + O2
(1R,2S)-1,2-dihydronaphthalene-1,2-diol + NAD+
-
-
-
?
naphthalene + NADH + O2
(1R,2S)-1,2-dihydronaphthalene-1,2-diol + NAD+
-
-
-
?
naphthalene + NADH + O2
(1R,2S)-1,2-dihydronaphthalene-1,2-diol + NAD+
-
initial oxidative reaction in bacterial naphthalene catabolism
-
?
naphthalene + NADH + O2
(1R,2S)-1,2-dihydronaphthalene-1,2-diol + NAD+
-
three-component dioxygenase, uses two proteins containing three redox centers to transfer electrons to the terminal oxygenase
-
?
naphthalene + NADH + O2
(1R,2S)-1,2-dihydronaphthalene-1,2-diol + NAD+
-
genes coding for naphthalene dioxygenase: ndoA, ndoB and ndoC
-
?
naphthalene + NADH + O2
(1R,2S)-1,2-dihydronaphthalene-1,2-diol + NAD+
-
-
-
?
additional information
?
-
-
the enzyme is responsible for the initial catabolic reactions onto naphthothiophenes and dibenzothiophene
-
-
?
additional information
?
-
-
the enzyme is responsible for the initial catabolic reactions onto naphthothiophenes and dibenzothiophene
-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
FAD
-
component A, ferredoxinNAP reductase is a flavoprotein, enzyme can use both FAD and FMN but exhibits slightly higher affinity for FAD
FAD
-
addition enhances ferredoxinNAP reductase activity with all in vitro electron-acceptors, e.g. cytochrome c, 2,6-dichlorophenolindophenol, Nitroblue tetrazolium and ferricyanide
FMN
-
requirement, ferredoxinNAP reductase is a flavoprotein, enzyme can use both FAD and FMN but exhibits slightly higher affinity for FAD, addition stimulates dioxygenase activity by 53% of FAD-stimulation
NADH
-
requirement, the oxygenase accepts two electrons from NADH, the reduction requires component A and C as mediators
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Fe2+
Iron
additional information
-
no significant activation by the addition of Fe2+, Fe3+, Zn2+, Mg2+ or Cu2+
Fe2+
-
alpha subunit of terminal oxygenase ISPNAP contains a Rieske [2Fe-2S] center in one domain and a mono-nuclear iron in the catalytic domain
Fe2+
-
component A, i.e. NADH-ferredoxinNAP reductase, of the multienzyme system is an iron-containing flavoprotein containing 1.8 g-atoms Fe2+ and 2 g-atoms sulfur
Fe2+
-
component B, the terminal oxygenase ISPNAP is an iron-sulfur protein, oxidized ISPNAP binds naphthalene without conformational changes that affect its FeS-chromophores, ISPNAP contains 6 g-atom Fe2+ and 4 g-atom acid-labile sulfur per mol enzyme, the enzyme complex is not stimulated by exogenous Fe2+
Fe2+
-
terminal dioxygenase ISPNAR may be a Rieske-type iron-sulfur protein containing 2.4 g-atoms of iron and 2.1 g-atoms of sulfur per alpha,beta subunit
Fe2+
-
the iron content of the oxygenase component ht-PhnI varies between 1.73 and 2.55 Fe atoms per pair of subunits depending on preparation, preincubation of ht-PhnI with ferrous ions under reducing conditions prior to enzyme assay results in a marginal increase of activity, the iron content of the ferredoxin component ht-PhnA3 is estimated to be 1.5 mol/mol of ferredoxin
Iron
-
in the presence of the aromatic substrate indole, nitric oxide is bound end-on to the active-site mononuclear iron of NDO
Iron
-
a molecular oxygen species is bound to the mononuclear iron in a side-on fashion
Iron
-
the catalytic ferrous site is primed for the O2 reaction when substrate is bound in the active site in the presence of the reduced Rieske site. These structural changes ensure that two electrons and the substrate are present before the binding and activation of O2, which avoids the uncontrolled formation and release of reactive oxygen species
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
4-chloromercuribenzoate
-
0.0005 mM, 94% inhibition of ferredoxinNAP reductase
H2O2
-
0.4 mM, complete inactivation of reduced terminal dioxygenase ISPNAP after 10 min in the absence of ferrous iron
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
ferricyanide
-
activation, direct reduction by reductaseNAP in the presence of NADH in vitro
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.00042
biphenyl
-
at 30°C in reaction mixtures containing 0.00013 mM ht-PhnI and 0.5 mM NADH in 50 mM potassium phosphate buffer, pH 7.0
0.00092
Naphthalene
-
at 30°C in reaction mixtures containing 0.00013 mM ht-PhnI and 0.5 mM NADH in 50 mM potassium phosphate buffer, pH 7.0
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1.01
biphenyl
-
at 30°C in reaction mixtures containing 0.00013 mM ht-PhnI and 0.5 mM NADH in 50 mM potassium phosphate buffer, pH 7.0
1.82
Naphthalene
-
at 30°C in reaction mixtures containing 0.00013 mM ht-PhnI and 0.5 mM NADH in 50 mM potassium phosphate buffer, pH 7.0
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
1.37
-
in the presence of partially purified components A and C of the 3 component enzyme system plus FAD
additional information
-
0.000125 mM/min/mg dry cell weight, naphthalene dioxygenase activity in cells grown on succinate in the presence of naphthalene as inducer
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
large alpha subunit and small beta subunit
UniProt
brenda
-
437842, 439081, 439083, 439084, 439085, 439087, 658492, 660501, 673725, 674304, 695702, 724086, 726479
-
-
brenda
NCIB 9816-4. Enzyme is recombinantly expressed in Escherichia coli
-
-
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
metabolism
-
the naphthalene dioxygenase system can develop the capacity of plants to tolerate a high concentration of phenanthrene and metabolize phenanthrene in vivo
physiological function
electron transfer subunit TmoF stimulates T4MO activity two- to threefold when coexpressed in Escherichia coli or Pseudomonas putida. The reductase component of the naphthalene dioxygenase system, encoded by the nahA gene of plasmid NAH7 from Pseudomonas putida G7, can largely replace the TmoF protein in stimulating T4MO activity, and TmoF can partially replace the NahA protein in forming active naphthalene dioxygenase
Show AA Sequence and Transmembrane Helices (153 entries)
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
20000
25000
-
x * 53000 + x * 25000, histidine-tagged recombinant enzyme, SDS-PAGE
37000
52000
-
3 * 52000, 3 * 20000, alpha3beta3 hexamer, oxygenase component, SDS-PAGE
53000
-
x * 53000 + x * 25000, histidine-tagged recombinant enzyme, SDS-PAGE
55000
additional information
20000
-
alpha2beta2 2 * 55000 + 2 * 20000, terminal oxygenase ISPNAP, SDS-PAGE
20000
-
3 * 52000, 3 * 20000, alpha3beta3 hexamer, oxygenase component, SDS-PAGE
55000
-
alpha2beta2 2 * 55000 + 2 * 20000, terminal oxygenase ISPNAP, SDS-PAGE
additional information
-
three component enzyme system consisting of: component A, i.e. ferredoxinNAP reductase, component B, i.e. terminal oxygenase ISPNAP, and component C, i.e. ferredoxinNAP
additional information
-
three component enzyme system consisting of: component A, i.e. ferredoxinNAP reductase, component B, i.e. terminal oxygenase ISPNAP, and component C, i.e. ferredoxinNAP
additional information
-
three component enzyme system consisting of: component A, i.e. ferredoxinNAP reductase, component B, i.e. terminal oxygenase ISPNAP, and component C, i.e. ferredoxinNAP
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hexamer
monomer
tetramer
additional information
hexamer
-
3 * 52000, 3 * 20000, alpha3beta3 hexamer, oxygenase component, SDS-PAGE
tetramer
-
alpha2beta2 2 * 55000 + 2 * 20000, terminal oxygenase ISPNAP, SDS-PAGE
tetramer
-
alpha2beta2 2 * 55000 + 2 * 20000, terminal oxygenase ISPNAP, SDS-PAGE
-
additional information
-
X-ray structure data from Pseudomonas sp. 9861-4 suggest an alpha3,beta3 hexameric structure
additional information
-
X-ray structure data from Pseudomonas sp. 9861-4 suggest an alpha3,beta3 hexameric structure
-
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystallized at 8°C using the vapor-diffusion method with a reservoir solution of 2 M (NH4)2SO4 and 2-3% dioxane in 50 mM 2-morpholinoethanesulfonic acid, pH 6.0
-
hanging drop vapor diffusion method, using 1.9-2.2 M ammonium sulfate, 4-6% (w/v) dioxane, 100 mM MES, pH 5.0-5.8
modeling of structure with naphthalene bound at the active site. The mononuclear iron is coordinated by amino acid residues His208, His213, and Asp362 and a dioxygen molecule is bound in a side-on fashion. The substrate, naphthalene, is found 2.7 to 3.0 A below the dioxygen molecule and is confined in a small substrate binding site which is surrounded by several hydrophobic residues. The amino acid residues with aromatic side chains, including Phe224, Phe202, Phe352, Trp358, and His295 form a small, but rigid, substrate binding site
-
vapor diffusion, equal volume of enzyme solution, 30 mg/ml, and reservoir solution, 2 M ammonium sulfate, 2-3% dioxane in 50 mM Mes, pH 6.0, mixed on a cover slip, deep red crystals, refinement of X-ray structure at 2.25 A resolution
-
hanging drop vapour diffusion method using 2-methyl-2,4-pentanediol as a precipitant
-
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
D362A
-
mutation in alpha subunit of terminal dioxygenase ISPNAP, no activity with naphthalene, biphenyl and phenanthrene
F202L
-
mutation in alpha subunit of terminal dioxygenase ISPNAP, no activity with naphthalene, biphenyl and phenanthrene
F202V
-
mutation in alpha subunit of terminal dioxygenase ISPNAP, similar activity with naphthalene, biphenyl and phenanthrene as wild-type
F352L
-
mutation in alpha subunit of terminal dioxygenase ISPNAP, similar activity with naphthalene, biphenyl and phenanthrene as wild-type, major product of biphenyl oxidation: biphenyl-3,4-dihydrodiol instead of biphenyl-2,3-dihydrodiol
F352V
M366W
-
mutation in alpha subunit of terminal dioxygenase ISPNAP, similar activity with naphthalene, biphenyl and phenanthrene as wild-type
N201A
-
mutation in alpha subunit of terminal dioxygenase ISPNAP, similar activity with naphthalene as wild-type, very weak activity with biphenyl
N201Q
-
mutation in alpha subunit of terminal dioxygenase ISPNAP, similar activity with naphthalene, biphenyl and phenanthrene as wild-type
N201S
-
mutation in alpha subunit of terminal dioxygenase ISPNAP, similar activity with naphthalene, biphenyl and phenanthrene as wild-type
T351N
-
mutation in alpha subunit of terminal dioxygenase ISPNAP, similar activity with naphthalene, biphenyl and phenanthrene as wild-type
T351R
-
mutation in alpha subunit of terminal dioxygenase ISPNAP, similar activity with naphthalene, biphenyl and phenanthrene as wild-type
T351S
-
mutation in alpha subunit of terminal dioxygenase ISPNAP, similar activity with naphthalene, biphenyl and phenanthrene as wild-type
V260A
-
mutation in alpha subunit of terminal dioxygenase ISPNAP, similar activity with naphthalene, biphenyl and phenanthrene as wild-type
V260L
-
mutation in alpha subunit of terminal dioxygenase ISPNAP, similar activity with naphthalene, biphenyl and phenanthrene as wild-type
V260N
-
mutation in alpha subunit of terminal dioxygenase ISPNAP, similar activity with naphthalene, biphenyl and phenanthrene as wild-type
W316A
-
mutation in alpha subunit of terminal dioxygenase ISPNAP, similar activity with naphthalene, biphenyl and phenanthrene as wild-type
W358A
-
mutation in alpha subunit of terminal dioxygenase ISPNAP, very low activity with naphthalene and biphenyl
F352V
-
mutation changes the product regioselectivities for naphthalene, phenanthrene, and biphenyl
-
F352V
-
mutation in alpha subunit of terminal dioxygenase ISPNAP, similar activity with naphthalene, biphenyl and phenanthrene as wild-type, product of biphenyl oxidation: 96% biphenyl-3,4-dihydrodiol instead of biphenyl-2,3-dihydrodiol
F352V
-
mutation changes the product regioselectivities for naphthalene, phenanthrene, and biphenyl
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
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ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, ferredoxinNAP reductase, 1 month, minimal loss of activity, prolonged storage leads to precipitation when preparation is heated above 5°C
-
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
affinity chromatography separates the reductase from the two other enzyme components
-
Blue Sepharose, Q-Sepharose, Superose 12, purification of component B, the terminal oxygenase ISPNAR
-
component B i.e. the terminal oxygenase ISPNAP, DEAE-Sephadex, DEAE-cellulose, octyl-Sepharose, presence of 10% ethanol and 10% glycerol is required to maintain stability
-
DEAE-cellulose DE52 column chromatography, immobilized metal affinity chromatography and DEAE cellulose column chromatography
-
Q Sepharose column chromatography, octyl Sepharose column chromatography, and hydroxyapatite ion-exchange column chromatography
Q-Sepharose FF column chromatography and 1 hydroxyapatite ion-exchange column chromatography
-
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21(DE3) cells
expression in Escherichia coli
expression of ferredoxinNAP reductase, ferredoxinNAP and ISPNAP in Escherichia coli JM 109
-
strain G7, fragment of plasmid NAH7 cloned and expressed in Escherichia coli HB101
-
strain NCIB 9816, nahA-gene containing ndoA, ndoB and ndoC is inserted into plasmid pT7-5, transferred to and expressed in Escherichia coli HB101
-
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
synthesis
-
oxidation of naphthalene to produce optically pure (+)-cis-(1R,2S)-1,2-naphthalene dihydrodiol. Increase of productivity of the biotransformation by using resting cells. The biocatalyst is recycled for at least four runs in both suspended and immobilized form. Suspended resting cells retain their activity for at least four runs for 6 h recycle, but the stability is not retained for more than two runs for 12 h recycle. The stability of the 12 h recycle is improved by immobilization
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Resnick, S.M.; Gibson, D.T.
Oxidation of 6,7-dihydro-5H-benzocycloheptene by bacterial strains expressing naphthalene dioxygenase, biphenyl dioxygenase, and toluene dioxygenase yields homochiral mono-ol or cis-diol enantiomers as major products
Appl. Environ. Microbiol.
62
1364-1368
1996
Pseudomonas sp.
brenda
Haigler, B.E.; Gibson, D.T.
Purification and properties of NADH-ferredoxinNAP reductase, a component of naphthalene dioxygenase from Pseudomonas sp. strain NCIB 9816
J. Bacteriol.
172
457-464
1990
Pseudomonas sp.
brenda
Jeffrey, A.M.; Yeh, H.J.C.; Jerina, D.M.; Patel, T.R.; Davey, J.F.; Gibson, D.T.
Initial reactions in the oxidation of naphthalene by Pseudomonas putida
Biochemistry
14
575-584
1975
Pseudomonas putida, Pseudomonas putida 119
brenda
Ensley, B.D.; Gibson, D.T.
Naphthalene dioxygenase: purification and properties of a terminal oxygenase component
J. Bacteriol.
155
505-511
1983
Pseudomonas sp., Pseudomonas sp. NCIB 9816
brenda
Ensley, B.D.; Haigler, B.E.
Naphthalene dioxygenase from Pseudomonas NCIB 9816
Methods Enzymol.
188
46-52
1990
Pseudomonas sp.
brenda
Kurkela, S.; Lehvslaiho, H.; Palva, E.T.; Teeri, T.H.
Cloning, nucleotide sequence and characterization of genes encoding naphthalene dioxygenase of Pseudomonas putida strain NCIB9816
Gene
73
355-362
1988
Pseudomonas sp.
brenda
Ensley, B.D.; Gibson, D.T.; Laborde, A.L.
Oxidation of naphthalene by a multicomponent enzyme system from Pseudomonas sp. strain NCIB 9816
J. Bacteriol.
149
948-954
1982
Pseudomonas sp.
brenda
Dua, R.D.; Meera, S.
Purification and characterisation of naphthalene oxygenase from Corynebacterium renale
Eur. J. Biochem.
120
461-465
1981
Corynebacterium renale
brenda
Catterall, F.A.; Williams, P.A.
Some properties of the naphthalene oxygenase from Pseudomonas sp. NCIB 9816
J. Gen. Microbiol.
67
117-124
1971
Pseudomonas sp.
brenda
Ensley, B.D.; Ratzkin, B.J.; Osslund, T.D.; Simon, M.J.; Wackett, L.P.; Gibson, D.T.
Expression of naphthalene oxidation genes in Escherichia coli results in the biosynthesis of indigo
Science
222
167-169
1983
Pseudomonas putida, Pseudomonas putida G7
brenda
Swanson, E.P
Microbial transformation of benzocyclubutene to benzocyclobutene-1-ol and benzocyclobutene-1-one
Appl. Environ. Microbiol.
58
3404-3406
1992
Pseudomonas fluorescens
brenda
Whited, G.M.; Downie, J.C.; Hudlicky, T.; Fearnley, S.P.; Dudding, t.C.; Olivo, H.F.; Parker, D.
Oxidation of 2-methoxynaphthalene by toluene, naphthalene and biphenyl dioxygenases: structure and absolute stereochemistry of metabolites
Bioorg. Med. chem.
2
727-734
1994
Pseudomonas sp.
brenda
Cidaria, D.; Deidda, F.; Bosetti, A.
A rapid method for naphthalene dioxygenase assay in whole cells of naphthalene cis-dihydrodiol dehydrogenase blocked Pseudomonas fluorescens: screening of potential inducrs of dioxyenase activity
Appl. Microbiol. Biotechnol.
41
689-693
1994
Pseudomonas fluorescens, Pseudomonas fluorescens NCIMB 40531
-
brenda
Gibson, D.T.; Resnick, S.M.; Lee, K.; Brand, J.M.; Torok, D.S.; Wackett, L.P.; Schocken, M.J.; Haigler, B.E.
Desaturation, dioxygenation, and monooxygenation reactions catalyzed by naphthalene dioxygenase from Pseudomonas sp. strain 9816-4
J. Bacteriol.
177
2615-2621
1995
Pseudomonas sp.
brenda
Torok, D.S.; Resnick, S.M.; Brand, J.M.; Cruden, D.L.; Gibson, D.T.
Desaturation and oxygenation of 1,2-dihydronaphthalene by toluene and naphthalene dioxygenase
J. Bacteriol.
177
5799-5805
1995
Pseudomonas sp.
brenda
Resnick, S.M.; Gibson, D.T.
Regio- and stereospecific oxidation of fluorene, dibenzofuran, and dibenzothiophene by naphthalene dioxygenase from Pseudomonas sp. strain NCIB 9816-4
Appl. Environ. Microbiol.
62
4073-4080
1996
Pseudomonas sp.
brenda
Resnick, s.M.; Gibson, D.T.
Regio- and stereospecific oxidation of 9,10-dihydroanthracene and 9,10-dihydrophenanthrene by naphthalene dioxygenase: structure and absolute stereochemistry of metabolites
Appl. Environ. Microbiol.
62
3355-3359
1996
Pseudomonas sp.
brenda
Lee, K.; Gibson, D.T.
Stereospecific dihydroxylation of the styrene vinyl group by purified naphthalene dioxygenase from Pseudomonas sp. strain NCIB 9816-4
J. Bacteriol.
178
3353-3356
1996
Pseudomonas sp.
brenda
Lee, K.; Resnick, S.M.; Gibson, D.T.
Stereospecific oxidation of (R)- and (S)-1-indanol by naphthalene dioxygenase from Pseudomonas sp. strain NCIB 9816-4
Appl. Environ. Microbiol.
63
2067-2070
1997
Pseudomonas sp.
brenda
Larkin, M.J.; Allen, C.C.R.; Kulakov, L.A.; Lipscomb, D.A.
Purification and characterization of a novel naphthalene dioxygenase from Rhodococcus sp. strain NCIMB12038
J. Bacteriol.
181
6200-6204
1999
Rhodococcus sp., Rhodococcus sp. NCIMB12038
brenda
Barriault, D.; Sylvestre, M.
Functionality of biphenyl 2,3-dioxygenase components in naphthalene 1,2-dioxygenase
Appl. Microbiol. Biotechnol.
51
592-597
1999
Pseudomonas putida, Pseudomonas putida G7
brenda
Lee, K
Benzene-induced uncoupling of naphthalene dioxygenase activity and enzyme inactivation by production of hydrogen peroxide
J. Bacteriol.
181
2719-2725
1999
Pseudomonas sp.
brenda
Parales, R.E.; Lee, K.; Resnick, S.M.; Jiang, H.; Lessner, D.J.; Gibson, D.T
Substrate specificity of naphthalene dioxygenase: effect of specific amino acids at the active site of the enzyme
J. Bacteriol.
182
1641-1649
2000
Pseudomonas sp.
brenda
Carredano, E.; Karlsson, A.; Kauppi, B.; Choudhury, D.; Parales, R.E.; Parales, J.V.; Lee, K.; Gibson, D.T.; Eklund, H.; Ramaswamy, S.
Substrate binding site of naphthalene 1,2-dioxygenase: functional implications of indole binding
J. Mol. Biol.
296
701-712
2000
Pseudomonas sp.
brenda
Malik, Z.A.; Allen, C.C.; Gakhar, L.; Lipscomb, D.A.; Larkin, M.J.; Ramaswamy, S.
Crystallization and preliminary X-ray diffraction analysis of naphthalene dioxygenase from Rhodococcus sp. strain NCIMB 12038
Acta Crystallogr. Sect. D
58
2173-2174
2002
Rhodococcus sp., Rhodococcus sp. NCIMB12038
brenda
Wackett, L.P.; Kwart, L.D.; Gibson, D.T.
Benzylic monooxygenation catalyzed by toluene dioxygenase from Pseudomonas putida
Biochemistry
27
1360-1367
1988
Pseudomonas putida
brenda
Matsui, T.; Tanaka, Y.; Maruhashi, K.; Kurane, R.
Naphtho[1,2-b]thiophene degradation by Pseudomonas sp. HKT554: involvement of naphthalene dioxygenase
Curr. Microbiol.
46
39-42
2003
Pseudomonas sp., Pseudomonas sp. HKT554
brenda
Karlsson, A.; Parales, J.V.; Parales, R.E.; Gibson, D.T.; Eklund, H.; Ramaswamy, S.
Crystal structure of naphthalene dioxygenase: side-on binding of dioxygen to iron
Science
299
1039-1042
2003
Pseudomonas sp.
brenda
Boyd, D.R.; Sharma, N.D.; Haughey, S.A.; Kennedy, M.A.; Malone, J.F.; Shepherd, S.D.; Allen, C.C.R.; Dalton, H.
Dioxygenase-catalyzed sulfoxidation of bicyclic alkylaryl sulfides and chemoenzymatic synthesis of acyclic disulfoxides
Tetrahedron
60
549-559
2004
Pseudomonas putida, Pseudomonas putida 8859
-
brenda
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
12380-12391
2006
Sphingomonas sp.
brenda
Lee, K.
p-hydroxylation reactions catalyzed by naphthalene dioxygenase
FEMS Microbiol. Lett.
255
316-320
2006
Pseudomonas sp., Pseudomonas sp. NCIB 9816-4
brenda
Gakhar, L.; Malik, Z.A.; Allen, C.C.; Lipscomb, D.A.; Larkin, M.J.; Ramaswamy, S.
Structure and increased thermostability of Rhodococcus sp. naphthalene 1,2-dioxygenase
J. Bacteriol.
187
7222-7231
2005
Rhodococcus sp., Rhodococcus sp. NCIMB12038
brenda
Ferraro, D.J.; Okerlund, A.L.; Mowers, J.C.; Ramaswamy, S.
Structural basis for regioselectivity and stereoselectivity of product formation by naphthalene 1,2-dioxygenase
J. Bacteriol.
188
6986-6994
2006
Pseudomonas sp., Pseudomonas sp. NCIB 9816-4
brenda
Karlsson, A.; Parales, J.V.; Parales, R.E.; Gibson, D.T.; Eklund, H.; Ramaswamy, S.
NO binding to naphthalene dioxygenase
J. Biol. Inorg. Chem.
10
483-489
2005
Escherichia coli, Escherichia coli JM109(DE3)
brenda
McIver, A.M.; Garikipati, S.V.; Bankole, K.S.; Gyamerah, M.; Peeples, T.L.
Microbial oxidation of naphthalene to cis-1,2-naphthalene dihydrodiol using naphthalene dioxygenase in biphasic media
Biotechnol. Prog.
24
593-598
2008
Escherichia coli
brenda
Ohta, T.; Chakrabarty, S.; Lipscomb, J.D.; Solomon, E.I.
Near-IR MCD of the nonheme ferrous active site in naphthalene 1,2-dioxygenase: correlation to crystallography and structural insight into the mechanism of Rieske dioxygenases
J. Am. Chem. Soc.
130
1601-1610
2008
Pseudomonas sp.
brenda
Chopard, C.; Azerad, R.; Prange, T.
Naphthalene-dioxygenase-catalyzed cis-dihydroxylation of azaarene derivatives. Part 1: 2-Pyridones and 2-quinolones
J. Mol. Catal. B
50
53-60
2008
Pseudomonas sp.
-
brenda
Pathak, H.; Madamwar, D.
Biosynthesis of indigo dye by newly isolated naphthalene-degrading strain Pseudomonas sp. HOB1 and its application in dyeing cotton fabric
Appl. Biochem. Biotechnol.
160
1616-1626
2009
Pseudomonas sp., Pseudomonas sp. HOB1
brenda
Piskonen, R.; Nyyssoenen, M.; Itaevaara, M.
Evaluating the biodegradation of aromatic hydrocarbons by monitoring of several functional genes
Biodegradation
19
883-895
2008
Pseudomonas putida (P0A110 and P0A112), Pseudomonas putida, Pseudomonas putida G7 (P0A110 and P0A112)
brenda
AbuBakr, S.; Macmil, S.; Nanny, M.; Duncan, K.
Enzymatic transformation of humic substances by NDO
Soil Biol. Biochem.
40
2055-2062
2008
Pseudomonas putida, Pseudomonas putida G7
brenda
Seo, J.; Ryu, J.Y.; Han, J.; Ahn, J.H.; Sadowsky, M.J.; Hur, H.G.; Chong, Y.
Amino acid substitutions in naphthalene dioxygenase from Pseudomonas sp. strain NCIB 9816-4 result in regio- and stereo-specific hydroxylation of flavanone and isoflavanone
Appl. Microbiol. Biotechnol.
97
693-704
2013
Pseudomonas sp., Pseudomonas sp. NCIB 9816-4
brenda
Tondervik, A.; Bruheim, P.; Berg, L.; Ellingsen, T.E.; Kotlar, H.K.; Valla, S.; Throne-Holst, M.
Ralstonia sp. U2 naphthalene dioxygenase and Comamonas sp. JS765 nitrobenzene dioxygenase show differences in activity towards methylated naphthalenes
J. Biosci. Bioeng.
113
173-178
2012
Ralstonia sp., Ralstonia sp. U2
brenda
Chopard, C.; Bertho, G.; Prange, T.
Naphthalene-dioxygenase catalysed cis-dihydroxylation of bicyclic azaarenes
RSC Adv.
2
605-615
2012
Pseudomonas sp., Pseudomonas sp. NCIB 9616-4
-
brenda
Yen, K.M.; Karl, M.R.
Identification of a new gene, tmoF, in the Pseudomonas mendocina KR1 gene cluster encoding toluene-4-monooxygenase
J. Bacteriol.
174
7253-7261
1992
plasmid NAH7 (Q52009), plasmid NAH7
brenda
Dutta, K.; Shityakov, S.; Das, P.P.; Ghosh, C.
Enhanced biodegradation of mixed PAHs by mutated naphthalene 1,2-dioxygenase encoded by Pseudomonas putida strain KD6 isolated from petroleum refinery waste
3 Biotech
7
365
2017
Pseudomonas putida, Pseudomonas putida KD6
brenda
Zhang, X.; Qu, Y.; Ma, Q.; Kong, C.; Zhou, H.; Cao, X.; Shen, W.; Shen, E.; Zhou, J.
Production of indirubin from tryptophan by recombinant Escherichia coli containing naphthalene dioxygenase genes from Comamonas sp. MQ
Appl. Biochem. Biotechnol.
172
3194-3206
2014
Comamonas sp. MQ (G9IE62), Comamonas sp. MQ (G9IE63)
brenda
Jouanneau, Y.; Meyer, C.; Duraffourg, N.
Dihydroxylation of four- and five-ring aromatic hydrocarbons by the naphthalene dioxygenase from Sphingomonas CHY-1
Appl. Microbiol. Biotechnol.
100
1253-1263
2016
Sphingomonas sp. CHY-1
brenda
Jin, J.N.; Yao, J.; Zhang, Q.Y.; Yu, C.; Chen, P.; Liu, W.J.; Peng, D.N.; Choi, M.M.
An integrated approach of bioassay and molecular docking to study the dihydroxylation mechanism of pyrene by naphthalene dioxygenase in Rhodococcus sp. ustb-1
Chemosphere
128
307-313
2015
Rhodococcus sp. ustb-1
brenda
Ji, X.; Xu, J.; Ning, S.; Li, N.; Tan, L.; Shi, S.
Cometabolic degradation of dibenzofuran and dibenzothiophene by a naphthalene-degrading Comamonas sp. JB
Curr. Microbiol.
74
1411-1416
2017
Comamonas sp. JB
brenda
Peng, R.H.; Fu, X.Y.; Zhao, W.; Tian, Y.S.; Zhu, B.; Han, H.J.; Xu, J.; Yao, Q.H.
Phytoremediation of phenanthrene by transgenic plants transformed with a naphthalene dioxygenase system from Pseudomonas
Environ. Sci. Technol.
48
12824-12832
2014
Pseudomonas putida
brenda
Ferraro, D.J.; Okerlund, A.; Brown, E.; Ramaswamy, S.
One enzyme, many reactions structural basis for the various reactions catalyzed by naphthalene 1,2-dioxygenase
IUCrJ
4
648-656
2017
Pseudomonas sp. (P0A111), Pseudomonas sp. C18 (P0A111)
brenda
Escalante, D.E.; Aukema, K.G.; Wackett, L.P.; Aksan, A.
Simulation of the bottleneck controlling access into a Rieske active site Predicting substrates of naphthalene 1,2-dioxygenase
J. Chem. Inf. Model.
57
550-561
2017
Pseudomonas putida (P0A110), Pseudomonas putida (P0A112)
brenda
Librando, V.; Pappalardo, M.
Theoretical approach to the innovative mutation of naphthalene 1,2-dioxygenase a molecular dynamics and docking study
J. Mol. Model.
20
2354
2014
Pseudomonas putida (P0A110)
brenda
Yang, Y.; Wang, J.; Liao, J.; Xie, S.; Huang, Y.
Distribution of naphthalene dioxygenase genes in crude oil-contaminated soils
Microb. Ecol.
68
785-793
2014
Pseudomonas sp.
brenda
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