1.14.12.22: carbazole 1,9a-dioxygenase
This is an abbreviated version!
For detailed information about carbazole 1,9a-dioxygenase, go to the full flat file.
Word Map on EC 1.14.12.22
-
1.14.12.22
-
ferredoxin
-
rieske
-
resinovorans
-
carac
-
carbazole-degradation
-
dibenzo-p-dioxins
-
dibenzofurans
-
fluorene
-
aromaticivorans
-
nocardioides
-
dianhydride
-
dibenzothiophene
-
polyimide
-
janthinobacterium
-
stipes
-
degradation
- 1.14.12.22
- ferredoxin
-
rieske
- resinovorans
- carac
-
carbazole-degradation
- dibenzo-p-dioxins
- dibenzofurans
- fluorene
- aromaticivorans
-
nocardioides
-
dianhydride
- dibenzothiophene
-
polyimide
- janthinobacterium
-
stipes
- degradation
Reaction
Synonyms
CarAa, CarAc, carbazole dioxygenase, CARDO, CARDO-F, CARDO-R
ECTree
1.14.12.22 carbazole 1,9a-dioxygenaseAdvanced search results
results (
results (Substrates Products
Substrates Products on EC 1.14.12.22 - carbazole 1,9a-dioxygenase
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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
9-fluorenone + NAD(P)H + H+ + O2
1,1a-dihydroxy-1-hydrofluoren-9-one + NAD(P)+
-
-
angular dioxygenation, yield 8-12%
-
?
biphenyl + NAD(P)H + H+ + O2
2-hydroxybiphenyl + 3-hydroxybiphenyl + biphenyl dihydrodiol + NAD(P)+
-
-
in Escherichia coli expressing terminal oxygenase gene CarAa and ferredoxin component gene CarAc, ratio of products depends on reaction time. Synthesis of up to 46% biphenyl dihydrodiol
-
?
biphenyl + NAD(P)H + H+ + O2
cis-2,3-dihydroxy-2,3-dihydrobiphenyl + 2-hydroxybiphenyl + 3-hydroxybiphenyl + NAD(P)+
-
-
lateral dioxygenation to cis-2,3-dihydroxy-2,3-dihydrobiphenyl, yield 85-90%, and to dihydrodiol, yield 9-11%
-
?
dibenzo-p-dioxin + NAD(P)H + H+ + O2
2,2',3-trihydroxybiphenyl ether + NAD(P)+
-
-
26% 2,2',3-trihydroxybiphenyl ether in Escherichia coli expressing terminal oxygenase gene CarAa and ferredoxin component gene CarAc
-
?
dibenzo-p-dioxin + NAD(P)H + H+ + O2
2,2',3-trihydroxydiphenyl ether + NAD(P)+
-
-
-
-
?
dibenzofuran + NADH + H+ + O2
2,2',3-trihydroxybiphenyl + NAD+
-
-
-
-
?
dibenzothiophene + NADH + H+ + O2
dibenzothiophene 5-oxide + NAD+
-
-
-
-
?
dibenzothiophene + NADH + H+ + O2
dibenzothiophene sulfoxide + NAD+ + H2O
-
-
monooxygenation, yield 99-100%
-
?
fluoranthene + NAD(P)H + H+ + O2
cis-2,3-dihydroxy-2,3-dihydrofluoranthene + monohydroxyfluoranthene + NAD(P)+
fluoranthene + NAD(P)H + H+ + O2
cis-2,3-dihydroxy-2,3-dihydrofluoranthene + NAD(P)+
-
poor substrate
-
-
?
fluorene + NAD(P)H + H+ + O2
9-fluorenol + ? + NAD(P)+
-
-
monooxygenation to 9-fluorenol, yield 3-5%, and lateral dioxygenation to dihydrodiol, yield 5-8%
-
?
fluorene + NAD(P)H + H+ + O2
9-fluorenone + 9-fluorenol + monohydroxyfluorene + fluorene dihydrodiol + NAD(P)+
-
-
in Escherichia coli expressing terminal oxygenase gene CarAa and ferredoxin component gene CarAc, ratio of products depends on reaction time
-
?
naphthalene + NAD(P)H + H+ + O2
1-naphthol + cis-1,2-dihydroxy-1,2-dihydronaphthalene + NAD(P)+
-
-
7.3% 1-naphthol and 93% cis-1,2-dihydroxy-1,2-dihydronaphthalene in Escherichia coli expressing terminal oxygenase gene CarAa and ferredoxin component gene CarAc
-
?
naphthalene + NAD(P)H + H+ + O2
cis-1,2-dihydroxy-1,2-dihydronaphthalene + 1-naphthol + NAD(P)+
-
-
lateral dioxygenation, yield 65-70%
-
?
phenanthrene + NAD(P)H + H+ + O2
phenanthrene dihydrodiol + monohydroxyphenanthrene + NAD(P)+
-
-
70% phenanthrene dihydrodiol and 9% monohydroxyphenanthrene in Escherichia coli expressing terminal oxygenase gene CarAa and ferredoxin component gene CarAc
-
?
phenothiazine + NAD(P)H + H+ + O2
? + NAD(P)+
18 h reaction time, 7.6% substrate remaining
-
-
?
phenoxazine + NAD(P)H + H+ + O2
? + NAD(P)+
18 h reaction time, 1.1% substrate remaining
-
-
?
9H-carbazole + NADH + H+ + O2
2'-aminobiphenyl-2,3-diol + NAD+
-
-
-
-
?
9H-carbazole + NADH + H+ + O2
2'-aminobiphenyl-2,3-diol + NAD+
-
-
-
?
9H-carbazole + NADH + H+ + O2
2'-aminobiphenyl-2,3-diol + NAD+
-
-
-
-
?
9H-carbazole + NADH + H+ + O2
2'-aminobiphenyl-2,3-diol + NAD+
-
-
-
-
?
9H-carbazole + NADPH + H+ + O2
2'-aminobiphenyl-2,3-diol + NADP+
-
-
-
-
?
9H-carbazole + NADPH + H+ + O2
2'-aminobiphenyl-2,3-diol + NADP+
-
-
-
?
9H-carbazole + NADPH + H+ + O2
2'-aminobiphenyl-2,3-diol + NADP+
-
-
-
-
?
9H-carbazole + NADPH + H+ + O2
2'-aminobiphenyl-2,3-diol + NADP+
-
-
-
-
?
anthracene + NAD(P)H + H+ + O2
cis-1,2-dihydroxy-1,2-dihydroanthracene + NAD(P)+
-
-
-
-
?
anthracene + NAD(P)H + H+ + O2
cis-1,2-dihydroxy-1,2-dihydroanthracene + NAD(P)+
-
-
-
-
?
anthracene + NAD(P)H + H+ + O2
cis-1,2-dihydroxy-1,2-dihydroanthracene + NAD(P)+
18 h reaction time, 8.7% substrate remaining
-
-
?
anthracene + NAD(P)H + H+ + O2
cis-1,2-dihydroxy-1,2-dihydroanthracene + NAD(P)+
-
-
-
-
?
anthracene + NAD(P)H + H+ + O2
cis-1,2-dihydroxy-1,2-dihydroanthracene + NAD(P)+
18 h reaction time, 8.7% substrate remaining
-
-
?
biphenyl + NAD(P)H + H+ + O2
cis-2,3-dihydroxy-2,3-dihydrobiphenyl + NAD(P)+
-
-
cis dihydroxylation
-
?
biphenyl + NAD(P)H + H+ + O2
cis-2,3-dihydroxy-2,3-dihydrobiphenyl + NAD(P)+
18 h reaction time, 0% substrate remaining
-
-
?
biphenyl + NAD(P)H + H+ + O2
cis-2,3-dihydroxy-2,3-dihydrobiphenyl + NAD(P)+
-
-
cis dihydroxylation
-
?
biphenyl + NAD(P)H + H+ + O2
cis-2,3-dihydroxy-2,3-dihydrobiphenyl + NAD(P)+
18 h reaction time, 0% substrate remaining
-
-
?
carbazole + NAD(P)H + H+ + O2
2'-aminobiphenyl-2,3-diol + NAD(P)+
-
-
-
-
?
carbazole + NAD(P)H + H+ + O2
2'-aminobiphenyl-2,3-diol + NAD(P)+
-
-
100% 2'-aminobiphenyl-2,3-diol in Escherichia coli expressing terminal oxygenase gene CarAa and ferredoxin component gene CarAc
-
?
carbazole + NAD(P)H + H+ + O2
2'-aminobiphenyl-2,3-diol + NAD(P)+
-
best substrate
angular dioxygenation, yield 70-80%
-
?
carbazole + NAD(P)H + H+ + O2
2'-aminobiphenyl-2,3-diol + NAD(P)+
18 h reaction time, 1.3% substrate remaining
-
-
?
carbazole + NAD(P)H + H+ + O2
2'-aminobiphenyl-2,3-diol + NAD(P)+
-
-
-
-
?
carbazole + NAD(P)H + H+ + O2
2'-aminobiphenyl-2,3-diol + NAD(P)+
18 h reaction time, 1.3% substrate remaining
-
-
?
carbazole + NAD(P)H + H+ + O2
2'-aminobiphenyl-2,3-diol + NAD(P)+
-
-
-
-
?
carbazole + NAD(P)H + H+ + O2
2'-aminobiphenyl-2,3-diol + NAD(P)+
-
about 80% conversion in Escherichia coli harboring genes car-AaAcfdr
-
?
carbazole + NAD(P)H + H+ + O2
2'-aminobiphenyl-2,3-diol + NAD(P)+
-
about 80% conversion in Escherichia coli harboring genes car-AaAcfdr
-
?
carbazole + NADH + H+ + O2
2'-aminobiphenyl-2,3-diol + NAD+
-
-
-
?
carbazole + NADH + H+ + O2
2'-aminobiphenyl-2,3-diol + NAD+
-
-
-
?
carbazole + NADPH + H+ + O2
2'-aminobiphenyl-2,3-diol + NADP+
-
-
-
?
carbazole + NADPH + H+ + O2
2'-aminobiphenyl-2,3-diol + NADP+
-
-
-
?
dibenzo-p-dioxin + NAD(P)H + H+ + O2
? + NAD(P)+
18 h reaction time, 3.9% substrate remaining
-
-
?
dibenzo-p-dioxin + NAD(P)H + H+ + O2
? + NAD(P)+
18 h reaction time, 3.9% substrate remaining
-
-
?
dibenzofuran + NAD(P)H
? + NAD(P)+
18 h reaction time, 48.5% substrate remaining
-
-
?
dibenzofuran + NAD(P)H
? + NAD(P)+
18 h reaction time, 48.5% substrate remaining
-
-
?
dibenzofuran + NAD(P)H + H+ + O2
2,2',3-trihydroxybiphenyl + NAD(P)+
-
-
74% 2,2',3-trihydroxybiphenyl in Escherichia coli expressing terminal oxygenase gene CarAa and ferredoxin component gene CarAc
-
?
dibenzofuran + NAD(P)H + H+ + O2
2,2',3-trihydroxybiphenyl + NAD(P)+
-
-
angular dioxygenation, yield 60-65%
-
?
dibenzothiophene + NAD(P)H + H+ + O2
dibenzothiophene-5-oxide + NAD(P)+
-
-
-
-
?
dibenzothiophene + NAD(P)H + H+ + O2
dibenzothiophene-5-oxide + NAD(P)+
-
-
-
-
?
dibenzothiophene + NAD(P)H + H+ + O2
dibenzothiophene-5-oxide + NAD(P)+
-
-
monooxygenation
-
?
dibenzothiophene + NAD(P)H + H+ + O2
dibenzothiophene-5-oxide + NAD(P)+
-
-
-
-
?
dibenzothiophene + NAD(P)H + H+ + O2
dibenzothiophene-5-oxide + NAD(P)+
-
-
monooxygenation
-
?
fluoranthene + NAD(P)H + H+ + O2
cis-2,3-dihydroxy-2,3-dihydrofluoranthene + monohydroxyfluoranthene + NAD(P)+
-
-
-
-
?
fluoranthene + NAD(P)H + H+ + O2
cis-2,3-dihydroxy-2,3-dihydrofluoranthene + monohydroxyfluoranthene + NAD(P)+
-
-
-
?
fluoranthene + NAD(P)H + H+ + O2
cis-2,3-dihydroxy-2,3-dihydrofluoranthene + monohydroxyfluoranthene + NAD(P)+
-
-
-
-
?
fluorene + NAD(P)H + H+ + O2
9-hydroxyfluorene + NAD(P)+
-
-
monooxygenation
-
?
fluorene + NAD(P)H + H+ + O2
9-hydroxyfluorene + NAD(P)+
18 h reaction time, 80.8% substrate remaining
-
-
?
fluorene + NAD(P)H + H+ + O2
9-hydroxyfluorene + NAD(P)+
-
-
monooxygenation
-
?
naphthalene + NAD(P)H + H+ + O2
cis-1,2-dihydroxy-1,2-dihydronaphthalene + NAD(P)+
-
-
cis dihydroxylation
-
?
naphthalene + NAD(P)H + H+ + O2
cis-1,2-dihydroxy-1,2-dihydronaphthalene + NAD(P)+
18 h reaction time, 23.6% substrate remaining
-
-
?
phenanthrene + NAD(P)H + H+ + O2
? + NAD(P)+
-
-
products are three dihydrodiols
-
?
phenanthrene + NAD(P)H + H+ + O2
? + NAD(P)+
18 h reaction time, 5.4% substrate remaining
-
-
?
phenoxathiin + NAD(P)H + H+ + O2
2,2',3-trihydroxydiphenyl sulfide + NAD(P)+
-
-
angular dioxygenation by CARDO occurs at the angular position adjacent to the oxygen atom to yield hetero ring-cleaved compounds
-
?
phenoxathiin + NAD(P)H + H+ + O2
2,2',3-trihydroxydiphenyl sulfide + NAD(P)+
18 h reaction time, 25% substrate remaining
-
-
?
xanthene + NAD(P)H + H+ + O2
2,2',3-trihydroxydiphenylmethane + NAD(P)+
-
-
angular dioxygenation
-
?
xanthene + NAD(P)H + H+ + O2
2,2',3-trihydroxydiphenylmethane + NAD(P)+
18 h reaction time, 52.8% substrate remaining
-
-
?
additional information
?
-
-
in the presence of NADH, His-tagged ferrdoxin subunit CarAc is reduced by His-tagged ferredoxin reductase CarAd. Terminal oxygenase subunit CarAa is reduced by His-tagged CarAc, His-tagged CarAd, and NADH. The three purified proteins CarAa, CarAc and CarAd can reconstitute the CARDO activity in vitro. In the reconstituted CARDO system, His-tagged CarAc is indispensable for electron transport, while His-tagged CarAd can be replaced by some unrelated reductases
-
-
?
additional information
?
-
in the presence of NADH, His-tagged ferrdoxin subunit CarAc is reduced by His-tagged ferredoxin reductase CarAd. Terminal oxygenase subunit CarAa is reduced by His-tagged CarAc, His-tagged CarAd, and NADH. The three purified proteins CarAa, CarAc and CarAd can reconstitute the CARDO activity in vitro. In the reconstituted CARDO system, His-tagged CarAc is indispensable for electron transport, while His-tagged CarAd can be replaced by some unrelated reductases
-
-
?
additional information
?
-
in the presence of NADH, His-tagged ferrdoxin subunit CarAc is reduced by His-tagged ferredoxin reductase CarAd. Terminal oxygenase subunit CarAa is reduced by His-tagged CarAc, His-tagged CarAd, and NADH. The three purified proteins CarAa, CarAc and CarAd can reconstitute the CARDO activity in vitro. In the reconstituted CARDO system, His-tagged CarAc is indispensable for electron transport, while His-tagged CarAd can be replaced by some unrelated reductases
-
-
?
additional information
?
-
-
in the presence of NADH, His-tagged ferrdoxin subunit CarAc is reduced by His-tagged ferredoxin reductase CarAd. The three purified proteins CarAa, CarAc and CarAd can reconstitute the CARDO activity in vitro. In the reconstituted CARDO system, His-tagged CarAc is indispensable for electron transport, while His-tagged CarAd can be replaced by some unrelated reductases
-
-
?
additional information
?
-
in the presence of NADH, His-tagged ferrdoxin subunit CarAc is reduced by His-tagged ferredoxin reductase CarAd. The three purified proteins CarAa, CarAc and CarAd can reconstitute the CARDO activity in vitro. In the reconstituted CARDO system, His-tagged CarAc is indispensable for electron transport, while His-tagged CarAd can be replaced by some unrelated reductases
-
-
?
additional information
?
-
in the presence of NADH, His-tagged ferrdoxin subunit CarAc is reduced by His-tagged ferredoxin reductase CarAd. The three purified proteins CarAa, CarAc and CarAd can reconstitute the CARDO activity in vitro. In the reconstituted CARDO system, His-tagged CarAc is indispensable for electron transport, while His-tagged CarAd can be replaced by some unrelated reductases
-
-
?
additional information
?
-
-
terminal oxygenase subunit CarAa is reduced by His-tagged ferredoxin CarAc, His-tagged ferredoxin reductase CarAd, and NADH. The three purified proteins can reconstitute the CARDO activity in vitro. In the reconstituted CARDO system, His-tagged CarAc is indispensable for electron transport, while His-tagged CarAd can be replaced by some unrelated reductases
-
-
?
additional information
?
-
terminal oxygenase subunit CarAa is reduced by His-tagged ferredoxin CarAc, His-tagged ferredoxin reductase CarAd, and NADH. The three purified proteins can reconstitute the CARDO activity in vitro. In the reconstituted CARDO system, His-tagged CarAc is indispensable for electron transport, while His-tagged CarAd can be replaced by some unrelated reductases
-
-
?
additional information
?
-
terminal oxygenase subunit CarAa is reduced by His-tagged ferredoxin CarAc, His-tagged ferredoxin reductase CarAd, and NADH. The three purified proteins can reconstitute the CARDO activity in vitro. In the reconstituted CARDO system, His-tagged CarAc is indispensable for electron transport, while His-tagged CarAd can be replaced by some unrelated reductases
-
-
?
additional information
?
-
-
terminal oxygenase subunit CarAa is reduced by His-tagged ferredoxin CarAc, His-tagged ferredoxin reductase CarAd, and NADH. The three purified proteins can reconstitute the CARDO activity in vitro. In the reconstituted CARDO system, His-tagged CarAc is indispensable for electron transport, while His-tagged CarAd can be replaced by some unrelated reductases
-
-
?
additional information
?
-
terminal oxygenase subunit CarAa is reduced by His-tagged ferredoxin CarAc, His-tagged ferredoxin reductase CarAd, and NADH. The three purified proteins can reconstitute the CARDO activity in vitro. In the reconstituted CARDO system, His-tagged CarAc is indispensable for electron transport, while His-tagged CarAd can be replaced by some unrelated reductases
-
-
?
additional information
?
-
terminal oxygenase subunit CarAa is reduced by His-tagged ferredoxin CarAc, His-tagged ferredoxin reductase CarAd, and NADH. The three purified proteins can reconstitute the CARDO activity in vitro. In the reconstituted CARDO system, His-tagged CarAc is indispensable for electron transport, while His-tagged CarAd can be replaced by some unrelated reductases
-
-
?
additional information
?
-
-
in the presence of NADH, His-tagged ferrdoxin subunit CarAc is reduced by His-tagged ferredoxin reductase CarAd. Terminal oxygenase subunit CarAa is reduced by His-tagged CarAc, His-tagged CarAd, and NADH. The three purified proteins CarAa, CarAc and CarAd can reconstitute the CARDO activity in vitro. In the reconstituted CARDO system, His-tagged CarAc is indispensable for electron transport, while His-tagged CarAd can be replaced by some unrelated reductases
-
-
?
additional information
?
-
in the presence of NADH, His-tagged ferrdoxin subunit CarAc is reduced by His-tagged ferredoxin reductase CarAd. Terminal oxygenase subunit CarAa is reduced by His-tagged CarAc, His-tagged CarAd, and NADH. The three purified proteins CarAa, CarAc and CarAd can reconstitute the CARDO activity in vitro. In the reconstituted CARDO system, His-tagged CarAc is indispensable for electron transport, while His-tagged CarAd can be replaced by some unrelated reductases
-
-
?
additional information
?
-
in the presence of NADH, His-tagged ferrdoxin subunit CarAc is reduced by His-tagged ferredoxin reductase CarAd. Terminal oxygenase subunit CarAa is reduced by His-tagged CarAc, His-tagged CarAd, and NADH. The three purified proteins CarAa, CarAc and CarAd can reconstitute the CARDO activity in vitro. In the reconstituted CARDO system, His-tagged CarAc is indispensable for electron transport, while His-tagged CarAd can be replaced by some unrelated reductases
-
-
?
additional information
?
-
-
in the presence of NADH, His-tagged ferrdoxin subunit CarAc is reduced by His-tagged ferredoxin reductase CarAd. The three purified proteins CarAa, CarAc and CarAd can reconstitute the CARDO activity in vitro. In the reconstituted CARDO system, His-tagged CarAc is indispensable for electron transport, while His-tagged CarAd can be replaced by some unrelated reductases
-
-
?
additional information
?
-
in the presence of NADH, His-tagged ferrdoxin subunit CarAc is reduced by His-tagged ferredoxin reductase CarAd. The three purified proteins CarAa, CarAc and CarAd can reconstitute the CARDO activity in vitro. In the reconstituted CARDO system, His-tagged CarAc is indispensable for electron transport, while His-tagged CarAd can be replaced by some unrelated reductases
-
-
?
additional information
?
-
in the presence of NADH, His-tagged ferrdoxin subunit CarAc is reduced by His-tagged ferredoxin reductase CarAd. The three purified proteins CarAa, CarAc and CarAd can reconstitute the CARDO activity in vitro. In the reconstituted CARDO system, His-tagged CarAc is indispensable for electron transport, while His-tagged CarAd can be replaced by some unrelated reductases
-
-
?
additional information
?
-
-
the enzyme does not degrade alkanes like pentadecane, hexadecane, heptadecane, octadecane, nonadecane and docosane
-
-
?
