Any feedback?
Information on EC 1.14.12.22 - carbazole 1,9a-dioxygenase
for references in articles please use BRENDA:EC1.14.12.22Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
1.14.12.22 carbazole 1,9a-dioxygenaseIUBMB Comments
This enzyme catalyses the first reaction in the pathway of carbazole degradation. The enzyme attacks at the 1 and 9a positions of carbazole, resulting in the formation of a highly unstable hemiaminal intermediate that undergoes a spontaneous cleavage and rearomatization, resulting in 2'-aminobiphenyl-2,3-diol. In most bacteria the enzyme is a complex composed of a terminal oxygenase, a ferredoxin, and a ferredoxin reductase. The terminal oxygenase component contains a nonheme iron centre and a Rieske [2Fe-2S] iron-sulfur cluster.
Specify your search results
Word Map
- 1.14.12.22
- ferredoxin
-
rieske
- resinovorans
- carac
-
carbazole-degradation
- dibenzo-p-dioxins
- dibenzofurans
- fluorene
- aromaticivorans
-
nocardioides
-
dianhydride
- dibenzothiophene
-
polyimide
- janthinobacterium
-
stipes
- degradation
The enzyme appears in viruses and cellular organisms
Synonyms
cardo, carbazole 1,9a-dioxygenase, caraa, carbazole dioxygenase, cardo-f, cardo-r, 
more
topPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
CARDO
CARDO-F
CARDO
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
9H-carbazole + NAD(P)H + H+ + O2 = 2'-aminobiphenyl-2,3-diol + NAD(P)+
-
-
-
-
9H-carbazole + NAD(P)H + H+ + O2 = 2'-aminobiphenyl-2,3-diol + NAD(P)+
catalytic mechanism is as follows: When the Rieske cluster is reduced, substrate binding induces several conformational changes that create room for oxygen binding. Dioxygen bound in a side-on fashion onto nonheme iron is activated by reduction to the peroxo state [Fe(III)-(hydro)peroxo]. This state may react directly with the bound substrate, or O-O bond cleavage may occur to generate Fe(V)-oxo-hydroxo species prior to the reaction. After producing a cisdihydrodiol, the product is released by reducing the nonheme iron
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SYSTEMATIC NAME
IUBMB Comments
9H-carbazole,NAD(P)H:oxygen oxidoreductase (2,3-hydroxylating)
This enzyme catalyses the first reaction in the pathway of carbazole degradation. The enzyme attacks at the 1 and 9a positions of carbazole, resulting in the formation of a highly unstable hemiaminal intermediate that undergoes a spontaneous cleavage and rearomatization, resulting in 2'-aminobiphenyl-2,3-diol. In most bacteria the enzyme is a complex composed of a terminal oxygenase, a ferredoxin, and a ferredoxin reductase. The terminal oxygenase component contains a nonheme iron centre and a Rieske [2Fe-2S] iron-sulfur cluster.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CAS REGISTRY NUMBER
COMMENTARY
194812-10-7
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
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+
-
-
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Ferredoxin
-
ferredoxin component CarAc acts as a mediator in the electron transfer from ferredoxin reductase CarAd to terminal oxygenase CarAa. It contains a Rieske [2Fe-2S] cluster, which is located at the tip of the cluster-binding domain, where it is exposed to solvent
-
Ferredoxin
-
ferredoxin component contains two Rieske [2Fe-2S] clusters
-
NADH
both NADH and NADPH are effective as electron donors for His-tagged ferrdoxin reductase CarAd. The ratio kcat/Km for NADH is 22.3-fold higher than that for NADPH in the 2,6-dichlorophenolindophenol reductase assay
NADPH
both NADH and NADPH are effective as electron donors for His-tagged ferrdoxin reductase CarAd. The ratio kcat/Km for NADH is 22.3-fold higher than that for NADPH in the 2,6-dichlorophenolindophenol reductase assay
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Iron
Iron
subunit CarAc, one Rieske type [2Fe-2S] cluster per monomer protein. The iron and sulfur contents of His-tagged CarAc are 1.7 to 1.9 and 1.3 to 1.6 mol/mol of protein, respectively
Iron
subunit CarAd, one Rieske type [2Fe-2S] cluster per monomer protein. The iron and sulfur contents of His-tagged CarAc are 1.8 to 2.0 and 1.8 to 1.9 mol/mol of protein, respectively
Iron
terminal oxygenase subunit contains one Rieske type [2Fe2S] cluster and one mononuclear iron center in each monomer
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Heart Failure
[Metabolic remodeling and the alteration of related receptors expressions in failing heart]
Heart Valve Diseases
[Metabolic remodeling and the alteration of related receptors expressions in failing heart]
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0034
NADH
CarAd activity, electron acceptor 2,6-dichlorophenolindophenol, pH 7.5, 30°C
0.182
NADPH
CarAd activity, electron acceptor 2,6-dichlorophenolindophenol, pH 7.5, 30°C
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2900
NADH
CarAd activity, electron acceptor 2,6-dichlorophenolindophenol, pH 7.5, 30°C
130
NADPH
CarAd activity, electron acceptor 2,6-dichlorophenolindophenol, pH 7.5, 30°C
0.000733
9H-carbazole
mutant enzyme Q282N, at pH 7.5 and 30°C
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.5 - 8.5
maximum cytochrome c reductase activity of subunit CarAd
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
35 - 45
maximum cytochrome c reductase activity of subunit CarAd
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE