Any feedback?
Please rate this page
(enzyme.php)
(0/150)

BRENDA support

BRENDA Home
show all | hide all No of entries

Information on EC 1.14.12.22 - carbazole 1,9a-dioxygenase

for references in articles please use BRENDA:EC1.14.12.22
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
IUBMB 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
Select one or more organisms in this record: ?
This record set is specific for:
UNIPROT: Q84II6
Show additional data
Do not include text mining results
Include (text mining) results
Include results (AMENDA + additional results, but less precise)
Word Map
hide
The enzyme appears in viruses and cellular organisms
Synonyms
cardo, carbazole 1,9a-dioxygenase, caraa, carbazole dioxygenase, cardo-f, cardo-r, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
CARDO
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
9H-carbazole + NAD(P)H + H+ + O2 = 2'-aminobiphenyl-2,3-diol + NAD(P)+
show the reaction diagram
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
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.
CAS REGISTRY NUMBER
COMMENTARY hide
194812-10-7
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
Q84II6_JANS3
Janthinobacterium sp. (strain J3)
384
0
43786
TrEMBL
-
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystal structures of the reduced carbazole-bound, dioxygen-bound, and both carbazole- and dioxygen-bound subunits CARDO-O:CARDO-F binary complex structures at 1.95, 1.85, and 2.00 A resolution, using the catalytic terminal oxygenase subunit from Janthinobacterium sp. J3 and ferredoxin from Pseudomonas resinovorans CA10. 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 cis-dihydrodiol, the product is released by reducing the nonheme iron
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Ashikawa, Y.; Fujimoto, Z.; Usami, Y.; Inoue, K.; Noguchi, H.; Yamane, H.; Nojiri, H.
Structural insight into the substrate- and dioxygen-binding manner in the catalytic cycle of rieske nonheme iron oxygenase system, carbazole 1,9a-dioxygenase
BMC Struct. Biol.
12
15
2012
Janthinobacterium sp. (Q84II6)
Manually annotated by BRENDA team