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

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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.
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This record set is specific for:
UNIPROT: Q8GI16
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Word Map
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
-
-
-
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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
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
additional information
?
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
ferredoxin subunit CarAc
UniProt
Manually annotated by BRENDA team
ferredoxin subunit CarAc
UniProt
Manually annotated by BRENDA team
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
CARAC_PSERE
107
0
11367
Swiss-Prot
other Location (Reliability: 1)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
1 * 13000, SDS-PAGE, subunit CarAc
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
0°C, 10% glycerol, 8 days, more than 90% residual activity for isolated subunit CarAa
0°C, 50 mM Tris-HCl pH 7.5, 24 h, 90% residual activity for reconstituted CARDO system
4°C, 10% glycerol, 24 h, full activity for isolated subunit CarAa
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression of ferredoxin subunit CarAc in Escherichia coli, His-tagged
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Nam, J.-W.; Nojiri, H.; Noguchi, H.; Uchimura, H.; Yoshida, T.; Habe, H.; Yamane, H.; Omori, T.
Purification and characterization of carbazole 1,9a-dioxygenase, a three-component dioxygenase system of Pseudomonas resinovorans strain CA10
Appl. Environ. Microbiol.
68
5882-5890
2002
Pseudomonas resinovorans, Pseudomonas resinovorans (Q8GI14), Pseudomonas resinovorans (Q8GI16), Pseudomonas resinovorans CA10, Pseudomonas resinovorans CA10 (Q8GI14), Pseudomonas resinovorans CA10 (Q8GI16)
Manually annotated by BRENDA team