Any feedback?
Information on EC 1.14.12.26 - chlorobenzene dioxygenase
for references in articles please use BRENDA:EC1.14.12.26Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
1.14.12.26 chlorobenzene dioxygenaseIUBMB Comments
This bacterial enzyme is a class IIB dioxygenase, comprising three components - a heterodimeric terminal dioxygenase, a ferredoxin protein, and a ferredoxin reductase. The enzyme acts on a range of aromatic compounds, including mono-, di-, tri-, and tetra-chlorinated benzenes and toluenes.
Specify your search results
Word Map
- 1.14.12.26
- toluene
-
dihydrodiols
- putida
-
chlorocatechol
- burkholderia
- ralstonia
- alpha-subunits
- biphenyls
- catechols
-
chlorinated
-
dioxygenation
-
1,2-dioxygenase
- 1,2,4,5-tetrachlorobenzene
- 1,2,4-trichlorobenzene
- naphthalene
-
dichlorobenzenes
-
biosurfactant
-
chloromuconate
-
meta-cleavage
-
dehalogenation
- 3-chlorobenzoate
-
cycloisomerase
- synthesis
-
dioxygenolytic
-
chloroaromatic
- 3-oxoadipate
- 1,3-dichlorobenzene
The enzyme appears in viruses and cellular organisms
Reaction Schemes
Synonyms
chlorobenzene dioxygenase, tetrachlorobenzene dioxygenase, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
TecA
TecA
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
chlorobenzene + NADH + H+ + O2 = (1R,2R)-3-chlorocyclohexa-3,5-diene-1,2-diol + NAD+
-
-
-
-
PATHWAY SOURCE
PATHWAYS
-
-, -, -, -, -, -, -, -, -, -
SYSTEMATIC NAME
IUBMB Comments
chlorobenzene,NADH:oxygen oxidoreductase (1,2-hydroxylating)
This bacterial enzyme is a class IIB dioxygenase, comprising three components - a heterodimeric terminal dioxygenase, a ferredoxin protein, and a ferredoxin reductase. The enzyme acts on a range of aromatic compounds, including mono-, di-, tri-, and tetra-chlorinated benzenes and toluenes.
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
1,4-dimethylbenzene + NADH + H+ + O2
? + NAD+
-
oxidized with low efficiency
-
-
?
2,3-dichlorotoluene + NADH + H+ + O2
2,3-dichlorobenzyl alcohol + NAD+
-
-
-
-
?
2,4,5-trichlorotoluene + NADH + H+ + O2
2,4,5-trichlorobenzyl alcohol + NAD+
-
-
-
-
?
2,6-dichlorotoluene + NADH + H+ + O2
2,6-dichlorobenzyl alcohol + NAD+
-
-
-
-
?
2-bromobenzonitrile + NADH + H+ + O2
cis-1,2-dihydroxy-3-cyanocyclohexa-4-bromo-3,5-diene + NAD+
Q52383; Q52384; Q52385; Q52386
-
-
-
?
2-chlorobenzonitrile + NADH + H+ + O2
cis-1,2-dihydroxy-3-cyanocyclohexa-4-chloro-3,5-diene + NAD+
Q52383; Q52384; Q52385; Q52386
-
-
-
?
2-fluorobenzonitrile + NADH + H+ + O2
cis-1,2-dihydroxy-3-cyanocyclohexa-4-fluoro-3,5-diene + NAD+
Q52383; Q52384; Q52385; Q52386
-
-
-
?
3,5-dichlorotoluene + NADH + H+ + O2
3,5-dichlorobenzyl alcohol + NAD+
-
-
-
-
?
3-fluorobenzonitrile + NADH + H+ + O2
cis-1,2-dihydroxy-3-cyanocyclohexa-5-fluoro-3,5-diene + NAD+
Q52383; Q52384; Q52385; Q52386
-
-
-
?
4-chlorobenzonitrile + NADH + H+ + O2
cis-1,2-dihydroxy-3-cyanocyclohexa-6-chloro-3,5-diene + NAD+
Q52383; Q52384; Q52385; Q52386
-
-
-
?
4-fluorobenzonitrile + NADH + H+ + O2
cis-1,2-dihydroxy-3-cyanocyclohexa-6-fluoro-3,5-diene + NAD+
Q52383; Q52384; Q52385; Q52386
-
-
-
?
4-methylbenzonitrile + NADH + H+ + O2
cis-1,2-dihydroxy-3-cyanocyclohexa-6-methyl-3,5-diene + NAD+
Q52383; Q52384; Q52385; Q52386
-
-
-
?
benzonitrile + NADH + H+ + O2
cis-1,2-dihydroxy-3-cyanocyclohexa-3,5-diene + NAD+
Q52383; Q52384; Q52385; Q52386
-
-
-
?
benzyl cyanide + NADH + H+ + O2
cis-1,2-dihydroxy-3,5-cyclohexadienyl acetonitrile + NAD+
Q52383; Q52384; Q52385; Q52386
-
-
-
?
cinnamonitrile + NADH + H+ + O2
trans-3-[(5S,6R)-5,6-dihydroxycyclo-hexa-1,3-dienyl]-acrylonitrile + NAD+
Q52383; Q52384; Q52385; Q52386
-
-
-
?
cinnamonitrile + NADH + H+ + O2
trans-3-[(5S,6R)-5,6-dihydroxycyclohexa-1,3-dienyl]-acrylonitrile + NAD+
Q52383; Q52384; Q52385; Q52386
-
-
-
?
methylbenzene + NADH + H+ + O2
? + NAD+
-
oxidized with low efficiency
-
-
?
1,2,4,5-tetrachlorobenzene + NADH + H+ + O2
? + NAD+
-
the enzyme dioxygenolytically attacks a chlorosubstituted carbon atom of Cl4-benzene, thereby forming an unstable diol intermediate which spontaneously rearomatizes with concomitant chloride elimination to the corresponding 3,4,6-trichlorocatechol (Cl3-catechol)
-
-
?
chlorobenzene + NADH + H+ + O2
(1R,2R)-3-chlorocyclohexa-3,5-diene-1,2-diol + NAD+
-
-
-
-
?
chlorobenzene + NADH + H+ + O2
(1R,2R)-3-chlorocyclohexa-3,5-diene-1,2-diol + NAD+
-
-
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Q52383: large subunit (tcbAa), Q52384: small subunit (tcbAb), Q52385: ferredoxin (tcbAc), Q52386: NADH-ferredoxin reductase (tcbAd)
Q52383; Q52384; Q52385; Q52386
UniProt
Q52383: large subunit (tcbAa), Q52384: small subunit (tcbAb), Q52385: ferredoxin (tcbAc), Q52386: NADH-ferredoxin reductase (tcbAd); the tcbA and tcbB genes for chlorobenzene dioxygenase and dehydrogenase are located on a transposable element, Tn5280
Q52383; Q52384; Q52385; Q52386
UniProt
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
Q52383; Q52384; Q52385; Q52386
chlorobenzene dioxygenase of Pseudomonas sp. strain P51 is linked evolutionarily to the enzymes for benzene and toluene degradation. The chlorobenzene dioxygenase originates from a toluene or benzene degradation pathway, probably by horizontal gene transfer
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
Q52383; Q52384; Q52385; Q52386
chlorobenzene dioxygenase is a four-protein complex, formed by the gene products of tcbAa for the large subunit of the terminal oxygenase, tcbAb for the small subunit, tcbAc for the ferredoxin, and tcbAd for the NADH reductase
additional information
Rhodococcus sp. MS11
-
the amino acid sequence of the amplified part of the alpha-subunit of the chlorobenzene dioxygenase of Rhodococcus sp. strain MS11 shows 99% identity to the alpha-subunit of the chlorobenzene dioxygenase from Cupriavidus sp. PS12 and the parts of both alpha-subunits responsible for substrate specificity were identical
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
chlorobenzene dioxygenase genes tcbAa, tcbAb, tcbAc, and tcbAd are expressed in Escherichia coli JM101 (pTEZ30) under the control of the alk regulatory system of Pseudomonas oleovorans GPo1
Q52383; Q52384; Q52385; Q52386
cloned under the strict control of the Palk promoter of Pseudomonas putida GPo1. Escherichia coli JM101 cells carrying the resulting plasmid pTEZ30 are used for the biotransformation of benzonitrile in a 2-l stirred tank bioreactor
Q52383; Q52384; Q52385; Q52386
Escherichia coli cells producing recombinant TecA enzyme dioxygenate and simultaneously eliminate a halogen substituent from 1,2,4,5-tetrachlorobenzene but show no activity toward benzene
-
the tcbA and tcbB genes for chlorobenzene dioxygenase and dehydrogenase are located on a transposable element, Tn5280. Tn5280 shows the features of a composite bacterial transposon with iso-insertion elements (IS1066 and IS1067) at each end of the transposon oriented in an inverted position. When a 12-kb Hindlll fragment of pP51 containing Tn5280 is cloned in the suicide donor plasmid pSUP202, marked with a kanamycin resistance gene, and introduced into Pseudomonas putida KT2442, TnS280 is found to transpose into the genome at random and in single copy. The presence of the catabolic genes tcbA and tcbB on TnS280 suggests a mechanism by which gene clusters can be mobilized as gene cassettes and joined with others to form novel catabolic pathways
Q52383; Q52384; Q52385; Q52386
the tecB gene is cloned into Escherichia coli DH5a together with the tecA gene into Escherichia coli DH5alpha
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
synthesis
synthesis
Q52383; Q52384; Q52385; Q52386
asymmetric dihydroxylation of non-natural cinnamonitrile to trans-3-[(5S,6R)-5,6-dihydroxycyclohexa-1,3-dienyl]-acrylonitrile by chlorobenzene dioxygenase in recombinant Escherichia coli JM101 (pTEZ30). Recombinant hosts with a strong expression system, such as Escherichia coli JM101 (pTEZ30), can be used to produce dioxygenases efficiently to performcis-dihydroxylations up to technical scales. The cells should be maintained in ametabolically active state duringthe biotransformation in order to increase and maintain the volumetric productivity for long-term reactions
synthesis
Q52383; Q52384; Q52385; Q52386
the enzyme is cloned under the strict control of the Palk promoter of Pseudomonas putida GPo1 and expressed in Escherichia coli JM101 cells carrying the resulting plasmid pTEZ30. Cells are used for regio- and stereoselective dihydroxylation of benzonitrile, ortho-, meta- and para-substituted benzonitriles, as well as cinnamonitrile and benzyl cyanide. cis-Dihydroxylations are at the 1,2 positions and the products have 42.9 to 97.1% enantiomeric excess
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Yildirim, S.; Zezula, J.; Hudlicky, T.; Witholt, B.; Schmid, A.
Asymmetric dihydroxylation of cinnamonitrile to trans-3-[(5S,6R)-5,6-dihydroxycyclohexa-1,3-dienyl]-acrylonitrile using chlorobenzene dioxygenase in Escherichia coli (pTEZ30)
Adv. Synth. Catal.
346
933-942
2004
Pseudomonas sp. P51 (Q52383 AND Q52384 AND Q52385 AND Q52386)
-
Yildirim, S.; Franko, T.; Wohlgemuth, R.; Kohler, H.; Witholt, B.; Schmid, A.
Recombinant chlorobenzene dioxygenase from Pseudomonas sp. P51 A biocatalyst for regioselective oxidation of aromatic nitriles
Adv. Synth. Catal.
347
1060-1072
2005
Pseudomonas sp. P51 (Q52383 AND Q52384 AND Q52385 AND Q52386)
-
Spiess, E.; Sommer, C.; Gorisch, H.
Degradation of 1,4-dichlorobenzene by Xanthobacter flavus 14p1
Appl. Environ. Microbiol.
61
3884-3888
1995
Xanthobacter flavus
Pollmann, K.; Beil, S.; Pieper, D.H.
Transformation of chlorinated benzenes and toluenes by Ralstonia sp. strain PS12 tecA (tetrachlorobenzene dioxygenase) and tecB (chlorobenzene dihydrodiol dehydrogenase) gene products
Appl. Environ. Microbiol.
67
4057-4063
2001
Cupriavidus sp. PS12
Sommer, C.; Goerisch, H.
Enzymology of the degradation of (di)chlorobenzenes by Xanthobacter flavus 14p1
Arch. Microbiol.
167
384-391
1997
Xanthobacter flavus 14p1
Beil, S.; Happe, B.; Timmis, K.N.; Pieper, D.H.
Genetic and biochemical characterization of the broad spectrum chlorobenzene dioxygenase from Burkholderia sp. strain PS12 - dechlorination of 1,2,4,5-tetrachlorobenzene
Eur. J. Biochem.
247
190-199
1997
Cupriavidus sp. PS12
van der Meer, J.R.; Zehnder, A.J.; de Vos, W.M.
Identification of a novel composite transposable element, Tn5280, carrying chlorobenzene dioxygenase genes of Pseudomonas sp. strain P51
J. Bacteriol.
173
7077-7083
1991
Pseudomonas sp. P51 (Q52383 AND Q52384 AND Q52385 AND Q52386)
Beil, S.; Mason, J.R.; Timmis, K.N.; Pieper, D.H.
Identification of chlorobenzene dioxygenase sequence elements involved in dechlorination of 1,2,4,5-tetrachlorobenzene
J. Bacteriol.
180
5520-5528
1998
Cupriavidus sp. PS12
Werlen, C.; Kohler, H.P.; van der Meer, J.R.
The broad substrate chlorobenzene dioxygenase and cis-chlorobenzene dihydrodiol dehydrogenase of Pseudomonas sp. strain P51 are linked evolutionarily to the enzymes for benzene and toluene degradation
J. Biol. Chem.
271
4009-4016
1996
Pseudomonas sp. P51 (Q52383 AND Q52384 AND Q52385 AND Q52386)
EXTERNAL LINKS (specific for EC-Number 1.14.12.26)
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
Legal
Curated at
Member of
