Information on EC 1.14.12.13 - 2-halobenzoate 1,2-dioxygenase

Word Map on EC 1.14.12.13
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Specify your search results
Select one or more organisms in this record:
Show additional data
Do not include text mining results
Include (text mining) results (more...)
Include results (AMENDA + additional results, but less precise; more...)

The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
1.14.12.13
-
RECOMMENDED NAME
GeneOntology No.
2-halobenzoate 1,2-dioxygenase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
a 2-halobenzoate + NADH + H+ + O2 = catechol + a halide anion + NAD+ + CO2
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
decarboxylation
-
-
-
-
dehalogenation
-
-
-
-
hydroxylation
-
-
-
-
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
2-chlorobenzoate degradation
-
-
Fluorobenzoate degradation
-
-
Microbial metabolism in diverse environments
-
-
SYSTEMATIC NAME
IUBMB Comments
2-halobenzoate,NADH:oxygen oxidoreductase (1,2-hydroxylating, dehalogenating, decarboxylating)
A multicomponent enzyme system composed of a dioxygenase component and an electron transfer component. The latter contains FAD. The enzyme, characterized from the bacterium Burkholderia cepacia 2CBS, has a broad substrate specificity. Substrates include 2-fluorobenzoate, 2-chlorobenzoate, 2-bromobenzoate, and 2-iodobenzoate, which are processed in this order of preference.
CAS REGISTRY NUMBER
COMMENTARY hide
125268-83-9
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
strain 2CBS
-
-
Manually annotated by BRENDA team
strain NK8 isolated from soil
-
-
Manually annotated by BRENDA team
-
UniProt
Manually annotated by BRENDA team
strain 142
-
-
Manually annotated by BRENDA team
strain 142
-
-
Manually annotated by BRENDA team
CPE2
-
-
Manually annotated by BRENDA team
CPE2
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2,4-dichlorobenzoate + NADH + O2
4-chlorocatechol + chloride + NAD+ + CO2
show the reaction diagram
2,5-dichlorobenzoate + NADH + O2
4-chlorocatechol + chloride + NAD+ + CO2
show the reaction diagram
2,5-dichlorobenzoate + NADH + O2
4-chlorocatechol + NAD+ + Cl- + CO2
show the reaction diagram
2,6-dichlorobenzoate + NADH + O2
? + NAD+ + CO2
show the reaction diagram
-
19% of the activity with 2-chlorobenzoate
-
-
?
2-amino-4-chlorobenzoate + NADH + O2
? + NAD+ + CO2
show the reaction diagram
-
28% of the activity with 2-chlorobenzoate
-
-
?
2-amino-5-chlorobenzoate + NADH + O2
? + NAD+ + CO2
show the reaction diagram
-
27% of the activity with 2-chlorobenzoate
-
-
?
2-aminobenzoate + NADH + O2
? + NAD+ + CO2
show the reaction diagram
-
-
-
-
?
2-bromobenzoate + NADH + O2
catechol + bromide + NAD+ + CO2
show the reaction diagram
2-chloro-5-bromobenzoate + NADH + O2
4-bromocatechol + chloride + NAD+ + CO2
show the reaction diagram
-
50% of the activity with 2-chlorobenzoate
-
-
?
2-chlorobenzoate + NADH + O2
3-chlorocatechol + NAD+ + O2
show the reaction diagram
2-chlorobenzoate + NADH + O2
catechol + chloride + NAD+ + CO2
show the reaction diagram
2-fluorobenzoate + NADH + O2
catechol + fluoride + NAD+ + CO2
show the reaction diagram
2-hydroxybenzoate + NADH + O2
catechol + ? + NAD+ + CO2
show the reaction diagram
-
-
-
?
2-iodobenzoate + NADH + O2
catechol + iodide + NAD+ + CO2
show the reaction diagram
2-methoxybenzoate + NADH + O2
catechol + ? + NAD+ + CO2
show the reaction diagram
-
-
-
?
2-methylbenzoate + NADH + O2
o-cresol + ? + NAD+ + CO2
show the reaction diagram
3,4-dichlorobenzoate + NADH + O2
? + NAD+ + CO2
show the reaction diagram
-
10% of the activity with 2-chlorobenzoate
-
-
?
3,5-dichlorobenzoate + NADH + O2
? + NAD+ + CO2
show the reaction diagram
-
16% of the activity with 2-chlorobenzoate
-
-
?
3-chlorobenzoate + NADH + O2
3-chlorocatechol + NAD+ + CO2
show the reaction diagram
-
-
-
?
3-chlorobenzoate + NADH + O2
4-chlorocatechol + NAD+ + CO2
show the reaction diagram
3-chlorobenzoate + NADH + O2
? + NAD+ + CO2
show the reaction diagram
-
-
-
?
3-chlorobenzoate + NADH + O2
catechol + chloride + NAD+ + CO2
show the reaction diagram
-
15% of the activity with 2-chlorobenzoate
-
-
?
4-amino-2-chlorobenzoate + NADH + O2
4-aminocatechol + chloride + NAD+ + CO2
show the reaction diagram
-
21% of the activity with 2-chlorobenzoate
-
-
?
4-chlorobenzoate + NADH + O2
4-chlorocatechol + NAD+ + CO2
show the reaction diagram
-
-
-
?
4-chlorobenzoate + NADH + O2
catechol + chloride + NAD+ + CO2
show the reaction diagram
-
21% of the activity with 2-chlorobenzoate
-
-
?
anthranilate + NADH + O2
catechol + ? + NAD+ + CO2
show the reaction diagram
-
-
-
?
benzoate + NADH + O2
3,5-cyclohexadiene-1,2-diol + NAD+ + CO2
show the reaction diagram
-
37% of the activity with 2-chlorobenzoate
-
-
?
benzoate + NADH + O2
3,5-cyclohexadiene-1,2-diol-1-carboxylic acid + NAD+ + CO2
show the reaction diagram
benzoate + NADH + O2
catechol + NAD+ + CO2
show the reaction diagram
additional information
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
2,5-dichlorobenzoate + NADH + O2
4-chlorocatechol + NAD+ + Cl- + CO2
show the reaction diagram
2-chlorobenzoate + NADH + O2
catechol + chloride + NAD+ + CO2
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
FMN
-
little increase of activity by addition of 0.002 mM
additional information
-
NADPH may not substitute for NADH
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Sulfide
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2,2'-dipyridyl
-
100% inhibition at 1 mM
Cu2+
-
100% inhibition compared to the activity without any metal
FAD
-
slight inhibition
Fe2+
-
slight inhibition
iodoacetate
-
55% inhibition at 2 mM
KCN
-
40% inhibition at 2 mM
N-ethylmaleimide
-
100% inhibition at 2 mM
Ni2+
-
25% inhibition compared to the activity without any metal
o-phenanthroline
-
100% inhibition at 0.5 mM
p-chloromercuribenzoate
-
17% inhibition at 0.005 mM
Zn2+
-
40% inhibition compared to the activity without any metal
additional information
-
no inhibition with sodium azide
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.063 - 0.079
2,5-dichlorobenzoate
-
cells grown on 2-chlorobenzoate or 2,5-dichlorobenzoate
0.023 - 0.117
2-Chlorobenzoate
0.079
NADH
-
component B
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.0013
-
cells are grown on 3-chlorobenzoate, benzoate as substrate for assay
0.0024
-
recombinant cells are grown on LB/IPTG, benzoate as substrate for assay
0.0032
-
cells are grown on benzoate, benzoate as substrate for assay
0.006
-
with 4-chlorobenzoate as substrate
0.0085
-
crude extract, 3.4 mg protein per ml in the assay
0.018 - 0.023
-
cells grown on 2-clorobenzoate or 2,5-dichlorobenzoate, enzyme activity for the conversion of both substrates
0.032
-
with 2-iodobenzoate as substrate
0.043
-
after anion exchange: fraction A + B + NADH + Fe2+
0.073
-
with 3-chlorobenzoate as substrate
0.195
-
with benzoate as substrate
0.303
-
with 2-bromobenzoate as substrate
0.458
-
with 2-chlorobenzoate as substrate
0.53
-
activity of component A after gel filtration in presence of component B
1.57
-
30C, pH 6.5
4
-
activity of component B in presence of component A
additional information
-
activity is similarly influenced by pH, temperature, concentration of oxygen, protein, Fe2+, FAD and NADH in assay medium independent if the cells are grown on 2-chlorobenzoate or 2,5-dichlorobenzoate
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.6
-
assay at
7.4
-
assay at, assay with cells
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.5 - 7.5
-
assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
13000
-
gel filtration
37500 - 38000
-
component B, gel filtration
200000 - 220000
-
component A, gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hexamer
-
3 * 52000, 3 * 20000, alpha3,beta3 structure of component A, SDS-PAGE
monomer
oligomer
-
x * 19500, x * 52400, alpha3beta3, small and large subunit of the oxygenase component, SDS-PAGE
additional information
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
sucrose has stabilizing effect
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20C component A, 80-85% loss of activity
-
-20C, component A, 20% glycerol, 50% loss of activity
-
-20C, component B, 20% sucrose, 2 weeks, 25% loss of activity
-
-80C or -20C, component B, 2 weeks, 70% loss of activity
-
-80C or -20C, component B, 20% glycerol, 2 weeks, 15% loss of activity
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
anion exchange
-
anion-exchange
-
by gel filtration
component A: anion-exchange, gel filtration, component B: anion-exchange, affinity and adsorption chromatography
-
gel filtration of oxygenase component
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Escherichia coli TG1, JM105, MV1190 and Pseudomonas putida KT2440 are used as host strains
-
expression in Cupriavidus necator strain H850
-
several constructs with relevant genes are expressed in Escherichia coli DH5alpha and S17-1 lambdapir
-
several gene constructs are expressed in Escherichia coli DH5alpha, S17-1, S17-lambdapir and HMS174(DE3)
-
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
Show AA Sequence (210 entries)
Please use the Sequence Search for a certain query.