Information on EC 3.5.5.6 - bromoxynil nitrilase

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The expected taxonomic range for this enzyme is: Klebsiella pneumoniae subsp. ozaenae

EC NUMBER
COMMENTARY hide
3.5.5.6
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RECOMMENDED NAME
GeneOntology No.
bromoxynil nitrilase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
3,5-dibromo-4-hydroxybenzonitrile + 2 H2O = 3,5-dibromo-4-hydroxybenzoate + NH3
show the reaction diagram
highly specific; involved in the bacterial degradation of the herbicide bromoxynil. Highly specific
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of nitriles
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-
-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Fluorobenzoate degradation
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Microbial metabolism in diverse environments
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SYSTEMATIC NAME
IUBMB Comments
3,5-dibromo-4-hydroxybenzonitrile aminohydrolase
Involved in the bacterial degradation of the herbicide bromoxynil. Highly specific.
CAS REGISTRY NUMBER
COMMENTARY hide
157857-12-0
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
3,5-dibromo-4-hydroxybenzonitrile + H2O
3,5-dibromo-4-hydroxybenzoic acid + NH3
show the reaction diagram
3,5-dichloro-4-hydroxybenzonitrile + H2O
3,5-dichloro-4-hydroxybenzoic acid + NH3
show the reaction diagram
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chloroxynil
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-
?
3,5-diiodo-4-hydroxybenzonitrile + H2O
3,5-diiodo-4-hydroxybenzoic acid + NH3
show the reaction diagram
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ioxynil
-
-
?
4-hydroxybenzonitrile + H2O
4-hydroxybenzoic acid + NH3
show the reaction diagram
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low activity
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-
?
5-bromo-4-hydroxybenzonitrile + H2O
5-bromo-4-hydroxybenzoic acid + NH3
show the reaction diagram
-
-
-
-
?
additional information
?
-
-
no detectable activity when benzonitrile is utilized as substrate, nor does 3,5-dibromo-4-hydroxybenzamide act as a substrate for the enzyme
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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
3,5-dibromo-4-hydroxybenzonitrile + H2O
3,5-dibromo-4-hydroxybenzoic acid + NH3
show the reaction diagram
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involved in bacterial degradation of the herbizide bromoxynil
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?
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Ag+
-
0.01 mM, 93.8% of maximum activity, 0.1 mM: 2.5% of maximal activity
Cu2+
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0.01 mM, 75% of maximal activity, 0.1 mM: 31.3% of maximal activity
iodoacetate
-
0.01 mM: 5% of maximal activity
p-hydroxymercuribenzoate
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0.0005 mM, 2.5% of maximal activity
Phenylmercuriacetate
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0.0005 mM, 4.3% of maximal activity
additional information
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Ca2+, Co2+, Mg2+, Mn2+, Zn2+ at 0.1 mM, as well as EDTA or HCN, or monovalent cations at 500 mM are no inhibitors
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.31
3,5-dibromo-4-hydroxybenzonitrile
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pH 9.2, 35°C
0.83
3,5-Dichloro-4-hydroxybenzonitrile
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pH 9.2, 35°C
0.55
3,5-Diiodo-4-hydroxybenzonitrile
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pH 9.2, 35°C
0.91
5-Bromo-4-hydroxybenzonitrile
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pH 9.2, 35°C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25.7
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3,5-dibromo-4-hydroxybenzonitrile
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.5 - 10.5
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15% of optimal activity demonstrated at pH 7.0, with a rapid rise to pH 9.2 and a steep decline approaching pH 10.6
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.4
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calculated pI, derived from the amino acid composition, this is in contrast to the final purification step using a chromatofocusing column, the active form of the enzyme binds to the column at pH 4.0 and must be eluted with high salt concentrations, this observation indicates that the actual pI for the bromoxynil-specific nitrilase must be lower than 4.0
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
38100
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2 * 37000 or 2 * 38100
72000
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recombinant enzyme, gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
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2 * 37000, SDS-PAGE; 2 * 38100,homodimer, nucleotide sequence analysis
homodimer
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2 * 37000 or 2 * 38100
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
DNA segment cloned and expressed in Escherichia coli MM 294, nucleotide sequence analysis of the bxn gene
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
agriculture
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recent experiments indicate that expression of this bacterial nitrilase in transgenic plants results in high levels of resistance to the herbicide bromoxynil