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EC Tree
IUBMB Comments Involved in the bacterial degradation of the herbicide bromoxynil. Highly specific.
The expected taxonomic range for this enzyme is: Klebsiella pneumoniae subsp. ozaenae
Synonyms
bromoxynil-specific nitrilase,
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bromoxynil-specific nitrilase
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3,5-dibromo-4-hydroxybenzonitrile + 2 H2O = 3,5-dibromo-4-hydroxybenzoate + NH3
3,5-dibromo-4-hydroxybenzonitrile + 2 H2O = 3,5-dibromo-4-hydroxybenzoate + NH3
highly specific
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3,5-dibromo-4-hydroxybenzonitrile + 2 H2O = 3,5-dibromo-4-hydroxybenzoate + NH3
involved in the bacterial degradation of the herbicide bromoxynil. Highly specific
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hydrolysis of nitriles
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3,5-dibromo-4-hydroxybenzonitrile aminohydrolase
Involved in the bacterial degradation of the herbicide bromoxynil. Highly specific.
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3,5-dibromo-4-hydroxybenzonitrile + H2O
3,5-dibromo-4-hydroxybenzoic acid + NH3
3,5-dichloro-4-hydroxybenzonitrile + H2O
3,5-dichloro-4-hydroxybenzoic acid + NH3
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chloroxynil
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?
3,5-diiodo-4-hydroxybenzonitrile + H2O
3,5-diiodo-4-hydroxybenzoic acid + NH3
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ioxynil
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?
4-hydroxybenzonitrile + H2O
4-hydroxybenzoic acid + NH3
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low activity
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?
5-bromo-4-hydroxybenzonitrile + H2O
5-bromo-4-hydroxybenzoic acid + NH3
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?
additional information
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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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?
3,5-dibromo-4-hydroxybenzonitrile + H2O
3,5-dibromo-4-hydroxybenzoic acid + NH3
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bromoxynil
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?
3,5-dibromo-4-hydroxybenzonitrile + H2O
3,5-dibromo-4-hydroxybenzoic acid + NH3
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involved in bacterial degradation of the herbizide bromoxynil
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?
3,5-dibromo-4-hydroxybenzonitrile + H2O
3,5-dibromo-4-hydroxybenzoic acid + NH3
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i.e. bromoxynil, the enzyme is highly specific for this substrate
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?
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3,5-dibromo-4-hydroxybenzonitrile + H2O
3,5-dibromo-4-hydroxybenzoic acid + NH3
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involved in bacterial degradation of the herbizide bromoxynil
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?
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Ag+
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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
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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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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
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25.7
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3,5-dibromo-4-hydroxybenzonitrile
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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
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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
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brenda
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38100
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2 * 37000 or 2 * 38100
72000
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recombinant enzyme, gel filtration
37000
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2 * 37000, SDS-PAGE
37000
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2 * 37000 or 2 * 38100
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homodimer
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2 * 37000 or 2 * 38100
dimer
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2 * 37000, SDS-PAGE
dimer
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2 * 38100,homodimer, nucleotide sequence analysis
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DNA segment cloned and expressed in Escherichia coli MM 294, nucleotide sequence analysis of the bxn gene
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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
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Stalker, D.M.; Malyj, L.D.; McBride, K.E.
Purification and properties of a nitrilase specific for the herbicide bromoxynil and corresponding nucleotide sequence analysis of the bxn gene
J. Biol. Chem.
263
6310-6314
1988
Klebsiella pneumoniae subsp. ozaenae
brenda
Thuku, R.; Brady, D.; Benedik, M.; Sewell, B.
Microbial nitrilases: Versatile, spiral forming, industrial enzymes
J. Appl. Microbiol.
106
703-727
2009
Klebsiella pneumoniae subsp. ozaenae
brenda
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