Information on EC 5.4.4.1 - (hydroxyamino)benzene mutase

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The expected taxonomic range for this enzyme is: Proteobacteria

EC NUMBER
COMMENTARY
5.4.4.1
-
RECOMMENDED NAME
GeneOntology No.
(hydroxyamino)benzene mutase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
(hydroxyamino)benzene = 2-aminophenol
show the reaction diagram
-
-
-
-
(hydroxyamino)benzene = 2-aminophenol
show the reaction diagram
intramolecular hydroxyl transfer
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(hydroxyamino)benzene = 2-aminophenol
show the reaction diagram
intramolecular hydroxyl transfer; proposed intramolecular rearrangment mechanism, different from the nonenzymatic Bamberger reaction which proceeds via intermolecular hydroxyl transfer
-
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
dismutation
-
-
-
-
PATHWAY
KEGG Link
MetaCyc Link
Aminobenzoate degradation
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Microbial metabolism in diverse environments
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nitrobenzene degradation I
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SYSTEMATIC NAME
IUBMB Comments
(hydroxyamino)benzene hydroxymutase
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SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
CnbB
Comamonas sp. CNB-1
-
-
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HAB mutase
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-
-
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hydroxylaminobenzene hydroxymutase
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-
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hydroxylaminobenzene mutase
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-
-
-
CAS REGISTRY NUMBER
COMMENTARY
261765-91-7
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ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
strain CNB-1 able to grow on 4-chloronitrobenzene and nitrobenzene as sole carbon sources. Enzymes involved in 4-chloronitrobenzene and nitrobenzene degradation are chloronitrobenzene nitroreductase, hydroxylaminobenzene mutase, 2-aminophenol 1,6-dioxygenase, and 2-aminomuconic semialdehyde dehydrogenase. When these enzymes are coupled in vitro, they sequentially catalyze the conversions of 4-chloronitrobenzene to 2-amino-5-chloromuconic acid and nitrobenzene to 2-aminomuconic acid
-
-
Manually annotated by BRENDA team
Comamonas sp. CNB-1
strain CNB-1 able to grow on 4-chloronitrobenzene and nitrobenzene as sole carbon sources. Enzymes involved in 4-chloronitrobenzene and nitrobenzene degradation are chloronitrobenzene nitroreductase, hydroxylaminobenzene mutase, 2-aminophenol 1,6-dioxygenase, and 2-aminomuconic semialdehyde dehydrogenase. When these enzymes are coupled in vitro, they sequentially catalyze the conversions of 4-chloronitrobenzene to 2-amino-5-chloromuconic acid and nitrobenzene to 2-aminomuconic acid
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-
Manually annotated by BRENDA team
encoded on 2 genes, habA and habB, only habA is expressed; strain JS45
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Manually annotated by BRENDA team
expression in Escherichia coli, together with nitrobenzene nitroreductase
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-
Manually annotated by BRENDA team
Pseudomonas pseudoalcaligenes JS45
strain JS45
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-
Manually annotated by BRENDA team
strain ZWL73
-
-
Manually annotated by BRENDA team
Pseudomonas putida ZWL73
strain ZWL73
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-
Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(hydroxyamino)benzene
2-aminophenol
show the reaction diagram
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-
-
-
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(hydroxyamino)benzene
2-aminophenol
show the reaction diagram
-
highly selective for the production of the ortho-isomer
highly selective for the production of the ortho-isomer
-
(hydroxyamino)benzene
2-aminophenol
show the reaction diagram
Pseudomonas pseudoalcaligenes, Pseudomonas pseudoalcaligenes JS45
-
highly selective for the production of the ortho-isomer
highly selective for the production of the ortho-isomer
?
(hydroxyamino)benzene
2-aminophenol
show the reaction diagram
Pseudomonas pseudoalcaligenes JS45
-
highly selective for the production of the ortho-isomer
highly selective for the production of the ortho-isomer
-
4-chloro-(hydroxyamino)benzene
2-amino-5-chlorophenol
show the reaction diagram
Pseudomonas putida, Pseudomonas putida ZWL73
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in presence of chloronitrobenzene nitroreductase, degradation of 4-chloronitrobenzene to 2-amino-5-chlorophenol, which is the ring-cleavage substrate in degradation of 4-chloronitrobenzene
-
-
?
4-hydoxyaminobiphenyl ether
2-amino-5-phenoxyphenol
show the reaction diagram
Pseudomonas pseudoalcaligenes, Pseudomonas pseudoalcaligenes JS45
-
-
-
?
4-hydroxyylaminobenzoate
4-amino-3-hydroxybenzoate
show the reaction diagram
-
-
-
?
additional information
?
-
Comamonas sp., Comamonas sp. CNB-1
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enzymes involved in 4-chloronitrobenzene and nitrobenzene degradation are chloronitrobenzene nitroreductase, hydroxylaminobenzene mutase, 2-aminophenol 1,6-dioxygenase, and 2-aminomuconic semialdehyde dehydrogenase. When these enzymes are coupled in vitro, they sequentially catalyze the conversions of 4-chloronitrobenzene to 2-amino-5-chloromuconic acid and nitrobenzene to 2-aminomuconic acid
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-
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INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
Zn2+
-
1 mM, 70% inhibition
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.15
-
(hydroxylamino)benzene
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at pH 7.0
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
pH RANGE
pH RANGE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
6.5
9.5
-
56% and 59% of maximal activity at pH 6.5 and pH 9.5 respectively
LOCALIZATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
additional information
-
not an integral membrane protein
-
Manually annotated by BRENDA team
additional information
Pseudomonas pseudoalcaligenes JS45
-
not an integral membrane protein
-
-
Manually annotated by BRENDA team
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
additional information
-
-
mutase forms high-molecular-mass complexes which elute with the void-volume, mutase tends to associate even in the presence of SDS
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
?
-
x * 15951, calculated
?
Comamonas sp. CNB-1
-
x * 15951, calculated
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TEMPERATURE STABILITY
TEMPERATURE STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
60
-
-
recombinant HabA, inactivation above, 50% loss of activity at 70°C after 10 min
85
-
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recombinant HabB, no loss of activity after 10 min
GENERAL STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
mutase in crude extracts is stable in the presence of 2% SDS, the partially purified enzyme loses 50% activity in the presence of 0.1% SDS after 30 sec
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Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
Hitrap-SP/Hitrap-Q, filtration/precipitation, Cu2+-chelating chromatography
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recombinant enzyme
-
recombinant HabB and HabA
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Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
expression in Escherichia coli
-
expression of habA and habB in Escherichia coli
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expression of HabB mutase in Escherichia coli
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expression in Escherichia coli
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APPLICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
synthesis
-
expression of enzyme plus nitrobenzene nitroreductase in Escherichia coli. Rapid and stoichiometric conversion of nitrobenzene to 2-aminophenol, of 2-nitroacetophenone to 2-amino-3-hydroxyacetophenone, and of 3-nitroacetophenone to 3-amino-2-hydroxyacetophenone, as well as further conversions. Final yields of aminophenols after extraction and recovery are over 64%