Substrates: 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 Products: -
Substrates: 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 Products: -
Substrates: 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 Products: -
Substrates: 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 Products: -
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
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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GENERAL STABILITY
ORGANISM
UNIPROT
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
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%
Production of 2-amino-5-phenoxyphenol from 4-nitrobiphenyl ether using nitrobenzene nitroreductase and hydroxylaminobenzene mutase from Pseudomonas pseudoalcaligenes JS45
Characterization of hydroxylaminobenzene mutase from pNBZ139 cloned from Pseudomonas pseudoalcaligenes JS45: a highly associated SDS-stable enzyme catalyzing an intramolecular transfer of hydroxy groups
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