Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
2,2',3-trihydroxybiphenylether + O2
?
-
-
-
?
2,3-dihydroxybiphenyl + O2
?
2,3-dihydroxybiphenylcatechol + O2
?
Halalkalibacterium ligniniphilum
WP_017726464.1
% of the activity as compared to 3-ethylcatechol
-
-
?
2,4-dichlorophenol + O2
?
2,6-dichlorophenol + O2
?
-
-
-
-
?
3,4-dihydroxybenzoate + O2
?
3,4-dimethylcatechol + O2
2-hydroxy-5-methyl-6-oxo-hepta-2,4-dienoate
3,5-dichlorocatechol + O2
2-hydroxy-3,5-dimethyl-6-oxohexa-2,4-dienoic acid
30.8% of the activity as compared to catechol
-
-
?
3,5-dichlorocatechol + O2
?
3,5-dimethylcatechol + O2
2-hydroxy-3,5-dimethyl-6-oxohexa-2,4-dienoic acid
3-chlorocatechol + O2
2-chloro-2-hydroxy-6-oxohexa-2,4-dienoate
3-chlorocatechol + O2
2-hydroxy-6-oxohepta-2,4-dienoate
3-chlorocatechol + O2
3-chloro-2-hydroxymuconate semialdehyde
3-ethylcatechol + O2
?
Halalkalibacterium ligniniphilum
WP_017726464.1
best substrate. The enzyme can cleave the catechol ring when substitutions occur at C3 more efficiently than C4 substitutes. The enzyme can cleave aromatic compounds with two 6-carbon ring structures
-
-
?
3-formylcatechol + O2
3-formyl-2-hydroxymuconate semialdehyde
3-hydroxycatechol + O2
3-hydroxymuconic acid
3-isopropylcatechol + O2
?
3-methoxycatechol + O2
2-hydroxy-3-methoxy-6-oxohexa-2,4-dienoate
-
-
-
-
?
3-methoxycatechol + O2
2-hydroxy-3-methoxymuconate semialdehyde
3-methylcatechol + O2
2-hydroxy-3-methoxymuconate semialdehyde
211.7% compared to the activity with catechol
-
-
?
3-methylcatechol + O2
2-hydroxy-3-methylmuconate semialdehyde
3-methylcatechol + O2
2-hydroxy-3-methylmuconate-6-semialdehyde
-
-
-
-
?
3-methylcatechol + O2
2-hydroxy-6-oxohepta-2,4-dienoate
3-methylcatechol + O2
2-hydroxy-6-oxohepta-2,4-dienoic acid
3-methylcatechol + O2
cis,cis-2-hydroxy-6-oxohepta-2,4-dienoate
3-phenylcatechol + O2
2-hydroxy-3-phenylmuconate semialdehyde
-
-
-
?
3-sulfocatechol + O2 + H2O
(2E,4Z)-2-hydroxymuconate + bisulfite + H+
-
-
-
-
?
3-vinylcatechol + O2
?
-
-
-
-
?
4,5-dichlorocatechol + O2
?
4-bromocatechol + O2
4-bromo-2-hydroxymuconate semialdehyde
-
-
-
?
4-chlorocatechol + O2
4-chloro-2-hydroxymuconate semialdehyde
4-chlorocatechol + O2
5-chloro-2-hydroxy-6-oxohexa-2,4-dienoate
4-chlorocatechol + O2
5-chloro-2-hydroxymuconic semialdehyde
4-chlorophenol + O2
?
-
-
-
-
?
4-ethylcatechol + O2
4-ethyl-2-hydroxymuconate semialdehyde
4-fluorocatechol + O2
3-fluoro-2-hydroxy-6-oxohexa-2,4-dienoate
-
-
-
-
?
4-formylcatechol + O2
4-formyl-2-hydroxymuconate semialdehyde
4-hydroxymethylcatechol + O2
2-hydroxy-4-hydroxymethylmuconate semialdehyde
rapid inactivation of enzyme during turnover
-
-
?
4-methylcatechol + O2
2-hydroxy-3-methyl-6-oxohexa-2,4-dienoate
4-methylcatechol + O2
2-hydroxy-4-methyl-6-oxohexa-2,4-dienoate
4-methylcatechol + O2
2-hydroxy-4-methylmuconate semialdehyde
4-methylcatechol + O2
2-hydroxy-5-methyl-6-oxohexa-2,4-dienoate
4-n-butylcatechol + O2
?
activity is 1.85fold higher than with catechol
-
-
?
4-n-heptylcatechol + O2
?
45% of the activity with catechol
-
-
?
4-n-hexylcatechol + O2
?
53% of the activity with catechol
-
-
?
4-n-nonylcatechol + O2
?
10% of the activity with catechol
-
-
?
4-nitrocatechol + O2
2-hydroxy-4-nitromuconate semialdehyde
4-nitrophenol + O2
?
-
best substrate
-
-
?
alkylcatechol + O2
?
degradation of aromatic compounds
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
catechol + O2
2-hydroxymuconate-6-semialdehyde
catechol + O2
cis,cis-muconate
methanol + O2
?
-
-
-
-
?
methylbenzene + O2
?
-
-
-
-
?
phenol + O2
2-hydroxymuconic semialdehyde
propanol + O2
?
-
-
-
-
?
protocatechualdehyde + O2
?
protocatechuate + O2
?
-
-
-
-
?
tetrachlorohydroquinone + O2
?
-
immobilized enzyme, no activity with the free enzyme
-
-
?
additional information
?
-
2,3-dihydroxybiphenyl + O2
?
-
5% of the activity with catechol
-
-
?
2,3-dihydroxybiphenyl + O2
?
-
5% of the activity with catechol
-
-
?
2,3-dihydroxybiphenyl + O2
?
-
-
-
-
?
2,3-dihydroxybiphenyl + O2
?
-
-
-
-
?
2,3-dihydroxybiphenyl + O2
?
1.3% of the activity with 2,3-dihydroxybiphenyl
-
-
?
2,3-dihydroxybiphenyl + O2
?
1.3% of the activity with 2,3-dihydroxybiphenyl
-
-
?
2,3-dihydroxybiphenyl + O2
?
-
-
-
-
?
2,3-dihydroxybiphenyl + O2
?
poor substrate
-
-
?
2,3-dihydroxybiphenyl + O2
?
-
-
-
?
2,3-dihydroxybiphenyl + O2
?
-
-
-
?
2,3-dihydroxybiphenyl + O2
?
poor substrate
-
-
?
2,3-dihydroxybiphenyl + O2
?
-
-
-
-
?
2,3-dihydroxybiphenyl + O2
?
-
-
-
-
?
2,3-dihydroxybiphenyl + O2
?
-
-
-
-
?
2,3-dihydroxybiphenyl + O2
?
-
-
-
-
?
2,3-dihydroxybiphenyl + O2
?
-
-
-
-
?
2,3-dihydroxybiphenyl + O2
?
9.47% compared to the activity with catechol
-
-
?
2,3-dihydroxybiphenyl + O2
?
9.47% compared to the activity with catechol
-
-
?
2,4-dichlorophenol + O2
?
-
-
-
-
?
2,4-dichlorophenol + O2
?
-
-
-
-
?
2,4-dichlorophenol + O2
?
-
-
-
-
?
2,4-dichlorophenol + O2
?
-
-
-
-
?
2,4-dichlorophenol + O2
?
-
-
-
-
?
2-chlorophenol + O2
?
-
-
-
-
?
2-chlorophenol + O2
?
-
-
-
-
?
2-methylphenol + O2
?
-
-
-
-
?
2-methylphenol + O2
?
-
-
-
?
2-methylphenol + O2
?
-
-
-
?
3,4-dihydroxybenzoate + O2
?
-
-
-
-
?
3,4-dihydroxybenzoate + O2
?
-
-
-
-
?
3,4-dihydroxybenzoate + O2
?
-
weak
-
-
?
3,4-dimethylcatechol + O2
2-hydroxy-5-methyl-6-oxo-hepta-2,4-dienoate
-
-
-
-
?
3,4-dimethylcatechol + O2
2-hydroxy-5-methyl-6-oxo-hepta-2,4-dienoate
-
-
-
-
?
3,5-dichlorocatechol + O2
?
-
-
-
-
?
3,5-dichlorocatechol + O2
?
-
immobilized enzyme, no activity with the free enzyme
-
-
?
3,5-dichlorocatechol + O2
?
-
immobilized enzyme, no activity with the free enzyme
-
-
?
3,5-dimethylcatechol + O2
2-hydroxy-3,5-dimethyl-6-oxohexa-2,4-dienoic acid
-
-
-
-
?
3,5-dimethylcatechol + O2
2-hydroxy-3,5-dimethyl-6-oxohexa-2,4-dienoic acid
-
-
-
-
?
3-chlorocatechol + O2
2-chloro-2-hydroxy-6-oxohexa-2,4-dienoate
-
weak
-
-
?
3-chlorocatechol + O2
2-chloro-2-hydroxy-6-oxohexa-2,4-dienoate
-
weak
-
-
?
3-chlorocatechol + O2
2-chloro-2-hydroxy-6-oxohexa-2,4-dienoate
-
weak
-
-
?
3-chlorocatechol + O2
2-chloro-2-hydroxy-6-oxohexa-2,4-dienoate
-
-
-
-
?
3-chlorocatechol + O2
2-chloro-2-hydroxy-6-oxohexa-2,4-dienoate
-
weak
-
-
?
3-chlorocatechol + O2
2-chloro-2-hydroxy-6-oxohexa-2,4-dienoate
-
weak
-
-
?
3-chlorocatechol + O2
2-hydroxy-6-oxohepta-2,4-dienoate
-
-
-
-
?
3-chlorocatechol + O2
2-hydroxy-6-oxohepta-2,4-dienoate
-
-
-
-
?
3-chlorocatechol + O2
2-hydroxy-6-oxohepta-2,4-dienoate
82.3% of the activity as compared to catechol
-
-
?
3-chlorocatechol + O2
3-chloro-2-hydroxymuconate semialdehyde
rapid inactivation of enzyme during turnover
-
-
?
3-chlorocatechol + O2
3-chloro-2-hydroxymuconate semialdehyde
about 9% of the rate with catechol
-
-
?
3-chlorocatechol + O2
3-chloro-2-hydroxymuconate semialdehyde
about 95% of the rate with catechol
-
-
?
3-chlorocatechol + O2
3-chloro-2-hydroxymuconate semialdehyde
rapid inactivation of enzyme during turnover
-
-
?
3-chlorocatechol + O2
3-chloro-2-hydroxymuconate semialdehyde
about 9% of the rate with catechol
-
-
?
3-formylcatechol + O2
3-formyl-2-hydroxymuconate semialdehyde
-
-
-
?
3-formylcatechol + O2
3-formyl-2-hydroxymuconate semialdehyde
-
-
-
?
3-hydroxycatechol + O2
3-hydroxymuconic acid
-
-
-
?
3-hydroxycatechol + O2
3-hydroxymuconic acid
-
-
-
?
3-hydroxycatechol + O2
3-hydroxymuconic acid
-
-
-
-
?
3-isopropylcatechol + O2
?
Halalkalibacterium ligniniphilum
WP_017726464.1
50% of the activity as compared to 3-ethylcatechol
-
-
?
3-isopropylcatechol + O2
?
Halalkalibacterium ligniniphilum L1
WP_017726464.1
50% of the activity as compared to 3-ethylcatechol
-
-
?
3-methoxycatechol + O2
2-hydroxy-3-methoxymuconate semialdehyde
rapid inactivation of enzyme during turnover
-
-
?
3-methoxycatechol + O2
2-hydroxy-3-methoxymuconate semialdehyde
rapid inactivation of enzyme during turnover
-
-
?
3-methylcatechol + O2
2-hydroxy-3-methylmuconate semialdehyde
-
19% of the activity with catechol
-
-
?
3-methylcatechol + O2
2-hydroxy-3-methylmuconate semialdehyde
-
19% of the activity with catechol
-
-
?
3-methylcatechol + O2
2-hydroxy-3-methylmuconate semialdehyde
-
-
-
?
3-methylcatechol + O2
2-hydroxy-3-methylmuconate semialdehyde
poor substrate
-
-
?
3-methylcatechol + O2
2-hydroxy-3-methylmuconate semialdehyde
-
most effective substrate
-
-
?
3-methylcatechol + O2
2-hydroxy-3-methylmuconate semialdehyde
-
most effective substrate
-
-
?
3-methylcatechol + O2
2-hydroxy-3-methylmuconate semialdehyde
about 30% of activity with catechol
-
-
?
3-methylcatechol + O2
2-hydroxy-6-oxohepta-2,4-dienoate
-
-
-
-
?
3-methylcatechol + O2
2-hydroxy-6-oxohepta-2,4-dienoate
-
-
-
-
?
3-methylcatechol + O2
2-hydroxy-6-oxohepta-2,4-dienoate
-
-
-
-
?
3-methylcatechol + O2
2-hydroxy-6-oxohepta-2,4-dienoate
-
-
-
-
?
3-methylcatechol + O2
2-hydroxy-6-oxohepta-2,4-dienoate
-
-
-
-
?
3-methylcatechol + O2
2-hydroxy-6-oxohepta-2,4-dienoate
-
-
-
-
?
3-methylcatechol + O2
2-hydroxy-6-oxohepta-2,4-dienoate
-
-
-
-
?
3-methylcatechol + O2
2-hydroxy-6-oxohepta-2,4-dienoate
-
-
-
-
?
3-methylcatechol + O2
2-hydroxy-6-oxohepta-2,4-dienoate
-
weak
-
-
?
3-methylcatechol + O2
2-hydroxy-6-oxohepta-2,4-dienoate
-
weak
-
-
?
3-methylcatechol + O2
2-hydroxy-6-oxohepta-2,4-dienoate
Halalkalibacterium ligniniphilum
WP_017726464.1
62.5% of the activity as compared to 3-ethylcatechol
-
-
?
3-methylcatechol + O2
2-hydroxy-6-oxohepta-2,4-dienoate
Halalkalibacterium ligniniphilum L1
WP_017726464.1
62.5% of the activity as compared to 3-ethylcatechol
-
-
?
3-methylcatechol + O2
2-hydroxy-6-oxohepta-2,4-dienoate
-
-
-
-
?
3-methylcatechol + O2
2-hydroxy-6-oxohepta-2,4-dienoate
-
-
-
-
?
3-methylcatechol + O2
2-hydroxy-6-oxohepta-2,4-dienoate
-
-
-
?
3-methylcatechol + O2
2-hydroxy-6-oxohepta-2,4-dienoate
6.12% activity compared to catechol
-
-
?
3-methylcatechol + O2
2-hydroxy-6-oxohepta-2,4-dienoate
-
weak
-
-
?
3-methylcatechol + O2
2-hydroxy-6-oxohepta-2,4-dienoate
-
-
-
-
?
3-methylcatechol + O2
2-hydroxy-6-oxohepta-2,4-dienoate
-
-
-
-
?
3-methylcatechol + O2
2-hydroxy-6-oxohepta-2,4-dienoate
-
-
-
-
?
3-methylcatechol + O2
2-hydroxy-6-oxohepta-2,4-dienoate
-
-
-
?
3-methylcatechol + O2
2-hydroxy-6-oxohepta-2,4-dienoate
-
-
-
-
?
3-methylcatechol + O2
2-hydroxy-6-oxohepta-2,4-dienoate
about 105% of the rate with catechol
-
-
?
3-methylcatechol + O2
2-hydroxy-6-oxohepta-2,4-dienoate
about 43% of the rate with catechol
-
-
?
3-methylcatechol + O2
2-hydroxy-6-oxohepta-2,4-dienoate
-
-
-
-
?
3-methylcatechol + O2
2-hydroxy-6-oxohepta-2,4-dienoate
-
-
-
-
?
3-methylcatechol + O2
2-hydroxy-6-oxohepta-2,4-dienoate
about 105% of the rate with catechol
-
-
?
3-methylcatechol + O2
2-hydroxy-6-oxohepta-2,4-dienoate
-
-
-
-
?
3-methylcatechol + O2
2-hydroxy-6-oxohepta-2,4-dienoate
-
-
-
?
3-methylcatechol + O2
2-hydroxy-6-oxohepta-2,4-dienoate
-
-
-
-
?
3-methylcatechol + O2
2-hydroxy-6-oxohepta-2,4-dienoate
-
-
-
-
?
3-methylcatechol + O2
2-hydroxy-6-oxohepta-2,4-dienoate
-
-
-
-
?
3-methylcatechol + O2
2-hydroxy-6-oxohepta-2,4-dienoate
-
-
-
-
?
3-methylcatechol + O2
2-hydroxy-6-oxohepta-2,4-dienoate
wild-type enzyme shows 6.1% of the activity as compared to catechol. The activities of the mutant enzyme T254A increases 3.7fold as compared to catechol
-
-
?
3-methylcatechol + O2
2-hydroxy-6-oxohepta-2,4-dienoate
about 30% of the rate with catechol
-
-
?
3-methylcatechol + O2
2-hydroxy-6-oxohepta-2,4-dienoate
about 30% of the rate with catechol
-
-
?
3-methylcatechol + O2
2-hydroxy-6-oxohepta-2,4-dienoate
90.8% of the activity as compared to catechol
-
-
?
3-methylcatechol + O2
2-hydroxy-6-oxohepta-2,4-dienoate
-
isoform C23O1 shows 49.5% activity compared to catechol, isoform C23O2 shows 239.2% activity compared to catechol
-
-
?
3-methylcatechol + O2
2-hydroxy-6-oxohepta-2,4-dienoic acid
-
-
-
-
?
3-methylcatechol + O2
2-hydroxy-6-oxohepta-2,4-dienoic acid
-
-
-
-
?
3-methylcatechol + O2
?
-
-
-
?
3-methylcatechol + O2
?
-
-
-
?
3-methylcatechol + O2
?
33% of the activity with 4-chlorocatechol
-
-
?
3-methylcatechol + O2
?
33% of the activity with 4-chlorocatechol
-
-
?
3-methylcatechol + O2
?
-
-
-
?
3-methylcatechol + O2
?
-
-
-
?
3-methylcatechol + O2
?
-
-
-
-
?
3-methylcatechol + O2
?
-
-
-
-
?
3-methylcatechol + O2
cis,cis-2-hydroxy-6-oxohepta-2,4-dienoate
-
-
-
-
?
3-methylcatechol + O2
cis,cis-2-hydroxy-6-oxohepta-2,4-dienoate
-
-
-
-
?
3-methylphenol + O2
?
-
-
-
-
?
3-methylphenol + O2
?
-
-
-
?
3-methylphenol + O2
?
-
-
-
?
4,5-dichlorocatechol + O2
?
4.6% compared to the activity with catechol
-
-
?
4,5-dichlorocatechol + O2
?
4.6% compared to the activity with catechol
-
-
?
4,5-dichlorocatechol + O2
?
-
-
-
-
?
4,5-dichlorocatechol + O2
?
23.4% of the activity as compared to catechol
-
-
?
4-alkylcatechol + O2
?
initial step of long-chain alkylphenol cleavage pathway
-
-
?
4-alkylcatechol + O2
?
alkyl chain length C1-C5 is accepted as substrate
-
-
?
4-alkylcatechol + O2
?
initial step of long-chain alkylphenol cleavage pathway
-
-
?
4-alkylcatechol + O2
?
alkyl chain length C1-C5 is accepted as substrate
-
-
?
4-chlorocatechol + O2
4-chloro-2-hydroxymuconate semialdehyde
-
-
-
?
4-chlorocatechol + O2
4-chloro-2-hydroxymuconate semialdehyde
44.88% activity compared to catechol
-
-
?
4-chlorocatechol + O2
4-chloro-2-hydroxymuconate semialdehyde
-
-
-
?
4-chlorocatechol + O2
4-chloro-2-hydroxymuconate semialdehyde
about 16% of the rate with catechol
-
-
?
4-chlorocatechol + O2
4-chloro-2-hydroxymuconate semialdehyde
about 75% of the rate with catechol
-
-
?
4-chlorocatechol + O2
4-chloro-2-hydroxymuconate semialdehyde
about 16% of the rate with catechol
-
-
?
4-chlorocatechol + O2
4-chloro-2-hydroxymuconate semialdehyde
-
-
-
?
4-chlorocatechol + O2
4-chloro-2-hydroxymuconate semialdehyde
at the same rate as catechol
-
-
?
4-chlorocatechol + O2
4-chloro-2-hydroxymuconate semialdehyde
17.4% compared to the activity with catechol
-
-
?
4-chlorocatechol + O2
4-chloro-2-hydroxymuconate semialdehyde
17.4% compared to the activity with catechol
-
-
?
4-chlorocatechol + O2
4-chloro-2-hydroxymuconate semialdehyde
-
isoform C23O1 shows 50.8% activity compared to catechol, isoform C23O2 shows 226.4% activity compared to catechol
-
-
?
4-chlorocatechol + O2
5-chloro-2-hydroxy-6-oxohexa-2,4-dienoate
-
-
-
-
?
4-chlorocatechol + O2
5-chloro-2-hydroxy-6-oxohexa-2,4-dienoate
19.2% of the activity as compared to catechol
-
-
?
4-chlorocatechol + O2
5-chloro-2-hydroxy-6-oxohexa-2,4-dienoate
71.1% of the activity as compared to catechol
-
-
?
4-chlorocatechol + O2
5-chloro-2-hydroxymuconic semialdehyde
-
-
-
-
?
4-chlorocatechol + O2
5-chloro-2-hydroxymuconic semialdehyde
-
-
-
-
?
4-chlorocatechol + O2
5-chloro-2-hydroxymuconic semialdehyde
-
-
-
?
4-chlorocatechol + O2
5-chloro-2-hydroxymuconic semialdehyde
-
-
-
?
4-chlorocatechol + O2
5-chloro-2-hydroxymuconic semialdehyde
-
weak
-
-
?
4-chlorocatechol + O2
5-chloro-2-hydroxymuconic semialdehyde
-
-
-
?
4-chlorocatechol + O2
?
-
46% of the activity with catechol
-
-
?
4-chlorocatechol + O2
?
-
46% of the activity with catechol
-
-
?
4-chlorocatechol + O2
?
-
-
-
?
4-chlorocatechol + O2
?
-
-
-
?
4-chlorocatechol + O2
?
39% of the activity with 4-chlorocatechol
-
-
?
4-chlorocatechol + O2
?
39% of the activity with 4-chlorocatechol
-
-
?
4-chlorocatechol + O2
?
-
-
-
?
4-chlorocatechol + O2
?
the enzyme shows the highest activity against catechol and 4-chlorocatechol
-
-
?
4-chlorocatechol + O2
?
the enzyme shows the highest activity against catechol and 4-chlorocatechol
-
-
?
4-chlorocatechol + O2
?
-
-
-
?
4-ethylcatechol + O2
4-ethyl-2-hydroxymuconate semialdehyde
effective substrate
-
-
?
4-ethylcatechol + O2
4-ethyl-2-hydroxymuconate semialdehyde
rapid inactivation of enzyme during turnover
-
-
?
4-ethylcatechol + O2
4-ethyl-2-hydroxymuconate semialdehyde
rapid inactivation of enzyme during turnover
-
-
?
4-formylcatechol + O2
4-formyl-2-hydroxymuconate semialdehyde
-
-
-
?
4-formylcatechol + O2
4-formyl-2-hydroxymuconate semialdehyde
rapid inactivation of enzyme during turnover
-
-
?
4-formylcatechol + O2
4-formyl-2-hydroxymuconate semialdehyde
rapid inactivation of enzyme during turnover
-
-
?
4-methylcatechol + O2
2-hydroxy-3-methyl-6-oxohexa-2,4-dienoate
-
hypoxic strains with significantly higher affinities
-
-
?
4-methylcatechol + O2
2-hydroxy-3-methyl-6-oxohexa-2,4-dienoate
-
hypoxic strains with significantly higher affinities
-
-
?
4-methylcatechol + O2
2-hydroxy-3-methyl-6-oxohexa-2,4-dienoate
-
-
-
-
?
4-methylcatechol + O2
2-hydroxy-3-methyl-6-oxohexa-2,4-dienoate
-
-
-
-
?
4-methylcatechol + O2
2-hydroxy-3-methyl-6-oxohexa-2,4-dienoate
-
-
-
-
?
4-methylcatechol + O2
2-hydroxy-3-methyl-6-oxohexa-2,4-dienoate
-
-
-
-
?
4-methylcatechol + O2
2-hydroxy-3-methyl-6-oxohexa-2,4-dienoate
-
weak
-
-
?
4-methylcatechol + O2
2-hydroxy-3-methyl-6-oxohexa-2,4-dienoate
-
weak
-
-
?
4-methylcatechol + O2
2-hydroxy-3-methyl-6-oxohexa-2,4-dienoate
-
-
-
?
4-methylcatechol + O2
2-hydroxy-3-methyl-6-oxohexa-2,4-dienoate
101.91% activity compared to catechol
-
-
?
4-methylcatechol + O2
2-hydroxy-3-methyl-6-oxohexa-2,4-dienoate
-
-
-
-
?
4-methylcatechol + O2
2-hydroxy-3-methyl-6-oxohexa-2,4-dienoate
-
hypoxic strains with significantly higher affinities
-
-
?
4-methylcatechol + O2
2-hydroxy-3-methyl-6-oxohexa-2,4-dienoate
-
hypoxic strains with significantly higher affinities
-
-
?
4-methylcatechol + O2
2-hydroxy-3-methyl-6-oxohexa-2,4-dienoate
-
-
-
-
?
4-methylcatechol + O2
2-hydroxy-3-methyl-6-oxohexa-2,4-dienoate
-
highly specific for
-
-
?
4-methylcatechol + O2
2-hydroxy-3-methyl-6-oxohexa-2,4-dienoate
-
hypoxic strains with significantly higher affinities
-
-
?
4-methylcatechol + O2
2-hydroxy-3-methyl-6-oxohexa-2,4-dienoate
-
-
-
-
?
4-methylcatechol + O2
2-hydroxy-3-methyl-6-oxohexa-2,4-dienoate
-
-
-
-
?
4-methylcatechol + O2
2-hydroxy-3-methyl-6-oxohexa-2,4-dienoate
-
-
-
-
?
4-methylcatechol + O2
2-hydroxy-3-methyl-6-oxohexa-2,4-dienoate
-
hypoxic strains with significantly higher affinities
-
-
?
4-methylcatechol + O2
2-hydroxy-3-methyl-6-oxohexa-2,4-dienoate
-
-
-
-
?
4-methylcatechol + O2
2-hydroxy-3-methyl-6-oxohexa-2,4-dienoate
-
hypoxic strains with significantly higher affinities
-
-
?
4-methylcatechol + O2
2-hydroxy-3-methyl-6-oxohexa-2,4-dienoate
-
hypoxic strains with significantly higher affinities
-
-
?
4-methylcatechol + O2
2-hydroxy-3-methyl-6-oxohexa-2,4-dienoate
-
hypoxic strains with significantly higher affinities
-
-
?
4-methylcatechol + O2
2-hydroxy-3-methyl-6-oxohexa-2,4-dienoate
-
best substrate for isoform C23O2 (280.7% activity compared to catechol), while isoform C23O1 shows 87.4% activity compared to catechol
-
-
?
4-methylcatechol + O2
2-hydroxy-4-methyl-6-oxohexa-2,4-dienoate
about 47% of the rate with catechol
-
-
?
4-methylcatechol + O2
2-hydroxy-4-methyl-6-oxohexa-2,4-dienoate
about 89% of the rate with catechol
-
-
?
4-methylcatechol + O2
2-hydroxy-4-methyl-6-oxohexa-2,4-dienoate
about 47% of the rate with catechol
-
-
?
4-methylcatechol + O2
2-hydroxy-4-methyl-6-oxohexa-2,4-dienoate
about 65% of the rate with catechol
-
-
?
4-methylcatechol + O2
2-hydroxy-4-methyl-6-oxohexa-2,4-dienoate
about 65% of the rate with catechol
-
-
?
4-methylcatechol + O2
2-hydroxy-4-methylmuconate semialdehyde
-
-
-
?
4-methylcatechol + O2
2-hydroxy-4-methylmuconate semialdehyde
very effective substrate
-
-
?
4-methylcatechol + O2
2-hydroxy-4-methylmuconate semialdehyde
rapid inactivation of enzyme during turnover
-
-
?
4-methylcatechol + O2
2-hydroxy-4-methylmuconate semialdehyde
-
-
-
-
?
4-methylcatechol + O2
2-hydroxy-4-methylmuconate semialdehyde
111.4% compared to the activity with catechol
-
-
?
4-methylcatechol + O2
2-hydroxy-4-methylmuconate semialdehyde
111.4% compared to the activity with catechol
-
-
?
4-methylcatechol + O2
2-hydroxy-5-methyl-6-oxohexa-2,4-dienoate
Halalkalibacterium ligniniphilum
WP_017726464.1
2.7% of the activity as compared to 3-ethylcatechol
-
-
?
4-methylcatechol + O2
2-hydroxy-5-methyl-6-oxohexa-2,4-dienoate
Halalkalibacterium ligniniphilum L1
WP_017726464.1
2.7% of the activity as compared to 3-ethylcatechol
-
-
?
4-methylcatechol + O2
2-hydroxy-5-methyl-6-oxohexa-2,4-dienoate
-
-
-
-
?
4-methylcatechol + O2
2-hydroxy-5-methyl-6-oxohexa-2,4-dienoate
-
-
-
-
?
4-methylcatechol + O2
2-hydroxy-5-methyl-6-oxohexa-2,4-dienoate
-
-
-
-
?
4-methylcatechol + O2
2-hydroxy-5-methyl-6-oxohexa-2,4-dienoate
wild-type enzyme shows 92.1% of the activity as compared to catechol. The activities of the mutant enzyme T254A increases 2.5fold as compared to catechol
-
-
?
4-methylcatechol + O2
2-hydroxy-5-methyl-6-oxohexa-2,4-dienoate
67.7% of the activity as compared to catechol
-
-
?
4-methylcatechol + O2
?
-
57% of the activity with catechol
-
-
?
4-methylcatechol + O2
?
-
57% of the activity with catechol
-
-
?
4-methylcatechol + O2
?
-
-
-
?
4-methylcatechol + O2
?
-
-
-
?
4-methylcatechol + O2
?
activity is 5.72fold higher than with catechol
-
-
?
4-methylcatechol + O2
?
-
-
-
?
4-methylcatechol + O2
?
about 65% of activity with catechol
-
-
?
4-methylcatechol + O2
?
-
-
-
?
4-methylcatechol + O2
?
-
-
-
-
?
4-Methylphenol + O2
?
-
-
-
-
?
4-Methylphenol + O2
?
-
-
-
?
4-Methylphenol + O2
?
-
-
-
?
4-nitrocatechol + O2
2-hydroxy-4-nitromuconate semialdehyde
-
-
-
?
4-nitrocatechol + O2
2-hydroxy-4-nitromuconate semialdehyde
rapid inactivation of enzyme during turnover
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
-
-
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
-
-
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
-
-
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
-
-
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
-
-
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
-
-
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
-
-
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
-
hypoxic strains have enzymes with significantly higher affinities for catechol than for nonhypoxic strains
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
-
-
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
-
hypoxic strains have enzymes with significantly higher affinities for catechol than for nonhypoxic strains
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
-
highly specific for
-
?
catechol + O2
2-hydroxymuconate semialdehyde
-
highly specific for
-
?
catechol + O2
2-hydroxymuconate semialdehyde
-
-
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
-
extradiol dioxygenase reaction
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
-
-
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
-
-
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
-
highly specific for
-
?
catechol + O2
2-hydroxymuconate semialdehyde
-
-
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
-
-
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
-
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
-
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
-
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
-
-
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
-
metacleavage enzyme of catechol metabolism
-
?
catechol + O2
2-hydroxymuconate semialdehyde
-
enzyme is a important component in the degradation pathways of toluene and xylene and catalyses the dioxygenolytic cleavage of the aromatic ring
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
-
metapyrocatechase 1 takes part in oxidation of aromatic compounds, producing catechol as an intermediate, metapyrocatechase 2 is involved in oxidation of methyl-substituted aromatic substrates
-
?
catechol + O2
2-hydroxymuconate semialdehyde
-
enzyme is induced by benzenesulfonate, catechol or toluene p-sulfonate
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
-
hypoxic strains have enzymes with significantly higher affinities for catechol than for nonhypoxic strains
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
-
enzyme is a important component in the degradation pathways of toluene and xylene and catalyses the dioxygenolytic cleavage of the aromatic ring
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
-
hypoxic strains have enzymes with significantly higher affinities for catechol than for nonhypoxic strains
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
-
enzyme is a important component in the degradation pathways of toluene and xylene and catalyses the dioxygenolytic cleavage of the aromatic ring
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
-
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
-
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
-
-
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
-
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
-
-
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
-
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
-
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
-
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
-
-
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
-
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
-
-
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
-
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
-
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
-
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
-
highly specific for
-
?
catechol + O2
2-hydroxymuconate semialdehyde
-
hypoxic strains have enzymes with significantly higher affinities for catechol than for nonhypoxic strains
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
best substrates
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
-
enzyme is a important component in the degradation pathways of toluene and xylene and catalyses the dioxygenolytic cleavage of the aromatic ring
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
degradation of aromatic compounds
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
-
benzoate degadation pathway
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
-
-
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
-
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
-
-
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
key role in the degradation of aromatic molecules
-
?
catechol + O2
2-hydroxymuconate semialdehyde
-
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
degradation of aromatic compounds
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
-
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
-
-
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
-
-
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
-
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
-
-
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
-
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
-
highly specific for
-
?
catechol + O2
2-hydroxymuconate semialdehyde
-
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
-
-
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
-
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
-
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
poor substrate
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
-
highly specific for
-
?
catechol + O2
2-hydroxymuconate semialdehyde
-
highly specific for
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
-
hypoxic strains have enzymes with significantly higher affinities for catechol than for nonhypoxic strains
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
-
enzyme is a important component in the degradation pathways of toluene and xylene and catalyses the dioxygenolytic cleavage of the aromatic ring
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
-
catechol 2,3-dioxygenase is a key enzyme in the catabolism of monocyclic aromatic compounds including aniline and catalyzes the extradiol cleavage of catechol
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
-
cleavage of aromatic compounds, involved in alpha-ketoadiapate pathway
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
degradation of aromatic compounds
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
involved in metabolism of aromatic compounds
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
-
key enzyme for the degradation of aromatic compounds
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
-
catechol 2,3-dioxygenase is involved in the meta phenol degradation pathway
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
-
catechol 2,3-dioxygenase is a critical enzyme in the multistep biodegradation of 3,4-dichloroaniline by Pseudomonas sp. KB35B
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
-
catechol 2,3-dioxygenase is a critical enzyme in the multistep biodegradation of 3,4-dichloroaniline by Pseudomonas sp. KB35B
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
poor substrate
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
involved in metabolism of aromatic compounds
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
-
-
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
-
cleavage of aromatic compounds, involved in alpha-ketoadiapate pathway
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
-
highly specific for
-
?
catechol + O2
2-hydroxymuconate semialdehyde
-
catechol 2,3-dioxygenase is involved in the meta phenol degradation pathway
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
-
highly specific for
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
-
hypoxic strains have enzymes with significantly higher affinities for catechol than for nonhypoxic strains
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
-
enzyme is a important component in the degradation pathways of toluene and xylene and catalyses the dioxygenolytic cleavage of the aromatic ring
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
-
-
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
-
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
most effective substrate
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
-
-
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
-
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
most effective substrate
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
-
hypoxic strains have enzymes with significantly higher affinities for catechol than for nonhypoxic strains
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
-
enzyme is a important component in the degradation pathways of toluene and xylene and catalyses the dioxygenolytic cleavage of the aromatic ring
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
-
hypoxic strains have enzymes with significantly higher affinities for catechol than for nonhypoxic strains
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
-
enzyme is a important component in the degradation pathways of toluene and xylene and catalyses the dioxygenolytic cleavage of the aromatic ring
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
-
involved in biodegradation of benzothiazoles
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
-
involved in biodegradation of benzothiazoles
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
-
-
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
-
-
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
-
poor substrate
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
-
degradation of aromatic compounds, involved in toluene and ortho-xylene metabolism
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
-
poor substrate
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
-
degradation of aromatic compounds, involved in toluene and ortho-xylene metabolism
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
-
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
and 4-chlorocatechol, best substrates
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
both the ortho- and the meta-degradation pathways are functional in presence of phenol. However, the activation of the catechol 2,3-dioxygenase, only when phenol is present, and the accumulation of only intermediary compounds related to this pathway lead us to the conclusion that the aromatic ring is preferentially opened through the meta-pathway
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
the enzyme shows the highest activity against catechol and 4-chlorocatechol
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
both the ortho- and the meta-degradation pathways are functional in presence of phenol. However, the activation of the catechol 2,3-dioxygenase, only when phenol is present, and the accumulation of only intermediary compounds related to this pathway lead us to the conclusion that the aromatic ring is preferentially opened through the meta-pathway
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
the enzyme shows the highest activity against catechol and 4-chlorocatechol
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
-
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
and 4-chlorocatechol, best substrates
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
-
-
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
-
key enzyme for the degradation of aromatic compounds
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
-
-
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
-
-
-
?
catechol + O2
2-hydroxymuconate-6-semialdehyde
-
-
-
-
?
catechol + O2
2-hydroxymuconate-6-semialdehyde
-
-
-
-
?
catechol + O2
2-hydroxymuconate-6-semialdehyde
-
-
-
-
?
catechol + O2
2-hydroxymuconate-6-semialdehyde
-
-
-
?
catechol + O2
2-hydroxymuconate-6-semialdehyde
Halalkalibacterium ligniniphilum
WP_017726464.1
1.5% of the activity as compared to 3-ethylcatechol
-
-
?
catechol + O2
2-hydroxymuconate-6-semialdehyde
Halalkalibacterium ligniniphilum L1
WP_017726464.1
1.5% of the activity as compared to 3-ethylcatechol
-
-
?
catechol + O2
2-hydroxymuconate-6-semialdehyde
-
-
-
-
?
catechol + O2
2-hydroxymuconate-6-semialdehyde
-
-
-
-
?
catechol + O2
2-hydroxymuconate-6-semialdehyde
-
-
-
-
?
catechol + O2
2-hydroxymuconate-6-semialdehyde
-
-
-
-
?
catechol + O2
2-hydroxymuconate-6-semialdehyde
-
-
-
-
?
catechol + O2
2-hydroxymuconate-6-semialdehyde
-
-
-
-
?
catechol + O2
2-hydroxymuconate-6-semialdehyde
-
-
-
?
catechol + O2
2-hydroxymuconate-6-semialdehyde
-
-
-
-
?
catechol + O2
2-hydroxymuconate-6-semialdehyde
-
-
-
?
catechol + O2
2-hydroxymuconate-6-semialdehyde
-
-
-
?
catechol + O2
2-hydroxymuconate-6-semialdehyde
100% activity
-
-
?
catechol + O2
2-hydroxymuconate-6-semialdehyde
-
-
-
-
?
catechol + O2
2-hydroxymuconate-6-semialdehyde
-
-
-
-
?
catechol + O2
2-hydroxymuconate-6-semialdehyde
-
-
-
-
?
catechol + O2
2-hydroxymuconate-6-semialdehyde
-
-
-
?
catechol + O2
2-hydroxymuconate-6-semialdehyde
-
-
-
?
catechol + O2
2-hydroxymuconate-6-semialdehyde
-
-
-
?
catechol + O2
2-hydroxymuconate-6-semialdehyde
-
-
-
?
catechol + O2
2-hydroxymuconate-6-semialdehyde
-
-
-
-
?
catechol + O2
2-hydroxymuconate-6-semialdehyde
-
-
-
?
catechol + O2
2-hydroxymuconate-6-semialdehyde
-
-
-
?
catechol + O2
2-hydroxymuconate-6-semialdehyde
-
-
-
?
catechol + O2
2-hydroxymuconate-6-semialdehyde
-
-
-
?
catechol + O2
2-hydroxymuconate-6-semialdehyde
-
-
-
?
catechol + O2
2-hydroxymuconate-6-semialdehyde
the enzyme is constitutively transcribed
-
-
?
catechol + O2
2-hydroxymuconate-6-semialdehyde
-
-
-
?
catechol + O2
2-hydroxymuconate-6-semialdehyde
the enzyme is constitutively transcribed
-
-
?
catechol + O2
2-hydroxymuconate-6-semialdehyde
-
-
-
?
catechol + O2
2-hydroxymuconate-6-semialdehyde
-
-
-
?
catechol + O2
2-hydroxymuconate-6-semialdehyde
-
-
-
-
?
catechol + O2
2-hydroxymuconate-6-semialdehyde
-
compared to the enzyme from Sphingobium yanoikuyae XLDN2-5, the recombinant Escherichia coli BL21 overexpressed C23O exhibits higher catalytic activity towards catechol. The whole cells provided a better environment for C23O to maintain its catalytic activity and stability compared with crude enzyme
-
-
?
catechol + O2
2-hydroxymuconate-6-semialdehyde
-
-
-
-
?
catechol + O2
2-hydroxymuconate-6-semialdehyde
-
compared to the enzyme from Sphingobium yanoikuyae XLDN2-5, the recombinant Escherichia coli BL21 overexpressed C23O exhibits higher catalytic activity towards catechol. The whole cells provided a better environment for C23O to maintain its catalytic activity and stability compared with crude enzyme
-
-
?
catechol + O2
2-hydroxymuconate-6-semialdehyde
-
-
-
-
?
catechol + O2
2-hydroxymuconate-6-semialdehyde
-
-
-
-
?
catechol + O2
2-hydroxymuconate-6-semialdehyde
-
-
-
-
?
catechol + O2
2-hydroxymuconate-6-semialdehyde
-
-
-
-
?
catechol + O2
2-hydroxymuconate-6-semialdehyde
-
-
-
?
catechol + O2
2-hydroxymuconate-6-semialdehyde
-
-
-
?
catechol + O2
2-hydroxymuconate-6-semialdehyde
-
-
-
?
catechol + O2
2-hydroxymuconate-6-semialdehyde
-
-
-
-
?
catechol + O2
2-hydroxymuconate-6-semialdehyde
-
-
-
-
?
catechol + O2
2-hydroxymuconate-6-semialdehyde
-
-
-
-
?
catechol + O2
2-hydroxymuconate-6-semialdehyde
-
best substrate for isoform C23O1 (100% activity)
-
-
?
catechol + O2
2-hydroxymuconate-6-semialdehyde
-
-
-
-
?
catechol + O2
2-hydroxymuconate-6-semialdehyde
-
-
-
-
?
catechol + O2
?
-
assay at pH 7.5, 30°C
-
-
?
catechol + O2
?
-
assay at pH 7.5, 30°C
-
-
?
catechol + O2
cis,cis-muconate
-
-
-
?
catechol + O2
cis,cis-muconate
-
-
-
-
?
catechol + O2
cis,cis-muconate
-
-
-
-
?
hydroquinone + O2
?
-
immobilized enzyme, no activity with the free enzyme
-
-
?
hydroquinone + O2
?
-
immobilized enzyme, no activity with the free enzyme
-
-
?
naphthalene + O2
?
-
-
-
-
?
naphthalene + O2
?
-
-
-
-
?
pentachlorophenol + O2
?
-
-
-
-
?
pentachlorophenol + O2
?
-
-
-
-
?
phenanthrene + O2
?
-
-
-
-
?
phenanthrene + O2
?
-
-
-
-
?
phenol + O2
2-hydroxymuconic semialdehyde
utilize phenol as sole carbon and energy source, concentration of phenol diversify from 25 mg/l to 1000 mg/l, assay at 28°C, pH 6.8-7.0
-
-
?
phenol + O2
2-hydroxymuconic semialdehyde
utilize phenol as sole carbon and energy source, concentration of phenol diversify from 25 mg/l to 1000 mg/l, assay at 28°C, pH 6.8-7.0
-
-
?
phenol + O2
?
-
-
-
?
phenol + O2
?
-
activity in cadmium-induced cells
-
-
?
phenol + O2
?
-
activity in cadmium-induced cells
-
-
?
protocatechualdehyde + O2
?
-
-
-
-
?
protocatechualdehyde + O2
?
-
weak
-
-
?
pyrogallol + O2
?
-
-
-
-
?
pyrogallol + O2
?
-
-
-
-
?
additional information
?
-
Halalkalibacterium ligniniphilum
WP_017726464.1
no activities observed for pyrogallol and 3-fluorocatechol
-
-
-
additional information
?
-
Halalkalibacterium ligniniphilum L1
WP_017726464.1
no activities observed for pyrogallol and 3-fluorocatechol
-
-
-
additional information
?
-
no cleavage of 4-carboxycatechol, 4-carboxymethylcatechol and 4-tert-butylcatechol
-
-
?
additional information
?
-
no activity with 4-tert-butylcatechol
-
-
?
additional information
?
-
no cleavage of 4-carboxycatechol, 4-carboxymethylcatechol and 4-tert-butylcatechol
-
-
?
additional information
?
-
no activity with 4-tert-butylcatechol
-
-
?
additional information
?
-
-
preferred substrates are catechol and 2,3-dihydroxybiphenyl, reaction of EC 1.13.11.39
-
-
-
additional information
?
-
no activity with 2,3-dihydroxybiphenyl and 3,4-dihydrophenylacetate
-
-
-
additional information
?
-
-
the two isoforms cannot oxidize 1, 2-dihydroxynaphthalene
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
2,4-dichlorophenol + O2
?
alkylcatechol + O2
?
degradation of aromatic compounds
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
catechol + O2
2-hydroxymuconate-6-semialdehyde
catechol + O2
cis,cis-muconate
-
-
-
?
2,4-dichlorophenol + O2
?
-
-
-
-
?
2,4-dichlorophenol + O2
?
-
-
-
-
?
2-chlorophenol + O2
?
-
-
-
-
?
2-chlorophenol + O2
?
-
-
-
-
?
2-methylphenol + O2
?
-
-
-
?
2-methylphenol + O2
?
-
-
-
?
3-methylphenol + O2
?
-
-
-
?
3-methylphenol + O2
?
-
-
-
?
4-alkylcatechol + O2
?
initial step of long-chain alkylphenol cleavage pathway
-
-
?
4-alkylcatechol + O2
?
initial step of long-chain alkylphenol cleavage pathway
-
-
?
4-Methylphenol + O2
?
-
-
-
?
4-Methylphenol + O2
?
-
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
-
-
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
-
-
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
-
-
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
-
metacleavage enzyme of catechol metabolism
-
?
catechol + O2
2-hydroxymuconate semialdehyde
-
enzyme is a important component in the degradation pathways of toluene and xylene and catalyses the dioxygenolytic cleavage of the aromatic ring
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
-
metapyrocatechase 1 takes part in oxidation of aromatic compounds, producing catechol as an intermediate, metapyrocatechase 2 is involved in oxidation of methyl-substituted aromatic substrates
-
?
catechol + O2
2-hydroxymuconate semialdehyde
-
enzyme is induced by benzenesulfonate, catechol or toluene p-sulfonate
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
-
enzyme is a important component in the degradation pathways of toluene and xylene and catalyses the dioxygenolytic cleavage of the aromatic ring
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
-
enzyme is a important component in the degradation pathways of toluene and xylene and catalyses the dioxygenolytic cleavage of the aromatic ring
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
-
enzyme is a important component in the degradation pathways of toluene and xylene and catalyses the dioxygenolytic cleavage of the aromatic ring
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
degradation of aromatic compounds
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
-
benzoate degadation pathway
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
key role in the degradation of aromatic molecules
-
?
catechol + O2
2-hydroxymuconate semialdehyde
degradation of aromatic compounds
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
-
enzyme is a important component in the degradation pathways of toluene and xylene and catalyses the dioxygenolytic cleavage of the aromatic ring
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
-
catechol 2,3-dioxygenase is a key enzyme in the catabolism of monocyclic aromatic compounds including aniline and catalyzes the extradiol cleavage of catechol
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
-
cleavage of aromatic compounds, involved in alpha-ketoadiapate pathway
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
degradation of aromatic compounds
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
involved in metabolism of aromatic compounds
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
-
key enzyme for the degradation of aromatic compounds
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
-
catechol 2,3-dioxygenase is involved in the meta phenol degradation pathway
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
-
catechol 2,3-dioxygenase is a critical enzyme in the multistep biodegradation of 3,4-dichloroaniline by Pseudomonas sp. KB35B
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
-
catechol 2,3-dioxygenase is a critical enzyme in the multistep biodegradation of 3,4-dichloroaniline by Pseudomonas sp. KB35B
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
involved in metabolism of aromatic compounds
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
-
cleavage of aromatic compounds, involved in alpha-ketoadiapate pathway
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
-
catechol 2,3-dioxygenase is involved in the meta phenol degradation pathway
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
-
enzyme is a important component in the degradation pathways of toluene and xylene and catalyses the dioxygenolytic cleavage of the aromatic ring
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
-
-
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
-
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
-
-
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
-
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
-
enzyme is a important component in the degradation pathways of toluene and xylene and catalyses the dioxygenolytic cleavage of the aromatic ring
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
-
enzyme is a important component in the degradation pathways of toluene and xylene and catalyses the dioxygenolytic cleavage of the aromatic ring
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
-
involved in biodegradation of benzothiazoles
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
-
involved in biodegradation of benzothiazoles
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
-
degradation of aromatic compounds, involved in toluene and ortho-xylene metabolism
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
-
degradation of aromatic compounds, involved in toluene and ortho-xylene metabolism
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
both the ortho- and the meta-degradation pathways are functional in presence of phenol. However, the activation of the catechol 2,3-dioxygenase, only when phenol is present, and the accumulation of only intermediary compounds related to this pathway lead us to the conclusion that the aromatic ring is preferentially opened through the meta-pathway
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
both the ortho- and the meta-degradation pathways are functional in presence of phenol. However, the activation of the catechol 2,3-dioxygenase, only when phenol is present, and the accumulation of only intermediary compounds related to this pathway lead us to the conclusion that the aromatic ring is preferentially opened through the meta-pathway
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
-
key enzyme for the degradation of aromatic compounds
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
-
-
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
-
-
-
?
catechol + O2
2-hydroxymuconate-6-semialdehyde
-
-
-
-
?
catechol + O2
2-hydroxymuconate-6-semialdehyde
-
-
-
-
?
catechol + O2
2-hydroxymuconate-6-semialdehyde
-
-
-
-
?
catechol + O2
2-hydroxymuconate-6-semialdehyde
-
-
-
?
catechol + O2
2-hydroxymuconate-6-semialdehyde
-
-
-
-
?
catechol + O2
2-hydroxymuconate-6-semialdehyde
-
-
-
-
?
catechol + O2
2-hydroxymuconate-6-semialdehyde
-
-
-
-
?
catechol + O2
2-hydroxymuconate-6-semialdehyde
-
-
-
?
catechol + O2
2-hydroxymuconate-6-semialdehyde
-
-
-
-
?
catechol + O2
2-hydroxymuconate-6-semialdehyde
-
-
-
?
catechol + O2
2-hydroxymuconate-6-semialdehyde
-
-
-
?
catechol + O2
2-hydroxymuconate-6-semialdehyde
100% activity
-
-
?
catechol + O2
2-hydroxymuconate-6-semialdehyde
-
-
-
-
?
catechol + O2
2-hydroxymuconate-6-semialdehyde
-
-
-
-
?
catechol + O2
2-hydroxymuconate-6-semialdehyde
-
-
-
-
?
catechol + O2
2-hydroxymuconate-6-semialdehyde
-
-
-
?
catechol + O2
2-hydroxymuconate-6-semialdehyde
-
-
-
?
catechol + O2
2-hydroxymuconate-6-semialdehyde
-
-
-
?
catechol + O2
2-hydroxymuconate-6-semialdehyde
-
-
-
?
catechol + O2
2-hydroxymuconate-6-semialdehyde
-
-
-
?
catechol + O2
2-hydroxymuconate-6-semialdehyde
-
-
-
?
catechol + O2
2-hydroxymuconate-6-semialdehyde
-
-
-
?
catechol + O2
2-hydroxymuconate-6-semialdehyde
the enzyme is constitutively transcribed
-
-
?
catechol + O2
2-hydroxymuconate-6-semialdehyde
the enzyme is constitutively transcribed
-
-
?
catechol + O2
2-hydroxymuconate-6-semialdehyde
-
-
-
-
?
catechol + O2
2-hydroxymuconate-6-semialdehyde
-
-
-
-
?
catechol + O2
2-hydroxymuconate-6-semialdehyde
-
-
-
-
?
catechol + O2
2-hydroxymuconate-6-semialdehyde
-
-
-
-
?
catechol + O2
2-hydroxymuconate-6-semialdehyde
-
-
-
-
?
catechol + O2
2-hydroxymuconate-6-semialdehyde
-
-
-
?
catechol + O2
2-hydroxymuconate-6-semialdehyde
-
-
-
?
catechol + O2
2-hydroxymuconate-6-semialdehyde
-
-
-
?
catechol + O2
2-hydroxymuconate-6-semialdehyde
-
-
-
-
?
catechol + O2
2-hydroxymuconate-6-semialdehyde
-
-
-
-
?
catechol + O2
2-hydroxymuconate-6-semialdehyde
-
-
-
-
?
catechol + O2
2-hydroxymuconate-6-semialdehyde
-
-
-
-
?
catechol + O2
2-hydroxymuconate-6-semialdehyde
-
-
-
-
?
phenol + O2
?
-
activity in cadmium-induced cells
-
-
?
phenol + O2
?
-
activity in cadmium-induced cells
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
E286A
-
mutation results in reduction in activity
E286D
-
activity is similar to wild-type enzyme
E286K
-
specific activity is 2.4fold higher than wild-type activity, in contrast with wild-type enzyme mutant enzyme shows no substrate inhibition
E286R
-
activity is similar to wild-type enzyme
E286A
-
mutation results in reduction in activity
-
E286D
-
activity is similar to wild-type enzyme
-
E286K
-
specific activity is 2.4fold higher than wild-type activity, in contrast with wild-type enzyme mutant enzyme shows no substrate inhibition
-
E286R
-
activity is similar to wild-type enzyme
-
H250G
-
reduced twofold relative kcat value for 3-methylcatechol
R215W
-
site-directed mutagenesis
H250G
-
reduced twofold relative kcat value for 3-methylcatechol
-
P229S
-
thermostability decreases compared with that of wild-type enzyme
A23T/F212S
-
random mutagenesis, the mutant shows decreased activity compared to the wild-type enzyme
C103R/K289stop
-
random mutagenesis, the mutant shows decreased activity compared to the wild-type enzyme
F191I/C268R/Y272H/V280A/Y293D /
-
random mutagenesis, the mutant shows decreased activity compared to the wild-type enzyme
G127D/P140T
-
random mutagenesis, the mutant shows decreased activity compared to the wild-type enzyme
H24R/F168S/Q275R
-
random mutagenesis, the mutant shows decreased activity compared to the wild-type enzyme
L13R
-
random mutagenesis, the mutant shows decreased activity compared to the wild-type enzyme
M65T
-
random mutagenesis, the mutant shows decreased activity compared to the wild-type enzyme
G127D/P140T
-
random mutagenesis, the mutant shows decreased activity compared to the wild-type enzyme
-
L13R
-
random mutagenesis, the mutant shows decreased activity compared to the wild-type enzyme
-
M65T
-
random mutagenesis, the mutant shows decreased activity compared to the wild-type enzyme
-
A23T/F212S
the mutant shows 40.65% activity with catechol compared to the wild type enzyme
F191I/C268R/Y272H/V280A/Y293D
the mutant shows 38.29% activity with catechol compared to the wild type enzyme
H24R/F168S/Q275R
the mutant shows 19.66% activity with catechol compared to the wild type enzyme
M65T
the mutant show increased activity compared to the wild type enzyme
R296Q
the mutant shows 128.47% activity with catechol compared to the wild type enzyme. The mutation also improves the activity of the enzyme against 4-chlorocatechol (582.04% activity compared to the wild type enzyme)
A177V
-
increased sensitivity to 3-methylcatechol
A229C
virtually mutated enzyme
H250G
-
reduced twofold relative kcat value for 3-methylcatechol
H294C
virtually mutated enzyme
L226S
-
increased activity with 4-ethylcatechol, reduced binding of the ferrous ion cofactor, modified the catalytic activity toward 3-methylcatechol
T196I
-
increased sensitivity to 3-methylcatechol
T253I
-
increased activity with 4-ethylcatechol, reduced binding of the ferrous ion cofactor
A177V
-
increased sensitivity to 3-methylcatechol
-
H250G
-
reduced twofold relative kcat value for 3-methylcatechol
-
L226S
-
increased activity with 4-ethylcatechol, reduced binding of the ferrous ion cofactor, modified the catalytic activity toward 3-methylcatechol
-
T196I
-
increased sensitivity to 3-methylcatechol
-
T253I
-
increased activity with 4-ethylcatechol, reduced binding of the ferrous ion cofactor
-
A177V
-
increased sensitivity to 3-methylcatechol
-
L226S
-
increased activity with 4-ethylcatechol, reduced binding of the ferrous ion cofactor, modified the catalytic activity toward 3-methylcatechol
-
T196I
-
increased sensitivity to 3-methylcatechol
-
T253I
-
increased activity with 4-ethylcatechol, reduced binding of the ferrous ion cofactor
-
A229C
-
forming disulfide bonds, more alkalescency stable, improvement of thermostability, widened optimum temperature from 40-50°C
H294C
-
forming disulfide bonds, more alkalescency stable, improvement of thermostability, widened optimum temperature from 40-50°C
A229C
-
forming disulfide bonds, more alkalescency stable, improvement of thermostability, widened optimum temperature from 40-50°C
-
H294C
-
forming disulfide bonds, more alkalescency stable, improvement of thermostability, widened optimum temperature from 40-50°C
-
H199N
strongly reduced activity, significant changes in pH profile
H246A
strongly reduced activity, significant changes in pH profile
H246N
strongly reduced activity, significant changes in pH profile
T249A
-
reduced kcat and increased Km-values
T249G
-
reduced kcat and increased Km-values
T249S
-
reduced kcat and increased Km-values
Y255F
strongly reduced activity
H199N
-
strongly reduced activity, significant changes in pH profile
-
H246A
-
strongly reduced activity, significant changes in pH profile
-
H246N
-
strongly reduced activity, significant changes in pH profile
-
T249A
-
reduced kcat and increased Km-values
-
T249G
-
reduced kcat and increased Km-values
-
T249S
-
reduced kcat and increased Km-values
-
Y255F
-
strongly reduced activity
-
E270A
mutant enzyme is almost completely inactivated
H157A
mutant enzyme is almost completely inactivated
H202A
mutant enzyme is almost completely inactivated
H219A
mutant enzyme is almost completely inactivated
T254A
catalytic activity of the mutant enzyme hardly changes. It shows a broader substrate specificity than the wild-type enzyme. The activities of the mutant enzyme on 3-methylcatechol and 4-methylcatechol increases 3.7fold and 2.5folds, respectively, as compared to catechol
R296Q
-
random mutagenesis, the mutant shows decreased activity compared to the wild-type enzyme
R296Q
-
random mutagenesis, the mutant shows significant tolerance to acidic pH with an optimum at pH 5.0, as well as a over 1.5fold increased activity, altered substrate inhibition, and 2.5fold lower KM compared to the wild-type enzyme
R296Q
-
random mutagenesis, the mutant shows decreased activity compared to the wild-type enzyme
-
R296Q
-
random mutagenesis, the mutant shows significant tolerance to acidic pH with an optimum at pH 5.0, as well as a over 1.5fold increased activity, altered substrate inhibition, and 2.5fold lower KM compared to the wild-type enzyme
-
environmental protection
-
integration and expression of catechol-2,3-dioxygenase gene in pyrene degrading bacteria genome. The engineering bacteria taking polycyclic aromatic hydrocarbons degrading dominant strain as acceptor can effectively remove polycyclic aromatic hydrocarbonss from petroleum-contaminated soil
environmental protection
-
integration and expression of catechol-2,3-dioxygenase gene in pyrene degrading bacteria genome. The engineering bacteria taking polycyclic aromatic hydrocarbons degrading dominant strain as acceptor can effectively remove polycyclic aromatic hydrocarbonss from petroleum-contaminated soil
-
additional information
construction of hybrid enzymes by exchange of parts of protein domain 2 with that of enzyme from Pseudomonas putida strain GJ31. Results indicate that the 43 C-terminal amino acids probably determine the substrate specificities
additional information
construction of hybrid enzymes by exchange of parts of protein domain 2 with that of enzyme from Pseudomonas putida strain GJ31. Results indicate that the 43 C-terminal amino acids probably determine the substrate specificities
additional information
-
construction of hybrid enzymes by exchange of parts of protein domain 2 with that of enzyme from Pseudomonas putida strain GJ31. Results indicate that the 43 C-terminal amino acids probably determine the substrate specificities
additional information
construction of hybrid enzymes by exchange of parts of protein domain 2 with that of enzyme from Pseudomonas putida strain UCC2. Results indicate that the 43 C-terminal amino acids probably determine the substrate specificities
additional information
construction of hybrid enzymes by exchange of parts of protein domain 2 with that of enzyme from Pseudomonas putida strain UCC2. Results indicate that the 43 C-terminal amino acids probably determine the substrate specificities
additional information
-
construction of hybrid enzymes by exchange of parts of protein domain 2 with that of enzyme from Pseudomonas putida strain UCC2. Results indicate that the 43 C-terminal amino acids probably determine the substrate specificities
additional information
used for identifying potential sites of introducing disulfide bond of C23O from Pseudomonas sp.
additional information
-
construction of hybrid enzymes by exchange of parts of protein domain 2 with that of enzyme from Pseudomonas putida strain GJ31. Results indicate that the 43 C-terminal amino acids probably determine the substrate specificities
-
additional information
-
construction of different hybrid enzymes containing different parts of type I.2.A and I.2.B enzyme, only one of the constructed enzymes is found to be active
additional information
-
construction of different hybrid enzymes containing different parts of type I.2.A and I.2.B enzyme, only one of the constructed enzymes is found to be active
additional information
-
immobilization of catechol 2,3-dioxygenase from KB2 strain using calcium alginate, the iimmobilized enzyme shows relatively higher activity against 3-methylcatechol, 4-methylcatechol, 4,5-dichlorocatechol, 3,5-dichlorocatechol, hydroquinone and tetrachlorohydroquinone than soluble enzyme, immobilization protects the enzyme from the inhibition and enhanced its resistance to inactivation during catalysis
additional information
-
immobilization of catechol 2,3-dioxygenase from KB2 strain using calcium alginate, the iimmobilized enzyme shows relatively higher activity against 3-methylcatechol, 4-methylcatechol, 4,5-dichlorocatechol, 3,5-dichlorocatechol, hydroquinone and tetrachlorohydroquinone than soluble enzyme, immobilization protects the enzyme from the inhibition and enhanced its resistance to inactivation during catalysis
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.