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1H-3-hydroxy-4-oxoquinaldine + H2O
?
2-hydroxy-5-methyl-6-oxohepta-2,4-dienoate + H2O
?
-
no activity with isoenzyme HODHI, 41% of the activity with 2-hydroxy-6-oxohepta-2,4-dienoate, isoenzyme HODHII
-
-
?
2-hydroxy-5-methyl-muconic semialdehyde + H2O
?
-
3% of the activity with 2-hydroxy-6-oxohepta-2,4-dienoate, isoenzyme HODHI. 5% of the activity with 2-hydroxy-6-oxohepta-2,4-dienoate, isoenzyme HODHI
-
-
?
2-hydroxy-5-methylmuconate-6-semialdehyde + H2O
?
2-hydroxy-5-methylmuconic semialdehyde + H2O
?
2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoate + H2O
?
2-hydroxy-6-oxo-7-methylocta-2,4-dienoate + H2O
?
2-hydroxy-6-oxohepta-2,4-dienoate + H2O
?
2-hydroxy-6-oxohepta-2,4-dienoate + H2O
formate + 2-oxopent-4-enoate
2-hydroxy-6-oxoocta-2,4-dienoate + H2O
?
2-hydroxy-7-methyl-6-oxoocta-2,4-dienoate + H2O
?
-
149% of the activity with 2-hydroxy-6-oxohepta-2,4-dienoate, isoenzyme HODHI, no activity with isoenzyme HODHII
-
-
?
2-hydroxymuconate 6-semialdehyde + H2O
formate + 2-oxopent-4-enoate
2-hydroxymuconate semialdehyde + H2O
formate + 2-oxopent-4-enoate
2-hydroxymuconate-6-semialdehyde + H2O
formate + 2-oxopent-4-enoate
2-hydroxymuconic semialdehyde + H2O
?
3-allylcatechol ring-fission product + H2O
?
-
meta-cleavage product resulting from the action of catechol 2,3-oxygenase upon 3-allylcatechol
-
-
?
3-ethylcatechol ring-fission product + H2O
?
-
meta-cleavage product resulting from the action of catechol 2,3-oxygenase upon 3-ethylcatechol
-
-
?
3-methylcatechol ring-fission product + H2O
?
3-propylcatechol ring-fission product + H2O
?
-
meta-cleavage product resulting from the action of catechol 2,3-oxygenase upon 3-propylcatechol
-
-
?
4-chlorocatechol ring-fission product + H2O
?
-
meta-cleavage product resulting from the action of catechol 2,3-oxygenase upon 4-chlorocatechol
-
-
?
4-ethylcatechol ring-fission product + H2O
?
-
meta-cleavage product resulting from the action of catechol 2,3-oxygenase upon 4-ethylcatechol
-
-
?
4-methylcatechol ring-fission product + H2O
?
-
meta-cleavage product resulting from the action of catechol 2,3-oxygenase upon 4-methylcatechol
-
-
?
4-propylcatechol ring-fission product + H2O
?
-
meta-cleavage product resulting from the action of catechol 2,3-oxygenase upon 4-propylcatechol
-
-
?
catechol ring-fission product + H2O
?
meta-cleavage product resulting from the action of catechol 2,3-oxygenase upon 3-allylcatechol + H2O
?
-
-
-
-
?
meta-cleavage product resulting from the action of catechol 2,3-oxygenase upon 3-ethylcatechol + H2O
?
-
-
-
-
?
meta-cleavage product resulting from the action of catechol 2,3-oxygenase upon 3-methylcatechol + H2O
?
-
-
-
-
?
meta-cleavage product resulting from the action of catechol 2,3-oxygenase upon 3-propylcatechol + H2O
?
-
-
-
-
?
meta-cleavage product resulting from the action of catechol 2,3-oxygenase upon 4-chlorocatechol + H2O
?
-
-
-
-
?
meta-cleavage product resulting from the action of catechol 2,3-oxygenase upon 4-ethylcatechol + H2O
?
-
-
-
-
?
meta-cleavage product resulting from the action of catechol 2,3-oxygenase upon 4-methylcatechol + H2O
?
-
-
-
-
?
meta-cleavage product resulting from the action of catechol 2,3-oxygenase upon 4-propylcatechol + H2O
?
-
-
-
-
?
meta-cleavage product resulting from the action of catechol 2,3-oxygenase upon catechol + H2O
?
-
-
-
-
?
additional information
?
-
1H-3-hydroxy-4-oxoquinaldine + H2O
?
-
-
-
-
?
1H-3-hydroxy-4-oxoquinaldine + H2O
?
-
-
-
-
?
2-hydroxy-5-methylmuconate-6-semialdehyde + H2O
?
-
-
-
?
2-hydroxy-5-methylmuconate-6-semialdehyde + H2O
?
prepared from 4-methylcatechol
-
-
?
2-hydroxy-5-methylmuconate-6-semialdehyde + H2O
?
-
-
-
?
2-hydroxy-5-methylmuconate-6-semialdehyde + H2O
?
prepared from 4-methylcatechol
-
-
?
2-hydroxy-5-methylmuconic semialdehyde + H2O
?
-
-
-
-
?
2-hydroxy-5-methylmuconic semialdehyde + H2O
?
-
-
-
-
?
2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoate + H2O
?
-
-
-
-
?
2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoate + H2O
?
-
slight hydrolysis
-
-
?
2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoate + H2O
?
slight hydrolytic activity
-
-
?
2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoate + H2O
?
-
-
-
-
?
2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoate + H2O
?
slight hydrolytic activity
-
-
?
2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoate + H2O
?
-
slight hydrolysis
-
-
?
2-hydroxy-6-oxo-7-methylocta-2,4-dienoate + H2O
?
-
-
-
-
?
2-hydroxy-6-oxo-7-methylocta-2,4-dienoate + H2O
?
-
-
-
?
2-hydroxy-6-oxo-7-methylocta-2,4-dienoate + H2O
?
-
-
-
-
?
2-hydroxy-6-oxo-7-methylocta-2,4-dienoate + H2O
?
-
-
-
?
2-hydroxy-6-oxo-7-methylocta-2,4-dienoate + H2O
?
-
-
-
-
?
2-hydroxy-6-oxo-7-methylocta-2,4-dienoate + H2O
?
-
-
-
-
?
2-hydroxy-6-oxo-7-methylocta-2,4-dienoate + H2O
?
-
-
-
-
?
2-hydroxy-6-oxohepta-2,4-dienoate + H2O
?
-
-
-
-
?
2-hydroxy-6-oxohepta-2,4-dienoate + H2O
?
-
-
-
-
?
2-hydroxy-6-oxohepta-2,4-dienoate + H2O
?
-
-
-
-
?
2-hydroxy-6-oxohepta-2,4-dienoate + H2O
?
-
-
-
-
?
2-hydroxy-6-oxohepta-2,4-dienoate + H2O
?
-
-
-
-
?
2-hydroxy-6-oxohepta-2,4-dienoate + H2O
?
-
-
-
-
?
2-hydroxy-6-oxohepta-2,4-dienoate + H2O
?
-
-
-
-
?
2-hydroxy-6-oxohepta-2,4-dienoate + H2O
?
-
-
-
-
?
2-hydroxy-6-oxohepta-2,4-dienoate + H2O
formate + 2-oxopent-4-enoate
-
-
-
?
2-hydroxy-6-oxohepta-2,4-dienoate + H2O
formate + 2-oxopent-4-enoate
prepared from 3-methylcatechol, best substrate
-
-
?
2-hydroxy-6-oxohepta-2,4-dienoate + H2O
formate + 2-oxopent-4-enoate
-
-
-
?
2-hydroxy-6-oxohepta-2,4-dienoate + H2O
formate + 2-oxopent-4-enoate
prepared from 3-methylcatechol, best substrate
-
-
?
2-hydroxy-6-oxoocta-2,4-dienoate + H2O
?
-
-
-
-
?
2-hydroxy-6-oxoocta-2,4-dienoate + H2O
?
-
-
-
-
?
2-hydroxy-6-oxoocta-2,4-dienoate + H2O
?
-
-
-
-
?
2-hydroxy-6-oxoocta-2,4-dienoate + H2O
?
-
-
-
-
?
2-hydroxymuconate 6-semialdehyde + H2O
formate + 2-oxopent-4-enoate
-
metabolism of 2-hydroxymuconate 6-semialdehyde through HMS hydrolase is predominant compared to metabolism by HMS dehydrogenase
-
?
2-hydroxymuconate 6-semialdehyde + H2O
formate + 2-oxopent-4-enoate
-
metabolism of 2-hydroxymuconate 6-semialdehyde through HMS hydrolase is predominant compared to metabolism by HMS dehydrogenase
-
?
2-hydroxymuconate semialdehyde + H2O
formate + 2-oxopent-4-enoate
-
-
-
?
2-hydroxymuconate semialdehyde + H2O
formate + 2-oxopent-4-enoate
-
-
-
?
2-hydroxymuconate semialdehyde + H2O
formate + 2-oxopent-4-enoate
-
31% of the activity with 2-hydroxy-6-oxohepta-2,4-dienoate, isoenzyme HODHI. 12% of the activity with 2-hydroxy-6-oxohepta-2,4-dienoate, isoenzyme HODHII
-
-
?
2-hydroxymuconate semialdehyde + H2O
formate + 2-oxopent-4-enoate
-
-
-
-
?
2-hydroxymuconate semialdehyde + H2O
formate + 2-oxopent-4-enoate
-
-
-
-
?
2-hydroxymuconate semialdehyde + H2O
formate + 2-oxopent-4-enoate
-
2-hydroxymuconate semialdehyde
-
-
?
2-hydroxymuconate semialdehyde + H2O
formate + 2-oxopent-4-enoate
-
2-hydroxymuconate semialdehyde
-
-
?
2-hydroxymuconate-6-semialdehyde + H2O
formate + 2-oxopent-4-enoate
-
-
-
?
2-hydroxymuconate-6-semialdehyde + H2O
formate + 2-oxopent-4-enoate
prepared from catechol
-
-
?
2-hydroxymuconic semialdehyde + H2O
?
-
-
-
-
?
2-hydroxymuconic semialdehyde + H2O
?
-
-
-
-
?
3-methylcatechol ring-fission product + H2O
?
-
-
-
-
?
3-methylcatechol ring-fission product + H2O
?
-
meta-cleavage product resulting from the action of catechol 2,3-oxygenase upon 3-methylcatechol
-
-
?
3-methylcatechol ring-fission product + H2O
?
-
meta-cleavage product resulting from the action of catechol 2,3-oxygenase upon 3-methylcatechol
-
-
?
catechol ring-fission product + H2O
?
-
-
-
-
?
catechol ring-fission product + H2O
?
-
meta-cleavage product resulting from the action of catechol 2,3-oxygenase upon catechol
-
-
?
catechol ring-fission product + H2O
?
-
meta-cleavage product resulting from the action of catechol 2,3-oxygenase upon catechol
-
-
?
additional information
?
-
-
the non-inducible levels of the enzyme activity appears negligible for metabolic purposes
-
-
?
additional information
?
-
-
the non-inducible levels of the enzyme activity appears negligible for metabolic purposes
-
-
?
additional information
?
-
-
enzyme of salicylate oxidation pathway
-
-
?
additional information
?
-
-
enzyme of salicylate oxidation pathway
-
-
?
additional information
?
-
-
can not hydrolyze 2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoate
-
-
?
additional information
?
-
-
can not hydrolyze 2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoate
-
-
?
additional information
?
-
-
no activity with (2E,4E)-2,4-dihydroxy-6-oxonona-2,4-dienedioic acid
-
-
-
additional information
?
-
-
no activity with (2E,4E)-2,4-dihydroxy-6-oxonona-2,4-dienedioic acid
-
-
-
additional information
?
-
-
no activity with (2E,4E)-2,4-dihydroxy-6-oxonona-2,4-dienedioic acid
-
-
-
additional information
?
-
-
enzyme is part of the pathway for the catabolism of toluene and m-xylene and p-xylene
-
-
?
additional information
?
-
-
enzyme of meta-cleavage pathway for the metabolism of benzoic acids to Krebs-cycle intermediates
-
-
?
additional information
?
-
-
enzyme of the hydrolytic branch of the meta-cleavage pathway for the catabolism of catechol and alkyl-substituted catechols
-
-
?
additional information
?
-
-
can not hydrolyze 2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoate
-
-
?
additional information
?
-
-
enzyme is part of the pathway for the catabolism of toluene and m-xylene and p-xylene
-
-
?
additional information
?
-
the enzyme shows the ability to hydrolyze all the three ring cleavage products from catechols although with different efficiency
-
-
?
additional information
?
-
-
the enzyme shows the ability to hydrolyze all the three ring cleavage products from catechols although with different efficiency
-
-
?
additional information
?
-
the enzyme shows the ability to hydrolyze all the three ring cleavage products from catechols although with different efficiency
-
-
?
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.
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0.027 - 0.044
1H-3-Hydroxy-4-oxoquinaldine
0.2315
2-hydroxy-5-methylmuconate-6-semialdehyde
recombinant enzyme, pH 7.5, 25°C
0.0074
2-hydroxy-5-methylmuconic semialdehyde
-
-
0.00045 - 0.01
2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoate
0.0008 - 0.022
2-hydroxy-6-oxo-7-methylocta-2,4-dienoate
0.0012 - 0.058
2-hydroxy-6-oxohepta-2,4-dienoate
0.0018 - 0.015
2-hydroxy-6-oxoocta-2,4-dienoate
0.232
2-hydroxymuconate-6-semialdehyde
recombinant enzyme, pH 7.5, 25°C
0.0057 - 62
2-hydroxymuconic semialdehyde
0.0075 - 0.023
3-methylcatechol ring-fission product
-
0.085 - 0.35
catechol ring-fission product
-
0.037
meta-cleavage product resulting from the action of catechol 2,3-oxygenase upon 3-allylcatechol
-
-
-
0.015
meta-cleavage product resulting from the action of catechol 2,3-oxygenase upon 3-ethylcatechol
-
-
-
0.036
meta-cleavage product resulting from the action of catechol 2,3-oxygenase upon 3-methylcatechol
-
-
-
0.005
meta-cleavage product resulting from the action of catechol 2,3-oxygenase upon 3-propylcatechol
-
-
-
0.122
meta-cleavage product resulting from the action of catechol 2,3-oxygenase upon 4-chlorocatechol
-
-
-
0.022
meta-cleavage product resulting from the action of catechol 2,3-oxygenase upon 4-ethylcatechol
-
-
-
0.01
meta-cleavage product resulting from the action of catechol 2,3-oxygenase upon 4-methylcatechol
-
-
-
0.023
meta-cleavage product resulting from the action of catechol 2,3-oxygenase upon 4-propylcatechol
-
-
-
0.03
meta-cleavage product resulting from the action of catechol 2,3-oxygenase upon catechol
-
-
-
additional information
additional information
-
0.027
1H-3-Hydroxy-4-oxoquinaldine
-
His-tagged HOD
0.0325
1H-3-Hydroxy-4-oxoquinaldine
-
mutant S101A
0.044
1H-3-Hydroxy-4-oxoquinaldine
-
mutant D233A
0.00045
2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoate
-
mutant I199V
0.00074
2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoate
-
-
0.0017
2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoate
-
mutant A129/I199V
0.0022
2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoate
-
wild-type
0.0049
2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoate
-
mutant V227I
0.0058
2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoate
-
mutant A129/V227I
0.01
2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoate
-
mutant A129V
0.0008
2-hydroxy-6-oxo-7-methylocta-2,4-dienoate
-
mutant S34G
0.0014
2-hydroxy-6-oxo-7-methylocta-2,4-dienoate
-
mutant I199V
0.0035
2-hydroxy-6-oxo-7-methylocta-2,4-dienoate
-
mutant A129/I199V
0.004
2-hydroxy-6-oxo-7-methylocta-2,4-dienoate
-
mutant F104M
0.0049
2-hydroxy-6-oxo-7-methylocta-2,4-dienoate
-
mutant V227I
0.005
2-hydroxy-6-oxo-7-methylocta-2,4-dienoate
-
mutant S34A
0.0056
2-hydroxy-6-oxo-7-methylocta-2,4-dienoate
-
mutant A129V
0.0073
2-hydroxy-6-oxo-7-methylocta-2,4-dienoate
-
150 mM phosphate, 25°C, pH 7.5
0.0073
2-hydroxy-6-oxo-7-methylocta-2,4-dienoate
150 mM phosphate buffer, at pH 7.5 and 25°C
0.0078
2-hydroxy-6-oxo-7-methylocta-2,4-dienoate
-
wild-type
0.01
2-hydroxy-6-oxo-7-methylocta-2,4-dienoate
-
mutant A129/V227I
0.022
2-hydroxy-6-oxo-7-methylocta-2,4-dienoate
-
-
0.0012
2-hydroxy-6-oxohepta-2,4-dienoate
-
isoenzyme HODHII
0.0025
2-hydroxy-6-oxohepta-2,4-dienoate
-
mutant S34A
0.0026
2-hydroxy-6-oxohepta-2,4-dienoate
-
mutant S34G
0.0028
2-hydroxy-6-oxohepta-2,4-dienoate
-
mutant V227I
0.0035
2-hydroxy-6-oxohepta-2,4-dienoate
-
mutant I199V
0.0039
2-hydroxy-6-oxohepta-2,4-dienoate
-
mutant F104M
0.0048
2-hydroxy-6-oxohepta-2,4-dienoate
-
-
0.0048
2-hydroxy-6-oxohepta-2,4-dienoate
-
mutant A129/I199V
0.0055
2-hydroxy-6-oxohepta-2,4-dienoate
-
mutant A129/V227I
0.0089
2-hydroxy-6-oxohepta-2,4-dienoate
-
wild-type
0.009
2-hydroxy-6-oxohepta-2,4-dienoate
-
-
0.0098
2-hydroxy-6-oxohepta-2,4-dienoate
-
mutant A129V
0.0164
2-hydroxy-6-oxohepta-2,4-dienoate
recombinant enzyme, pH 7.5, 25°C
0.017
2-hydroxy-6-oxohepta-2,4-dienoate
-
-
0.058
2-hydroxy-6-oxohepta-2,4-dienoate
-
isoenzyme HODHI
0.0018
2-hydroxy-6-oxoocta-2,4-dienoate
-
mutant A129V
0.002
2-hydroxy-6-oxoocta-2,4-dienoate
-
mutant V227I
0.0023
2-hydroxy-6-oxoocta-2,4-dienoate
-
mutant I199V
0.0024
2-hydroxy-6-oxoocta-2,4-dienoate
-
mutant A129/V227I
0.0027
2-hydroxy-6-oxoocta-2,4-dienoate
-
mutant F104M
0.0031
2-hydroxy-6-oxoocta-2,4-dienoate
-
mutant S34A
0.0042
2-hydroxy-6-oxoocta-2,4-dienoate
-
mutant S34G
0.005
2-hydroxy-6-oxoocta-2,4-dienoate
-
mutant A129/I199V
0.0095
2-hydroxy-6-oxoocta-2,4-dienoate
-
-
0.011
2-hydroxy-6-oxoocta-2,4-dienoate
-
wild-type
0.015
2-hydroxy-6-oxoocta-2,4-dienoate
-
-
0.0057
2-hydroxymuconic semialdehyde
-
-
0.36
2-hydroxymuconic semialdehyde
-
isoenzyme HODHI
62
2-hydroxymuconic semialdehyde
-
isoenzyme HODHII
0.0075
3-methylcatechol ring-fission product
-
mutant F108M
-
0.0076
3-methylcatechol ring-fission product
-
mutant S152A
-
0.0134
3-methylcatechol ring-fission product
-
mutant H249A
-
0.0136
3-methylcatechol ring-fission product
-
-
-
0.023
3-methylcatechol ring-fission product
-
mutant H36A
-
0.085
catechol ring-fission product
-
-
-
0.14
catechol ring-fission product
-
mutant H36A
-
0.155
catechol ring-fission product
-
mutant S152A
-
0.231
catechol ring-fission product
-
mutant H249A
-
0.35
catechol ring-fission product
-
mutant F108M
-
additional information
additional information
steady-state kinetic analysis
-
additional information
additional information
-
steady-state kinetic analysis
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
1.15
2-hydroxy-5-methylmuconate-6-semialdehyde
recombinant enzyme, pH 7.5, 25°C
16
2-hydroxy-5-methylmuconic semialdehyde
-
-
0.002 - 0.037
2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoate
0.41 - 29
2-hydroxy-6-oxo-7-methylocta-2,4-dienoate
0.3 - 81
2-hydroxy-6-oxohepta-2,4-dienoate
1.3 - 78
2-hydroxy-6-oxoocta-2,4-dienoate
18.2
2-hydroxymuconate-6-semialdehyde
recombinant enzyme, pH 7.5, 25°C
42
2-hydroxymuconic semialdehyde
-
-
0.002
2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoate
-
mutant A129/V227I
0.01
2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoate
-
mutant A129/I199V
0.01
2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoate
-
mutant A129V
0.02
2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoate
-
mutant I199V
0.02
2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoate
-
mutant V227I
0.03
2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoate
-
-
0.037
2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoate
-
wild-type
0.41
2-hydroxy-6-oxo-7-methylocta-2,4-dienoate
-
-
0.73
2-hydroxy-6-oxo-7-methylocta-2,4-dienoate
-
mutant A129/V227I
3.3
2-hydroxy-6-oxo-7-methylocta-2,4-dienoate
-
mutant A129/I199V
4.55
2-hydroxy-6-oxo-7-methylocta-2,4-dienoate
-
mutant A129/I199V
6.4
2-hydroxy-6-oxo-7-methylocta-2,4-dienoate
-
mutant F104M
6.7
2-hydroxy-6-oxo-7-methylocta-2,4-dienoate
-
mutant S34A
8.1
2-hydroxy-6-oxo-7-methylocta-2,4-dienoate
-
mutant S34G
20
2-hydroxy-6-oxo-7-methylocta-2,4-dienoate
-
mutant V227I
21
2-hydroxy-6-oxo-7-methylocta-2,4-dienoate
-
150 mM phosphate, 25°C, pH 7.5
21
2-hydroxy-6-oxo-7-methylocta-2,4-dienoate
150 mM phosphate buffer, at pH 7.5 and 25°C
23.1
2-hydroxy-6-oxo-7-methylocta-2,4-dienoate
-
wild-type
25
2-hydroxy-6-oxo-7-methylocta-2,4-dienoate
-
mutant A129V
29
2-hydroxy-6-oxo-7-methylocta-2,4-dienoate
-
mutant I199V
0.3
2-hydroxy-6-oxohepta-2,4-dienoate
-
mutant S34A
1.5
2-hydroxy-6-oxohepta-2,4-dienoate
-
mutant S34G
6.5
2-hydroxy-6-oxohepta-2,4-dienoate
-
mutant F104M
18
2-hydroxy-6-oxohepta-2,4-dienoate
-
-
19
2-hydroxy-6-oxohepta-2,4-dienoate
-
mutant A129/I199V
19.5
2-hydroxy-6-oxohepta-2,4-dienoate
-
wild-type
29
2-hydroxy-6-oxohepta-2,4-dienoate
-
mutant A129/V227I
35
2-hydroxy-6-oxohepta-2,4-dienoate
-
-
36.53
2-hydroxy-6-oxohepta-2,4-dienoate
recombinant enzyme, pH 7.5, 25°C
38
2-hydroxy-6-oxohepta-2,4-dienoate
-
mutant I199V
52
2-hydroxy-6-oxohepta-2,4-dienoate
-
mutant V227I
57
2-hydroxy-6-oxohepta-2,4-dienoate
-
-
81
2-hydroxy-6-oxohepta-2,4-dienoate
-
mutant A129V
1.3
2-hydroxy-6-oxoocta-2,4-dienoate
-
mutant S34A
8.4
2-hydroxy-6-oxoocta-2,4-dienoate
-
mutant S34G
14
2-hydroxy-6-oxoocta-2,4-dienoate
-
-
15.4
2-hydroxy-6-oxoocta-2,4-dienoate
-
mutant F104M
24
2-hydroxy-6-oxoocta-2,4-dienoate
-
mutant A129/V227I
35
2-hydroxy-6-oxoocta-2,4-dienoate
-
mutant A129/I199V
37
2-hydroxy-6-oxoocta-2,4-dienoate
-
mutant I199V
41
2-hydroxy-6-oxoocta-2,4-dienoate
-
-
42.4
2-hydroxy-6-oxoocta-2,4-dienoate
-
wild-type
75
2-hydroxy-6-oxoocta-2,4-dienoate
-
mutant A129V
78
2-hydroxy-6-oxoocta-2,4-dienoate
-
mutant V227I
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D233A
-
residual activity of 62.6%
S101A
-
residual activity of 43.1%
D233A
-
residual activity of 62.6%
-
S101A
-
residual activity of 43.1%
-
A129V/I199V/V227I
-
combination of mutations incompatible for correct folding
D224A
-
aggregates into inclusion bodies and thus can not be purified
F104M
-
mutation does not have any significant effect on enzyme characteristics
H252A
-
aggregates into inclusion bodies and thus can not be purified
I199V/V2271
-
combination of mutations incompatible for correct folding
S34A
-
lower Km and turnover rates compared to wild-type
S34G
-
lower Km and turnover rates compared to wild-type
A129V/I199V/V227I
-
combination of mutations incompatible for correct folding
-
I199V/V2271
-
combination of mutations incompatible for correct folding
-
S103A
-
the mutant has 100000fold lower activity than that of the wild type enzyme
-
D224A
-
aggregates into inclusion bodies and thus can not be purified
-
H252A
-
aggregates into inclusion bodies and thus can not be purified
-
S103A
-
has 600000fold lower activity than that of the wild-type enzyme, can be found in the soluble fraction and thus can be purified
-
C254S
-
1% of the activity of wild-type enzyme, expressed at lower levels than the other mutant enzymes
D228A
-
activity below detection
D65V
-
activity below detection. Unstable, decreases in cellular extrects after 10 min
F108M
-
18% of the activity of wild-type enzyme, enzyme displays greater thermostability than the wild-type enzyme
H249A
-
26% of the activity of wild-type enzyme, expressed at lower levels than the other mutant enzymes, severe decrease in protein stability compared to wild-type enzyme
H256A
-
activity below detection
H36A
-
15% of the activity of wild-type enzyme, severe decrease in protein stability over that of the wild-type enzyme
S107A
-
activity below detection
S107C
-
0.44% of the activity of wild-type enzyme
S152A
-
80% of the activity of wild-type enzyme, severe decrease in protein stability over that of the wild-type enzyme
A129V
-
improved catalytic efficiency than the wild type enzyme, possesses a more appropiate binding pocket for substrates with smaller C6 substituents
A129V
the kcat/Km value of the single mutant is higher than that of the wild type enzyme. The mutant shows the highest kcat/Km value for 2-hydroxy-6-oxohepta-2,4-dienoate
I199V
-
improved catalytic efficiency than the wild type enzyme
I199V
the kcat/Km value of the single mutant is higher than that of the wild type enzyme
S103A
-
has 600000fold lower activity than that of the wild-type enzyme, can be found in the soluble fraction and thus can be purified
S103A
the mutant has 100000fold lower activity than that of the wild type enzyme
V227I
-
improved catalytic efficiency than the wild type enzyme
V227I
the kcat/Km value of the single mutant is higher than that of the wild type enzyme
A129V
-
improved catalytic efficiency than the wild type enzyme, possesses a more appropiate binding pocket for substrates with smaller C6 substituents
-
A129V
-
the kcat/Km value of the single mutant is higher than that of the wild type enzyme. The mutant shows the highest kcat/Km value for 2-hydroxy-6-oxohepta-2,4-dienoate
-
I199V
-
improved catalytic efficiency than the wild type enzyme
-
I199V
-
the kcat/Km value of the single mutant is higher than that of the wild type enzyme
-
V227I
-
improved catalytic efficiency than the wild type enzyme
-
V227I
-
the kcat/Km value of the single mutant is higher than that of the wild type enzyme
-
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Sala-Trepat, J.M.; Evans, W.C.
The meta cleavage of catechol by Azotobacter species. 4-Oxalocrotonate pathway
Eur. J. Biochem.
20
400-413
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Azotobacter vinelandii, Azotobacter vinelandii 206
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Pseudomonas putida
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Identification of functional residues in a 2-hydroxymuconic semialdehyde hydrolase. A new member of the alpha/beta hydrolase-fold family of enzymes which cleaves carbon-carbon bonds
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1995
Pseudomonas putida
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Nordlund, I.; Shingler, V.
Nucleotide sequences of the meta-cleavage pathway enzymes 2-hydroxymuconic semialdehyde dehydrogenase and 2-hydroxymuconic semialdehyde hydrolase from Pseudomonas CF600
Biochim. Biophys. Acta
1049
227-230
1990
Pseudomonas sp., Pseudomonas sp. CF 600
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The purification and properties of two isofunctional 2-hydroxy-6-oxohepta-2,4-dienoate hydrolase from Alcaligenes eutrophus strain 345
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133
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1987
Cupriavidus necator
-
brenda
Duggleby, C.J.; Williams, P.A.
Purification and some properties of the 2-hydroxy-6-oxohepta-2,4-dienoate hydrolase (2-hydroxymuconic semialdehyde hydrolase) encoded by the TOL plasmid pWW0 from Pseudomonas putida mt-2
J. Gen. Microbiol.
132
717-726
1986
Pseudomonas putida, Pseudomonas putida mt-2 / ATCC 33015 / DSM 3931 / NCIB 12182 / NCIMB 12182
-
brenda
Aoki, K.; Kodama, N.; Murakami, S.; Shinke, R.
A high level of accumulation of 2-hydroxymuconic 6-semialdehyde from aniline by the transpositional mutant Y-2 of Pseudomonas species AW-2
Microbiol. Res.
152
129-135
1997
Pseudomonas sp., Pseudomonas sp. AW-2
brenda
Arenghi, F.L.; Berlanda, D.; Galli, E.; Sello, G.; Barbieri, P.
Organization and regulation of meta cleavage pathway genes for toluene and o-xylene derivative degradation in Pseudomonas stutzeri OX1
Appl. Environ. Microbiol.
67
3304-3308
2001
Pseudomonas stutzeri, Pseudomonas stutzeri OX1
brenda
Khajamohiddin, S.; Babu, P.S.; Chakka, D.; Merrick, M.; Bhaduri, A.; Sowdhamini, R.; Siddavattam, D.
A novel meta-cleavage product hydrolase from Flavobacterium sp. ATCC27551
Biochem. Biophys. Res. Commun.
351
675-681
2006
Flavobacterium sp., Flavobacterium sp. ATCC 27551
brenda
Jun, S.; Fushinobu, S.; Nojiri, H.; Omori, T.; Shoun, H.; Wakagi, T.
Improving the catalytic efficiency of a meta-cleavage product hydrolase (CumD) from Pseudomonas fluorescens IP01
Biochim. Biophys. Acta
1764
1159-1166
2006
Pseudomonas putida, Pseudomonas fluorescens, Pseudomonas fluorescens IP01
brenda
Betz, A.; Facey, S.J.; Hauer, B.; Tshisuaka, B.; Lingens, F.
Molecular cloning, sequencing, expression, and site-directed mutagenesis of the 1H-3-hydroxy-4-oxoquinaldine 2,4-dioxygenase gene from Arthrobacter spec. Rue61a
J. Basic Microbiol.
40
7-23
2000
Arthrobacter sp., Arthrobacter sp. Rue61a
brenda
Saku, T.; Fushinobu, S.; Jun, J.S.; Ikeda, N.; Nojiri, H.; Yamane, H.; Omori, T.; Wakagi, T.
Purification, characterization, and steady-state kinetics of a meta-cleavage compound hydrolase from Pseudomonas fluorescens IPO1
J. Biosci. Bioeng.
93
568-574
2002
Pseudomonas fluorescens, Pseudomonas fluorescens IPO1
brenda
Bertini, L.; Cafaro, V.; Proietti, S.; Caporale, C.; Capasso, P.; Caruso, C.; Di Donato, A.
Deepening TOL and TOU catabolic pathways of Pseudomonas sp. OX1: cloning, sequencing and characterization of the lower pathways
Biochimie
95
241-250
2013
Pseudomonas sp. (G3KFX4), Pseudomonas sp., Pseudomonas sp. OX1 (G3KFX4)
brenda
Jun, S.Y.; Fushinobu, S.; Nojiri, H.; Omori, T.; Shoun, H.; Wakagi, T.
Improving the catalytic efficiency of a meta-cleavage product hydrolase (CumD) from Pseudomonas fluorescens IP01
Biochim. Biophys. Acta
1764
1159-1166
2006
Pseudomonas fluorescens (P96965), Pseudomonas fluorescens IP01 (P96965), Pseudomonas fluorescens IP01
brenda
Saku, T.; Fushinobu, S.; Jun, S.; Ikeda, N.; Nojiri, H.; Yamane, H.; Omori, T.; Wakagi, T.
Purification, characterization, and steady-state kinetics of a meta-cleavage compound hydrolase from Pseudomonas fluorescens IP01
J. Biosci. Bioeng.
93
568-574
2002
Pseudomonas fluorescens (P96965), Pseudomonas fluorescens IP01 (P96965), Pseudomonas fluorescens IP01
brenda
Krikstaponis, A.; Meskys, R.
Biodegradation of 7-Hydroxycoumarin in Pseudomonas mandelii 7HK4 via ipso-hydroxylation of 3-(2,4-dihydroxyphenyl)-propionic acid
Molecules
23
2613
2018
Pseudomonas mandelii, Pseudomonas mandelii 7HK4, Pseudomonas mandelii DSM 107615
brenda