EC Number | Application | Comment | Organism |
---|---|---|---|
1.13.11.37 | degradation | the highly purified Ar 1,2-HQD can be used as a key enzyme in the biodegradation of aromatic hydrocarbon contaminants | Pseudarthrobacter chlorophenolicus |
EC Number | Cloned (Comment) | Organism |
---|---|---|
1.13.11.37 | expressed in Escherichia coli BL21(DE3) cells | Pseudarthrobacter chlorophenolicus |
1.13.11.37 | gene cphA-I, DNA and amino acid sequence determination and analysis, sequence comparisons, recombinant expression of His-tagged enzyme in Escherichia coli strain BL21(DE3) | Pseudarthrobacter chlorophenolicus |
EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
1.13.11.37 | hydroxyquinol + O2 | Pseudarthrobacter chlorophenolicus | - |
maleylacetate | - |
? | |
1.13.11.37 | hydroxyquinol + O2 | Pseudarthrobacter chlorophenolicus A6 / DSM 12829 | - |
maleylacetate | - |
? |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
1.13.11.37 | Pseudarthrobacter chlorophenolicus | - |
- |
- |
1.13.11.37 | Pseudarthrobacter chlorophenolicus | Q3BEM2 | - |
- |
1.13.11.37 | Pseudarthrobacter chlorophenolicus A6 / DSM 12829 | - |
- |
- |
1.13.11.37 | Pseudarthrobacter chlorophenolicus A6 / DSM 12829 | Q3BEM2 | - |
- |
EC Number | Purification (Comment) | Organism |
---|---|---|
1.13.11.37 | ammonium sulfate precipitation and Ni-NTA column chromatography | Pseudarthrobacter chlorophenolicus |
1.13.11.37 | recombinant His-tagged enzyme by nickel affinity chromatography and gel filtration by 51.7-65.2fold from Escherichia coli strain BL21(DE3) | Pseudarthrobacter chlorophenolicus |
EC Number | Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
---|---|---|---|---|
1.13.11.37 | 5.5 | - |
recombinant enzyme, crude enzyme extract, substrate 4-chlorocatechol, pH 7.5, 25°C | Pseudarthrobacter chlorophenolicus |
1.13.11.37 | 15.3 | - |
recombinant enzyme, crude enzyme extract, substrate hydroxyquinol, pH 7.5, 25°C | Pseudarthrobacter chlorophenolicus |
1.13.11.37 | 284.6 | - |
51.7fold purified enzyme, with 4-chlorocatechol as substrate, at pH 7.5 and 25°C | Pseudarthrobacter chlorophenolicus |
1.13.11.37 | 284.6 | - |
purified recombinant enzyme, substrate 4-chlorocatechol, pH 7.5, 25°C | Pseudarthrobacter chlorophenolicus |
1.13.11.37 | 391 | - |
62.5fold purified enzyme, with catechol as substrate, at pH 7.5 and 25°C | Pseudarthrobacter chlorophenolicus |
1.13.11.37 | 391 | - |
purified recombinant enzyme, substrate catechol , pH 7.5, 25°C | Pseudarthrobacter chlorophenolicus |
1.13.11.37 | 479.5 | - |
purified recombinant enzyme, substrate 3-methylcatechol, pH 7.5, 25°C | Pseudarthrobacter chlorophenolicus |
1.13.11.37 | 479.6 | - |
65.2fold purified enzyme, with 3-methylcatechol as substrate, at pH 7.5 and 25°C | Pseudarthrobacter chlorophenolicus |
1.13.11.37 | 795.6 | - |
52fold purified enzyme, with hydroxyquinol as substrate, at pH 7.5 and 25°C | Pseudarthrobacter chlorophenolicus |
1.13.11.37 | 795.6 | - |
purified recombinant enzyme, substrate hydroxyquinol, pH 7.5, 25°C | Pseudarthrobacter chlorophenolicus |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
1.13.11.37 | 3-methylcatechol + O2 | - |
Pseudarthrobacter chlorophenolicus | ? | - |
? | |
1.13.11.37 | 3-methylcatechol + O2 | - |
Pseudarthrobacter chlorophenolicus A6 / DSM 12829 | ? | - |
? | |
1.13.11.37 | 4-chlorocatechol + O2 | - |
Pseudarthrobacter chlorophenolicus | ? | - |
? | |
1.13.11.37 | 4-chlorocatechol + O2 | - |
Pseudarthrobacter chlorophenolicus A6 / DSM 12829 | ? | - |
? | |
1.13.11.37 | catechol + O2 | - |
Pseudarthrobacter chlorophenolicus | ? | - |
? | |
1.13.11.37 | catechol + O2 | - |
Pseudarthrobacter chlorophenolicus A6 / DSM 12829 | ? | - |
? | |
1.13.11.37 | catechol + O2 | - |
Pseudarthrobacter chlorophenolicus | cis,cis-muconate | - |
? | |
1.13.11.37 | catechol + O2 | - |
Pseudarthrobacter chlorophenolicus A6 / DSM 12829 | cis,cis-muconate | - |
? | |
1.13.11.37 | hydroxyquinol + O2 | - |
Pseudarthrobacter chlorophenolicus | maleylacetate | - |
? | |
1.13.11.37 | hydroxyquinol + O2 | - |
Pseudarthrobacter chlorophenolicus A6 / DSM 12829 | maleylacetate | - |
? | |
1.13.11.37 | additional information | decomposition of aromatic hydrocarbon intermediates by recombinant hydroxyquinol 1,2-dioxygenase. Substrate specificity of Ar 1,2-HQD indicates that the catalytic function of this enzyme is similar to that of the type-II catechol 1,2-dioxygenase (1,2-CTD) | Pseudarthrobacter chlorophenolicus | ? | - |
? | |
1.13.11.37 | additional information | decomposition of aromatic hydrocarbon intermediates by recombinant hydroxyquinol 1,2-dioxygenase. Substrate specificity of Ar 1,2-HQD indicates that the catalytic function of this enzyme is similar to that of the type-II catechol 1,2-dioxygenase (1,2-CTD) | Pseudarthrobacter chlorophenolicus A6 / DSM 12829 | ? | - |
? |
EC Number | Subunits | Comment | Organism |
---|---|---|---|
1.13.11.37 | ? | x * 35000-37000, SDS-PAGE | Pseudarthrobacter chlorophenolicus |
1.13.11.37 | ? | x * 35000-37000, recombinant His-tagged enzyme, SDS-PAGE, x * 33000-33500, about, His-tagged enzyme, sequence calculation | Pseudarthrobacter chlorophenolicus |
1.13.11.37 | More | enzyme Ar 1,2-HQD is an intradiol dioxygenase and it is related closely to 1,2-CTD. Its structure consisted of 5 alpha-helices in the N-terminal domain and 13 beta-sheets in the C-terminal domain. Three-dimensional enzyme structure homology modeling using structure PDB ID 1TMXA as template, overview | Pseudarthrobacter chlorophenolicus |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
1.13.11.37 | 1,2-HQD | - |
Pseudarthrobacter chlorophenolicus |
1.13.11.37 | Ar 1,2-HQD | - |
Pseudarthrobacter chlorophenolicus |
1.13.11.37 | cphA-I | - |
Pseudarthrobacter chlorophenolicus |
1.13.11.37 | HQD | - |
Pseudarthrobacter chlorophenolicus |
EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|---|
1.13.11.37 | 25 | - |
assay at | Pseudarthrobacter chlorophenolicus |
EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|---|
1.13.11.37 | 7.5 | - |
assay at | Pseudarthrobacter chlorophenolicus |
EC Number | General Information | Comment | Organism |
---|---|---|---|
1.13.11.37 | additional information | three-dimensional enzyme structure homology modeling using structure PDB ID 1TMXA as template, overview | Pseudarthrobacter chlorophenolicus |
1.13.11.37 | physiological function | decomposition of aromatic hydrocarbon intermediates by recombinant hydroxyquinol 1,2-dioxygenase. Substrate hydroxyquinol is an intermediate found in the central pathway of biodegradation of various aromatic compounds by yeast, fungi, and bacteria | Pseudarthrobacter chlorophenolicus |