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Literature summary extracted from
- Degradation potential of protocatechuate 3,4-dioxygenase from crude extract of Stenotrophomonas maltophilia strain KB2 immobilized in calcium alginate hydrogels and on glyoxyl agarose (2014), BioMed Res. Int., 2014, 138768 .
Activating Compound
| EC Number | Activating Compound | Comment | Organism | Structure |
|---|---|---|---|---|
| 1.13.11.3 | butanol | activates the free enzyme and enzyme immobilized on calcium alginate by 20% and 9% at 0.3 mM, respectively | Stenotrophomonas maltophilia |  |
| 1.13.11.3 | ethanol | activates the free enzyme and enzyme immobilized on calcium alginate by 42% and 56% at 0.3 mM, respectively | Stenotrophomonas maltophilia | |
| 1.13.11.3 | additional information | propanol has no effect on the activity of enzyme immobilized on calcium alginate at 0.3 mM | Stenotrophomonas maltophilia | |
| 1.13.11.3 | Propanol | activates the free enzyme by 30% at 0.3 mM | Stenotrophomonas maltophilia | |
Protein Variants
| EC Number | Protein Variants | Comment | Organism |
|---|---|---|---|
| 1.13.11.3 | additional information | immobilization of the enzyme in alginate gel shifts its optimum pH towards high-alkaline pH while immobilization of the enzyme on glyoxyl agarose does not influence pH-profile of the enzyme. Protocatechuate 3,4-dioygenase immobilized in calcium alginate shows increased activity towards 2,5-dihydroxybenzoate, caffeic acid, 2,3-dihydroxybenzoate, and 3,5-dihydroxybenzoate. Slightly lower activity of the enzyme is observed after its immobilization on glyoxyl agarose. Entrapment of the enzyme in alginate gel protects it against chelators and aliphatic alcohols while its immobilization on glyoxyl agarose enhanced enzyme resistance to inactivation by metal ions. Immobilization of dioxygenase in calcium alginate or on glyoxyl agarose results in decrease in the optimum temperature by 5°C and10°C, respectively. Activity of the enzyme immobilized on calcium alginate increases particularly towards 2,5-dihydroxybenzoate, caffeic acid, 2,3-dihydroxybenzoate, and 3,5-dihydroxybenzoate | Stenotrophomonas maltophilia |
Inhibitors
| EC Number | Inhibitors | Comment | Organism | Structure |
|---|---|---|---|---|
| 1.13.11.3 | 2,2'-dipyridyl | activates the enzyme immobilized on calcium alginate, but inhibits the free enzyme and the enzyme immobilized on glyoxyl agarose, at 0.3 mM | Stenotrophomonas maltophilia | |
| 1.13.11.3 | Al3+ | slight inhibition of the glyoxyl agarose-immobilized enzyme | Stenotrophomonas maltophilia | |
| 1.13.11.3 | butanol | inhibits the activity of the enzyme immobilized on glyoxyl agarose by 23.5% at 0.3 mM | Stenotrophomonas maltophilia | |
| 1.13.11.3 | Cd2+ | - |
Stenotrophomonas maltophilia | |
| 1.13.11.3 | Co2+ | - |
Stenotrophomonas maltophilia | |
| 1.13.11.3 | Cu2+ | - |
Stenotrophomonas maltophilia | |
| 1.13.11.3 | EDTA | activates the enzyme immobilized on calcium alginate, but inhibits the free enzyme and the enzyme immobilized on glyoxyl agarose, at 0.3 mM | Stenotrophomonas maltophilia | |
| 1.13.11.3 | ethanol | inhibits the activity of the enzyme immobilized on glyoxyl agarose by 50% at 0.3 mM | Stenotrophomonas maltophilia | |
| 1.13.11.3 | Fe3+ | inhibits the free enzyme and the enzyme immobilized on glyoxyl agarose | Stenotrophomonas maltophilia | |
| 1.13.11.3 | methanol | inhibits the activity of the enzyme immobilized on calcium alginate by 28% at 0.3 mM | Stenotrophomonas maltophilia | |
| 1.13.11.3 | Mn2+ | - |
Stenotrophomonas maltophilia | |
| 1.13.11.3 | additional information | protective effect of immobilization on calcium alginate on enzyme activity is observed in the presence of Cd2+, Al3+, and Fe3+ while in the presence of Mn2+ and Zn2+ the inhibitory effect of metals on enzyme activity increases | Stenotrophomonas maltophilia | |
| 1.13.11.3 | Ni2+ | - |
Stenotrophomonas maltophilia | |
| 1.13.11.3 | Phenanthroline | - |
Stenotrophomonas maltophilia | |
| 1.13.11.3 | Propanol | inhibits the activity of the enzyme immobilized on glyoxyl agarose by 23% at 0.3 mM | Stenotrophomonas maltophilia | |
| 1.13.11.3 | Zn2+ | - |
Stenotrophomonas maltophilia | |
Metals/Ions
| EC Number | Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|---|
| 1.13.11.3 | 2,2'-dipyridyl | activates the enzyme immobilized on calcium alginate, but inhibits the free enzyme and the enzyme immobilized on glyoxyl agarose, at 0.3 mM | Stenotrophomonas maltophilia | |
| 1.13.11.3 | Al3+ | activates the free enzyme and enzyme immobilized on calcium alginate | Stenotrophomonas maltophilia | |
| 1.13.11.3 | EDTA | activates the enzyme immobilized on calcium alginate, but inhibits the free enzyme and the enzyme immobilized on glyoxyl agarose, at 0.3 mM | Stenotrophomonas maltophilia | |
| 1.13.11.3 | Fe3+ | activates the enzyme immobilized on calcium alginate | Stenotrophomonas maltophilia | |
| 1.13.11.3 | additional information | protective effect of immobilization on calcium alginate on enzyme activity is observed in the presence of Cd2+, Al3+, and Fe3+ while in the presence of Mn2+ and Zn2+ the inhibitory effect of metals on enzyme activity increases | Stenotrophomonas maltophilia |
Natural Substrates/ Products (Substrates)
| EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 1.13.11.3 | 3,4-dihydroxybenzoate + O2 | Stenotrophomonas maltophilia | - |
3-carboxy-cis,cis-muconate | - |
? | |
| 1.13.11.3 | 3,4-dihydroxybenzoate + O2 | Stenotrophomonas maltophilia KB2 | - |
3-carboxy-cis,cis-muconate | - |
? | |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 1.13.11.3 | Stenotrophomonas maltophilia | I0DHJ0 AND I0DHJ1 | alpha- und beta-subunit | - |
| 1.13.11.3 | Stenotrophomonas maltophilia KB2 | I0DHJ0 AND I0DHJ1 | alpha- und beta-subunit | - |
Storage Stability
| EC Number | Storage Stability | Organism |
|---|---|---|
| 1.13.11.3 | 4°C, stability of free and the immobilized protocatechuate 3,4-dioxygenase in phosphate buffer containing 50 mM, pH 7.0, for free enzyme or immobilized enzyme in calcium alginate, and 40mM, pH 8.0, for enzyme immobilized on glyoxyl agarose, immobilized enzyme shows 9.93% of its initial activity after 28 days of storage, while the free enzyme becomes inactive | Stenotrophomonas maltophilia |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 1.13.11.3 | 2,3-dihydroxybenzoate + O2 | 23.6% of the activity with protocatechuate for the free enzyme, 149.3% for the calcium alginate-immobilized enzyme, and 119.8% for the glyoxyl agarose-immobilized enzyme | Stenotrophomonas maltophilia | ? | - |
? | |
| 1.13.11.3 | 2,4-dihydroxybenzoate + O2 | 43.5% of the activity with protocatechuate for the free enzyme, 96.5% for the calcium alginate-immobilized enzyme, and 65.6% for the glyoxyl agarose-immobilized enzyme | Stenotrophomonas maltophilia | ? | - |
? | |
| 1.13.11.3 | 2,5-dihydroxybenzoate + O2 | 33.5% of the activity with protocatechuate for the free enzyme, 158.6% for the calcium alginate-immobilized enzyme, and 72.1% for the glyoxyl agarose-immobilized enzyme | Stenotrophomonas maltophilia | ? | - |
? | |
| 1.13.11.3 | 2,6-dihydroxybenzoate + O2 | 30.5% of the activity with protocatechuate for the free enzyme, 90.4% for the calcium alginate-immobilized enzyme, and 36.2% for the glyoxyl agarose-immobilized enzyme | Stenotrophomonas maltophilia | ? | - |
? | |
| 1.13.11.3 | 3,4-dihydroxybenzoate + O2 | - |
Stenotrophomonas maltophilia | 3-carboxy-cis,cis-muconate | - |
? | |
| 1.13.11.3 | 3,4-dihydroxybenzoate + O2 | best substrate | Stenotrophomonas maltophilia | 3-carboxy-cis,cis-muconate | - |
? | |
| 1.13.11.3 | 3,4-dihydroxybenzoate + O2 | - |
Stenotrophomonas maltophilia KB2 | 3-carboxy-cis,cis-muconate | - |
? | |
| 1.13.11.3 | 3,4-dihydroxybenzoate + O2 | best substrate | Stenotrophomonas maltophilia KB2 | 3-carboxy-cis,cis-muconate | - |
? | |
| 1.13.11.3 | 3,4-dihydroxyhydrocinnamic acid + O2 | 29.5% of the activity with protocatechuate for the free enzyme, 95.0% for the calcium alginate-immobilized enzyme, and 41.1% for the glyoxyl agarose-immobilized enzyme | Stenotrophomonas maltophilia | ? | - |
? | |
| 1.13.11.3 | 3,4-dihydroxyhydrocinnamic acid + O2 | 29.5% of the activity with protocatechuate for the free enzyme, 95.0% for the calcium alginate-immobilized enzyme, and 41.1% for the glyoxyl agarose-immobilized enzyme | Stenotrophomonas maltophilia KB2 | ? | - |
? | |
| 1.13.11.3 | 3,5-dihydroxybenzoate + O2 | 44.3% of the activity with protocatechuate for the free enzyme, 113.3% for the calcium alginate-immobilized enzyme, and 42.9% for the glyoxyl agarose-immobilized enzyme | Stenotrophomonas maltophilia | ? | - |
? | |
| 1.13.11.3 | caffeic acid + O2 | 34.2% of the activity with protocatechuate for the free enzyme, 150% for the calcium alginate-immobilized enzyme, and 97% for the glyoxyl agarose-immobilized enzyme | Stenotrophomonas maltophilia | ? | - |
? | |
| 1.13.11.3 | caffeic acid + O2 | 34.2% of the activity with protocatechuate for the free enzyme, 150% for the calcium alginate-immobilized enzyme, and 97% for the glyoxyl agarose-immobilized enzyme | Stenotrophomonas maltophilia KB2 | ? | - |
? | |
| 1.13.11.3 | additional information | protocatechuate 3,4-dioxygenase from KB2 strain shows activity against various dihydroxybenzoic acids, but highest activity with primary substrate protocatechuate. Activity of the enzyme immobilized on calcium alginate increases particularly towards 2,5-dihydroxybenzoate, caffeic acid, 2,3-dihydroxybenzoate, and 3,5-dihydroxybenzoate, overview | Stenotrophomonas maltophilia | ? | - |
? | |
| 1.13.11.3 | additional information | protocatechuate 3,4-dioxygenase from KB2 strain shows activity against various dihydroxybenzoic acids, but highest activity with primary substrate protocatechuate. Activity of the enzyme immobilized on calcium alginate increases particularly towards 2,5-dihydroxybenzoate, caffeic acid, 2,3-dihydroxybenzoate, and 3,5-dihydroxybenzoate, overview | Stenotrophomonas maltophilia KB2 | ? | - |
? | |
Temperature Optimum [°C]
| EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 1.13.11.3 | 35 | - |
glyoxyl agarose-immobilized enzyme | Stenotrophomonas maltophilia |
| 1.13.11.3 | 40 | - |
calcium alginate-immobilized enzyme | Stenotrophomonas maltophilia |
| 1.13.11.3 | 45 | 50 | free enzyme | Stenotrophomonas maltophilia |
Temperature Range [°C]
| EC Number | Temperature Minimum [°C] | Temperature Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 1.13.11.3 | 4 | 60 | free and immobilized enzyme, profile overview | Stenotrophomonas maltophilia |
pH Optimum
| EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|---|
| 1.13.11.3 | 9.2 | - |
free enzyme and glyoxyl agarose-immobilized enzyme | Stenotrophomonas maltophilia |
| 1.13.11.3 | 14 | - |
calcium alginate-immobilized enzyme | Stenotrophomonas maltophilia |
pH Range
| EC Number | pH Minimum | pH Maximum | Comment | Organism |
|---|---|---|---|---|
| 1.13.11.3 | 2.2 | 13 | glyoxyl agarose-immobilized enzyme, profile overview | Stenotrophomonas maltophilia |
| 1.13.11.3 | 4 | 14 | calcium alginate-immobilized enzyme, profile overview | Stenotrophomonas maltophilia |
| 1.13.11.3 | 6.5 | 11.5 | free enzyme, profile overview | Stenotrophomonas maltophilia |
Expression
| EC Number | Organism | Comment | Expression |
|---|---|---|---|
| 1.13.11.3 | Stenotrophomonas maltophilia | 4-hydroxybenzoate induces the protocatechuate 3,4-dioxygenase | up |
General Information
| EC Number | General Information | Comment | Organism |
|---|---|---|---|
| 1.13.11.3 | additional information | enzyme immobilized on calcium alginate gel binds to the carrier by electrostatic interaction while glyoxyl agarose is linked with the enzyme by covalent bonds. Since positively charged amino acids are localized at the entrance of crevasse, the electrostatic interaction plays the key role in modulation of enzyme activity. Significant increase of enzyme activity after its immobilization in calcium alginate is probably caused by strong electrostatic interactions between positively charged amino acid residues of the enzyme and negatively charged groups of alginate. High activity of immobilized protocatechuate 3,4-dioxygenase towards 2,3-dihydroxybenzoate, 2,5-dihydroxybenzoate, and 3,5-dihydroxybenzoate can be connected with modification of its catalytic mechanism as only 2,3-dihydroxybenzoate is in configuration typical for protocatechuate 3,4-dioxygenase's substrate | Stenotrophomonas maltophilia |
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