Any feedback?
Literature summary extracted from
- Isolation and purification of Thermus thermophilus HpaB by a crystallization approach (2010), Acta Crystallogr. Sect. F, 66, 352-356.
Crystallization (Commentary)
| EC Number | Crystallization (Comment) | Organism |
|---|---|---|
| 1.14.14.9 | sitting drop vapour diffusion method, 10 mg/ml protein in 0.01 M Tris-HCl, pH 7.6, equilibration against 0.5 ml of reservoir solution, different mixtures, overview, 20°C, well shaped single crystals, X-ray diffraction structure determination and analysis at 1.82 A resolution | Thermus thermophilus |
Localization
| EC Number | Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|---|
| 1.14.14.9 | membrane | - |
Thermus thermophilus | 16020 | - |
Natural Substrates/ Products (Substrates)
| EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 1.14.14.9 | 4-hydroxyphenylacetate + NADH + H+ + O2 | Thermus thermophilus | - |
3,4-dihydroxyphenylacetate + NAD+ + H2O | - |
? |  |
| 1.14.14.9 | 4-hydroxyphenylacetate + NADH + H+ + O2 | Thermus thermophilus HB8 / ATCC 27634 / DSM 579 | - |
3,4-dihydroxyphenylacetate + NAD+ + H2O | - |
? | |
| 1.14.14.9 | 4-hydroxyphenylacetate + NADPH + H+ + O2 | Thermus thermophilus | - |
3,4-dihydroxyphenylacetate + NADP+ + H2O | - |
? | |
| 1.14.14.9 | 4-hydroxyphenylacetate + NADPH + H+ + O2 | Thermus thermophilus HB8 / ATCC 27634 / DSM 579 | - |
3,4-dihydroxyphenylacetate + NADP+ + H2O | - |
? | |
| 1.14.14.9 | additional information | Thermus thermophilus | the oxygenase HpaB is a component of the 4-hydroxyphenylacetate 3-monooxygenase enzyme that is responsible for the hydroxylation of 4-hydroxyphenylacetate. It utilizes molecular oxygen and a reduced flavin, which is provided by HpaC, the second component of the enzyme | ? | - |
? | |
| 1.14.14.9 | additional information | Thermus thermophilus HB8 / ATCC 27634 / DSM 579 | the oxygenase HpaB is a component of the 4-hydroxyphenylacetate 3-monooxygenase enzyme that is responsible for the hydroxylation of 4-hydroxyphenylacetate. It utilizes molecular oxygen and a reduced flavin, which is provided by HpaC, the second component of the enzyme | ? | - |
? | |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 1.14.14.9 | Thermus thermophilus | Q5SJP8 | - |
- |
| 1.14.14.9 | Thermus thermophilus HB8 / ATCC 27634 / DSM 579 | Q5SJP8 | - |
- |
Purification (Commentary)
| EC Number | Purification (Comment) | Organism |
|---|---|---|
| 1.14.14.9 | from membranes by solubilization with 0.1% Triton X-100, anion exchange chromatography, dialysis, exchange of detergent to dodecyl-beta-D-maltoside, another ion exchange chromatography, and gel filtration, further purification of HpaB by repetitive crystallization, method overview | Thermus thermophilus |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 1.14.14.9 | 4-hydroxyphenylacetate + NADH + H+ + O2 | - |
Thermus thermophilus | 3,4-dihydroxyphenylacetate + NAD+ + H2O | - |
? | |
| 1.14.14.9 | 4-hydroxyphenylacetate + NADH + H+ + O2 | - |
Thermus thermophilus HB8 / ATCC 27634 / DSM 579 | 3,4-dihydroxyphenylacetate + NAD+ + H2O | - |
? | |
| 1.14.14.9 | 4-hydroxyphenylacetate + NADPH + H+ + O2 | - |
Thermus thermophilus | 3,4-dihydroxyphenylacetate + NADP+ + H2O | - |
? | |
| 1.14.14.9 | 4-hydroxyphenylacetate + NADPH + H+ + O2 | - |
Thermus thermophilus HB8 / ATCC 27634 / DSM 579 | 3,4-dihydroxyphenylacetate + NADP+ + H2O | - |
? | |
| 1.14.14.9 | additional information | the oxygenase HpaB is a component of the 4-hydroxyphenylacetate 3-monooxygenase enzyme that is responsible for the hydroxylation of 4-hydroxyphenylacetate. It utilizes molecular oxygen and a reduced flavin, which is provided by HpaC, the second component of the enzyme | Thermus thermophilus | ? | - |
? | |
| 1.14.14.9 | additional information | the hydroxylation of 4-hydroxyphenylacetate by this oxygenase is performed in two stages. Firstly, the reductase component of the enzyme, the small 16.1 kDa protein HpaC, reduces flavin with the use of NAD(P)H. Subsequently, reduced flavin is transported to the oxygenase component HpaB of 4HPA 3-monooxygenase by free diffusion where, together with the oxygen molecule, it is used for the oxygenation of substrates. HpaB determines the substrate specificity | Thermus thermophilus | ? | - |
? | |
| 1.14.14.9 | additional information | the oxygenase HpaB is a component of the 4-hydroxyphenylacetate 3-monooxygenase enzyme that is responsible for the hydroxylation of 4-hydroxyphenylacetate. It utilizes molecular oxygen and a reduced flavin, which is provided by HpaC, the second component of the enzyme | Thermus thermophilus HB8 / ATCC 27634 / DSM 579 | ? | - |
? | |
| 1.14.14.9 | additional information | the hydroxylation of 4-hydroxyphenylacetate by this oxygenase is performed in two stages. Firstly, the reductase component of the enzyme, the small 16.1 kDa protein HpaC, reduces flavin with the use of NAD(P)H. Subsequently, reduced flavin is transported to the oxygenase component HpaB of 4HPA 3-monooxygenase by free diffusion where, together with the oxygen molecule, it is used for the oxygenation of substrates. HpaB determines the substrate specificity | Thermus thermophilus HB8 / ATCC 27634 / DSM 579 | ? | - |
? | |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 1.14.14.9 | 4HPA 3-monooxygenase | - |
Thermus thermophilus |
| 1.14.14.9 | HpaB | - |
Thermus thermophilus |
| 1.14.14.9 | HpaC | - |
Thermus thermophilus |
| 1.14.14.9 | More | 4-hydroxyphenylacetate 3-monooxygenase is a member of the two-component non-heme flavin-diffusible monooxygenase family | Thermus thermophilus |
Cofactor
| EC Number | Cofactor | Comment | Organism | Structure |
|---|---|---|---|---|
| 1.14.14.9 | NADH | - |
Thermus thermophilus | |
| 1.14.14.9 | NADPH | - |
Thermus thermophilus | |
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
Legal
Curated at
Member of
