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Literature summary extracted from
- Characterization of 4-hydroxyphenylacetate 3-hydroxylase (HpaB) of Escherichia coli as a reduced flavin adenine dinucleotide-utilizing monooxygenase (2000), Appl. Environ. Microbiol., 66, 481-486.
Cloned(Commentary)
| EC Number | Cloned (Comment) | Organism |
|---|---|---|
| 1.14.14.9 | hpaB gene is expressed in Escherichia coli BL21(DE3) | Escherichia coli |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 1.14.14.9 | Escherichia coli | - |
strain W, ATCC 11105 derived from ATCC 9637 | - |
Purification (Commentary)
| EC Number | Purification (Comment) | Organism |
|---|---|---|
| 1.14.14.9 | ammonium sulfate precipitation, ion exchange | Escherichia coli |
Reaction
| EC Number | Reaction | Comment | Organism | Reaction ID |
|---|---|---|---|---|
| 1.14.14.9 | 4-hydroxyphenylacetate + FADH2 + O2 = 3,4-dihydroxyphenylacetate + FAD + H2O | new type of FADH-utilizing monooxygenase | Escherichia coli |
Specific Activity [micromol/min/mg]
| EC Number | Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
|---|---|---|---|---|
| 1.14.14.9 | 0.231 | - |
for 4-hydroxyphenylacetate oxidation | Escherichia coli |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 1.14.14.9 | 4-hydroxyphenylacetate + NADH + O2 | O2 can be replaced by FADH | Escherichia coli | 3,4-dihydroxyphenylacetate + NAD+ + H2O | - |
? |  |
| 1.14.14.9 | additional information | hydroxylation of aromatic compounds | Escherichia coli | ? | - |
? | |
Temperature Optimum [°C]
| EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 1.14.14.9 | 24 | - |
assay at | Escherichia coli |
pH Optimum
| EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|---|
| 1.14.14.9 | 7 | - |
assay at | Escherichia coli |
Cofactor
| EC Number | Cofactor | Comment | Organism | Structure |
|---|---|---|---|---|
| 1.14.14.9 | FAD | reduction of FAD is rate limiting | Escherichia coli | |
| 1.14.14.9 | FADH2 | used as substrate and cofactor, enzyme binds FADH in absence of 4-hydroxyphenlyacetate and protects it from rapid autoxidation by O2 | Escherichia coli | |
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Release 2023.1 (January 2023)
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