Literature summary extracted from
Xun, L.; Sandvik, E.R.
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 |
|