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Literature summary for 1.14.14.9 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.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 1.14.14.9

Cloned(Commentary)

Cloned (Comment) Organism
hpaB gene is expressed in Escherichia coli BL21(DE3) Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
 strain W, ATCC 11105 derived from ATCC 9637
-

Purification (Commentary)

Purification (Comment) Organism
ammonium sulfate precipitation, ion exchange Escherichia coli

Reaction

Reaction Comment Organism Reaction ID
4-hydroxyphenylacetate + FADH2 + O2 = 3,4-dihydroxyphenylacetate + FAD + H2O new type of FADH-utilizing monooxygenase Escherichia coli
a

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
0.231
-
 for 4-hydroxyphenylacetate oxidation Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4-hydroxyphenylacetate + NADH + O2 O2 can be replaced by FADH Escherichia coli 3,4-dihydroxyphenylacetate + NAD+ + H2O
-
 ?
additional information hydroxylation of aromatic compounds Escherichia coli ?
-
 ?

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
24
-
 assay at Escherichia coli

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7
-
 assay at Escherichia coli

Cofactor

Cofactor Comment Organism Structure
FAD reduction of FAD is rate limiting Escherichia coli
FADH2 used as substrate and cofactor, enzyme binds FADH in absence of 4-hydroxyphenlyacetate and protects it from rapid autoxidation by O2 Escherichia coli