EC 1.14 - Acting on paired donors, with incorporation or reduction of molecular oxygen. The oxygen incorporated need not be derived from O2
EC 220.127.116.11 - 4-hydroxyphenylacetate 3-monooxygenase
IntEnz Enzyme Nomenclature
p-hydroxyphenylacetate hydroxylase (FAD)
p-hydroxyphenylacetate 3-hydroxylase (FAD)
- 4-hydroxyphenylacetate + FADH2 + O2 = 3,4-dihydroxyphenylacetate + FAD + H2O
The enzyme from Escherichia coli attacks a broad spectrum of phenolic compounds. The enzyme uses FADH2 as a substrate rather than a cofactor . FADH2 is provided by EC 18.104.22.168, flavin reductase (NADH) [5,6].
Links to other databases
Metabolism of p-hydroxyphenylacetic acid in Pseudomonas ovalis.Biochim. Biophys. Acta 93 : 483-493 (1964).
Characterization of an Escherichia coli aromatic hydroxylase with a broad substrate range.J. Bacteriol. 175 : 2162-2167 (1993). [PMID: 8458860]
Molecular characterization of 4-hydroxyphenylacetate 3-hydroxylase of Escherichia coli. A two-protein component enzyme.J. Biol. Chem. 269 : 22823-22829 (1994). [PMID: 8077235]
Characterization of 4-hydroxyphenylacetate 3-hydroxylase (HpaB) of Escherichia coli as a reduced flavin adenine dinucleotide-utilizing monooxygenase.Appl. Environ. Microbiol. 66 : 481-486 (2000). [PMID: 10653707]
Functional analysis of the small component of the 4-hydroxyphenylacetate 3-monooxygenase of Escherichia coli W: a prototype of a new flavin:NAD(P)H reductase subfamily.J. Bacteriol. 182 : 627-636 (2000). [PMID: 10633095]
Coordinated production and utilization of FADH2 by NAD(P)H-flavin oxidoreductase and 4-hydroxyphenylacetate 3-monooxygenase.Biochemistry 42 : 7509-7517 (2003). [PMID: 12809507]
[EC 22.214.171.124 created 1972 as EC 126.96.36.199, transferred 2011 to EC 188.8.131.52]