IntEnz

EC 1.14.14.9 - 4-hydroxyphenylacetate 3-monooxygenase

IntEnz Enzyme Nomenclature
EC 1.14.14.9

Names

Reaction

• 4-hydroxyphenylacetate + FADH2 + O2 = 3,4-dihydroxyphenylacetate + FAD + H2O

Cofactor

• FAD

Comments:

The enzyme from Escherichia coli attacks a broad spectrum of phenolic compounds. The enzyme uses FADH2 as a substrate rather than a cofactor [4]. FADH2 is provided by EC 1.5.1.36, flavin reductase (NADH) [5,6].

Links to other databases

References

1. Adachi, K., Takeda, Y., Senoh, S. and Kita, H.
   Metabolism of p-hydroxyphenylacetic acid in Pseudomonas ovalis.
   Biochim. Biophys. Acta 93 : 483-493 (1964).
2. Prieto, M. A., Perez-Aranda, A., Garcia, J. L.
   Characterization of an Escherichia coli aromatic hydroxylase with a broad substrate range.
   J. Bacteriol. 175 : 2162-2167 (1993). [PMID: 8458860]
3. Prieto, M. A., Garcia, J. L.
   Molecular characterization of 4-hydroxyphenylacetate 3-hydroxylase of Escherichia coli. A two-protein component enzyme.
   J. Biol. Chem. 269 : 22823-22829 (1994). [PMID: 8077235]
4. Xun, L., Sandvik, E. R.
   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]
5. Galan, B., Diaz, E., Prieto, M. A., Garcia, J. L.
   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]
6. Louie, T. M., Xie, X. S., Xun, L.
   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 1.14.14.9 created 1972 as EC 1.14.13.3, transferred 2011 to EC 1.14.14.9]