IntEnz

EC 1.14.14.9 - 4-hydroxyphenylacetate 3-monooxygenase

IntEnz Enzyme Nomenclature
EC 1.14.14.9

Names

Reaction

• 30595 [IUBMB]
  4-hydroxyphenylacetate

  4-hydroxyphenylacetate

  Name origin: UniProt - CHECKED (C)

  CHEBI:48999

  Formula: C8H7O3
  Charge: -1

  ChEBI compound status: CHECKED (C)

  

  +

  FADH₂

  FADH2

  Name origin: UniProt - CHECKED (C)

  CHEBI:58307

  Formula: C27H33N9O15P2
  Charge: -2

  ChEBI compound status: CHECKED (C)

  

  +

  O₂

  O2

  Name origin: UniProt - CHECKED (C)

  CHEBI:15379

  Formula: O2
  Charge: 0

  ChEBI compound status: CHECKED (C)

  

  =

  3,4-dihydroxyphenylacetate

  3,4-dihydroxyphenylacetate

  Name origin: UniProt - CHECKED (C)

  CHEBI:17612

  Formula: C8H7O4
  Charge: -1

  ChEBI compound status: CHECKED (C)

  

  +

  FAD

  FAD

  Name origin: UniProt - CHECKED (C)

  CHEBI:57692

  Formula: C27H30N9O15P2
  Charge: -3

  ChEBI compound status: CHECKED (C)

  

  +

  H⁺

  H(+)

  Name origin: UniProt - CHECKED (C)

  CHEBI:15378

  Formula: H
  Charge: 1

  ChEBI compound status: CHECKED (C)

  

  +

  H₂O

  H2O

  Name origin: UniProt - CHECKED (C)

  CHEBI:15377

  Formula: H2O
  Charge: 0

  ChEBI compound status: CHECKED (C)

  

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]