The Enzyme Database

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Accepted name: 4-hydroxyphenylacetate 3-monooxygenase
Reaction: 4-hydroxyphenylacetate + FADH2 + O2 = 3,4-dihydroxyphenylacetate + FAD + H2O
Other name(s): p-hydroxyphenylacetate 3-hydroxylase; 4-hydroxyphenylacetic acid-3-hydroxylase; p-hydroxyphenylacetate hydroxylase (FAD); 4 HPA 3-hydroxylase; p-hydroxyphenylacetate 3-hydroxylase (FAD); HpaB
Systematic name: 4-hydroxyphenylacetate,FADH2:oxygen oxidoreductase (3-hydroxylating)
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, flavin reductase (NADH) [5,6].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, UM-BBD, CAS registry number: 37256-71-6
1.  Adachi, K., Takeda, Y., Senoh, S. and Kita, H. Metabolism of p-hydroxyphenylacetic acid in Pseudomonas ovalis. Biochim. Biophys. Acta 93 (1964) 483–493. [PMID: 14263147]
2.  Prieto, M.A., Perez-Aranda, A. and Garcia, J.L. Characterization of an Escherichia coli aromatic hydroxylase with a broad substrate range. J. Bacteriol. 175 (1993) 2162–2167. [PMID: 8458860]
3.  Prieto, M.A. and Garcia, J.L. Molecular characterization of 4-hydroxyphenylacetate 3-hydroxylase of Escherichia coli. A two-protein component enzyme. J. Biol. Chem. 269 (1994) 22823–22829. [PMID: 8077235]
4.  Xun, L. and 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 (2000) 481–486. [PMID: 10653707]
5.  Galan, B., Diaz, E., Prieto, M.A. and 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 (2000) 627–636. [PMID: 10633095]
6.  Louie, T.M., Xie, X.S. and Xun, L. Coordinated production and utilization of FADH2 by NAD(P)H-flavin oxidoreductase and 4-hydroxyphenylacetate 3-monooxygenase. Biochemistry 42 (2003) 7509–7517. [PMID: 12809507]
[EC created 1972 as EC, transferred 2011 to EC]

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