This view shows enzymes only for those organisms listed below, in the list of taxa known to possess the pathway. If an enzyme name is shown in bold, there is experimental evidence for this enzymatic activity.
Synonyms: 4-HPA degradation, homoprotocatechuate degradation
|Superclasses:||Degradation/Utilization/Assimilation → Aromatic Compounds Degradation|
Some taxa known to possess this pathway include : Acinetobacter , Escherichia coli B , Escherichia coli C , Escherichia coli W , Klebsiella pneumoniae , Pseudomonas aeruginosa PAO1 , Pseudomonas putida , Pseudomonas putida U
Expected Taxonomic Range: Proteobacteria
4-hydroxyphenylacetate is a common product of aromatic amino acids fermentation (see L-tyrosine degradation II). It is also produced during the degradation of some plant materials in animal intestinal tracts [Diaz01]. Several bacteria are capable of degrading 4-hydroxyphenylacetate by first converting it into 3,4-dihydroxyphenylacetate (homoprotocatechuate), which is then degraded into TCA cycle internediates via an inducible meta-cleavage pathway that provides both a carbon source and energy to the bacteria [Sparnins74, Martin91a].
This pathway is found in several Escherichia coli strains, including Escherichia coli B, Escherichia coli C and Escherichia coli W, but not Escherichia coli K-12 [Burlingame83a]. Some, but not all, strains can also catabolize 3-hydroxyphenylacetate via the same pathway [Cooper80].
The genes encoding the enzymes of this pathway are located in Escherichia coli in two operons. The first operon includes hpaABC, and is induced by the presence of 4-hydroxyphenylacetate. The rest of the genes are located in a second operon, and are induced by 3,4-dihydroxyphenylacetate [Prieto96]. This second operon has been named either hpa or hpc operon in Escherichia coli W and Escherichia coli C, respectively.
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Roper93: Roper DI, Fawcett T, Cooper RA (1993). "The Escherichia coli C homoprotocatechuate degradative operon: hpc gene order, direction of transcription and control of expression." Mol Gen Genet 237(1-2);241-50. PMID: 8384293
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Donnelly81: Donnelly MI, Cooper RA (1981). "Two succinic semialdehyde dehydrogenases are induced when Escherichia coli K-12 Is grown on gamma-aminobutyrate." J Bacteriol 1981;145(3);1425-7. PMID: 7009588
Galan00: Galan B, Diaz E, Prieto MA, Garcia JL (2000). "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(3);627-36. PMID: 10633095
GarridoPeritier81: Garrido-Peritierra A, Cooper RA (1981). "Identification and purification of distinct isomerase and decarboxylase enzymes involved in the 4-hydroxyphenylacetate catabolic pathway of Escherichia coli." Eur J Biochem 1981;117(3);581-4. PMID: 7026235
Gibello94: Gibello A, Ferrer E, Martin M, Garrido-Pertierra A (1994). "3,4-Dihydroxyphenylacetate 2,3-dioxygenase from Klebsiella pneumoniae, a Mg(2+)-containing dioxygenase involved in aromatic catabolism." Biochem J 301 ( Pt 1);145-50. PMID: 8037662
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Langendorf10: Langendorf CG, Key TL, Fenalti G, Kan WT, Buckle AM, Caradoc-Davies T, Tuck KL, Law RH, Whisstock JC (2010). "The X-ray crystal structure of Escherichia coli succinic semialdehyde dehydrogenase; structural insights into NADP+/enzyme interactions." PLoS One 5(2);e9280. PMID: 20174634
Liebgott09: Liebgott PP, Amouric A, Comte A, Tholozan JL, Lorquin J (2009). "Hydroxytyrosol from tyrosol using hydroxyphenylacetic acid-induced bacterial cultures and evidence of the role of 4-HPA 3-hydroxylase." Res Microbiol 160(10);757-66. PMID: 19837158
Lobo02: Lobo C, Sanchez M, Garbi C, Ferrer E, Martinez-Inigo MJ, Allende JL, Martin C, Casasus L, Alonso R, Gibello A, Martin M (2002). "Immobilized native bacteria as a tool for bioremediation of soils and waters: implementation and modeling." ScientificWorldJournal 2;1361-8. PMID: 12805921
Louie03: Louie TM, Xie XS, Xun L (2003). "Coordinated production and utilization of FADH2 by NAD(P)H-flavin oxidoreductase and 4-hydroxyphenylacetate 3-monooxygenase." Biochemistry 42(24);7509-17. PMID: 12809507
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