3,4-dihydroxyphenylacetate 2,3-dioxygenase

In enzymology, a 3,4-dihydroxyphenylacetate 2,3-dioxygenase (EC 1.13.11.15) is an enzyme that catalyzes the chemical reaction

3,4-dihydroxyphenylacetate + O₂ 2-hydroxy-5-carboxymethylmuconate semialdehyde

Thus, the two substrates of this enzyme are 3,4-dihydroxyphenylacetate and O₂, whereas its product is 2-hydroxy-5-carboxymethylmuconate semialdehyde.

This enzyme belongs to the family of oxidoreductases, specifically those acting on single donors with O₂ as oxidant and incorporation of two atoms of oxygen into the substrate (oxygenases). The oxygen incorporated need not be derived from O₂. The systematic name of this enzyme class is 3,4-dihydroxyphenylacetate:oxygen 2,3-oxidoreductase (decyclizing). Other names in common use include 3,4-dihydroxyphenylacetic acid 2,3-dioxygenase, HPC dioxygenase, and homoprotocatechuate 2,3-dioxygenase. This enzyme participates in tyrosine metabolism. It employs one cofactor, iron.

1 Structural studies
2 References
3 External links
- 3.1 Gene Ontology (GO) codes

Structural studies

As of late 2007, 8 structures have been solved for this class of enzymes, with PDB accession codes 1F1R, 1F1U, 1F1V, 1F1X, 1Q0C, 1Q0O, 2IG9, and 2IGA.

References

IUBMB entry for 1.13.11.15
BRENDA references for 1.13.11.15 (Recommended.)
PubMed references for 1.13.11.15
PubMed Central references for 1.13.11.15
Google Scholar references for 1.13.11.15
ADACHI K, TAKEDA Y, SENOH S, KITA H (1964). "METABOLISM OF P-HYDROXYPHENYLACETIC ACID IN PSEUDOMONAS OVALIS". Biochim. Biophys. Acta. 93: 483–93. PMID 14263147.
Barbour MG, Bayly RC (1981). "Control of meta-cleavage degradation of 4-hydroxyphenylacetate in Pseudomonas putida". J. Bacteriol. 147: 844–50. PMID 6895079.
Kutty RK, Devi NA, Veeraswamy M, Ramesh S, Rao PV (1977). "Degradation of (+/-)-synephrine by Arthrobacter synephrinum Oxidation of 3,4-dihydroxyphenylacetate to 2-hydroxy-5-carboxymethyl-muconate semialdehyde". Biochem. J. 167: 163–70. PMID 588248.