View source for 1-hydroxy-2-naphthoate 1,2-dioxygenase

{{enzyme
| Name = 3,4-dihydroxyphenylacetate 2,3-dioxygenase
| EC_number = 1.13.11.15
| CAS_number = 37256-56-7
| IUBMB_EC_number = 1/13/11/15
| GO_code = 0008687
| image = 
| width = 
| caption = 
}}
In [[enzymology]], a '''3,4-dihydroxyphenylacetate 2,3-dioxygenase''' ({{EC number|1.13.11.15}}) is an [[enzyme]] that [[catalysis|catalyzes]] the [[chemical reaction]]

:3,4-dihydroxyphenylacetate + O<sub>2</sub> <math>\rightleftharpoons</math> 2-hydroxy-5-carboxymethylmuconate semialdehyde

Thus, the two [[substrate (biochemistry)|substrates]] of this enzyme are [[3,4-dihydroxyphenylacetate]] and [[oxygen|O<sub>2</sub>]], whereas its [[product (chemistry)|product]] is [[2-hydroxy-5-carboxymethylmuconate semialdehyde]].

This enzyme belongs to the family of [[oxidoreductase]]s, specifically those acting on single donors with O<sub>2</sub> as oxidant and incorporation of two atoms of oxygen into the substrate (oxygenases). The oxygen incorporated need not be derived from O<sub>2</sub>.  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 (biochemistry)|cofactor]], [[iron]].  

==Structural studies==

As of late 2007, 8 [[tertiary structure|structures]] have been solved for this class of enzymes, with [[Protein Data Bank|PDB]] accession codes {{PDB link|1F1R}}, {{PDB link|1F1U}}, {{PDB link|1F1V}}, {{PDB link|1F1X}}, {{PDB link|1Q0C}}, {{PDB link|1Q0O}}, {{PDB link|2IG9}}, and {{PDB link|2IGA}}.

==References==
{{reflist|1}}
* {{cite journal | author = Adachi K, Takeda Y, Senoh S, Kita H | date = 1964 | title = Metabolism Of P-Hydroxyphenylacetic Acid In Psuedomonas ovalis | journal = Biochim. Biophys. Acta.  | volume = 93 | pages = 483&ndash;93  | pmid = 14263147 }}
* {{cite journal | author = Barbour MG, Bayly RC | date = 1981 | title = Control of meta-cleavage degradation of 4-hydroxyphenylacetate in Pseudomonas putida | journal = J. Bacteriol.  | volume = 147 | pages = 844&ndash;50  | pmid = 6895079 | issue = 3 | pmc = 216120 }}
* {{cite journal | author = Kutty RK, Devi NA, Veeraswamy M, Ramesh S, Rao PV | date = 1977 | title = Degradation of (+/-)-synephrine by Arthrobacter synephrinum. Oxidation of 3,4-dihydroxyphenylacetate to 2-hydroxy-5-carboxymethyl-muconate semialdehyde | journal = Biochem. J.  | volume = 167 | pages = 163&ndash;70  | pmid = 588248 | issue = 1 | pmc = 1183633 }}

[[Category:EC 1.13.11]]
[[Category:Iron enzymes]]
[[Category:Enzymes of known structure]]